A group of cytochromes with covalent thioether linkages between either or both of the vinyl side chains of protoheme and the protein. (Enzyme Nomenclature, 1992, p539)
Cytochromes of the c type that are found in eukaryotic MITOCHONDRIA. They serve as redox intermediates that accept electrons from MITOCHONDRIAL ELECTRON TRANSPORT COMPLEX III and transfer them to MITOCHONDRIAL ELECTRON TRANSPORT COMPLEX IV.
Hemeproteins whose characteristic mode of action involves transfer of reducing equivalents which are associated with a reversible change in oxidation state of the prosthetic group. Formally, this redox change involves a single-electron, reversible equilibrium between the Fe(II) and Fe(III) states of the central iron atom (From Enzyme Nomenclature, 1992, p539). The various cytochrome subclasses are organized by the type of HEME and by the wavelength range of their reduced alpha-absorption bands.
A superfamily of hundreds of closely related HEMEPROTEINS found throughout the phylogenetic spectrum, from animals, plants, fungi, to bacteria. They include numerous complex monooxygenases (MIXED FUNCTION OXYGENASES). In animals, these P-450 enzymes serve two major functions: (1) biosynthesis of steroids, fatty acids, and bile acids; (2) metabolism of endogenous and a wide variety of exogenous substrates, such as toxins and drugs (BIOTRANSFORMATION). They are classified, according to their sequence similarities rather than functions, into CYP gene families (>40% homology) and subfamilies (>59% homology). For example, enzymes from the CYP1, CYP2, and CYP3 gene families are responsible for most drug metabolism.
The 30-kDa membrane-bound c-type cytochrome protein of mitochondria that functions as an electron donor to CYTOCHROME C GROUP in the mitochondrial and bacterial RESPIRATORY CHAIN. (From Enzyme Nomenclature, 1992, p545)
A multisubunit enzyme complex containing CYTOCHROME A GROUP; CYTOCHROME A3; two copper atoms; and 13 different protein subunits. It is the terminal oxidase complex of the RESPIRATORY CHAIN and collects electrons that are transferred from the reduced CYTOCHROME C GROUP and donates them to molecular OXYGEN, which is then reduced to water. The redox reaction is simultaneously coupled to the transport of PROTONS across the inner mitochondrial membrane.
Type C cytochromes that are small (12-14 kD) single-heme proteins. They function as mobile electron carriers between membrane-bound enzymes in photosynthetic BACTERIA.
Cytochromes (electron-transporting proteins) with protoheme (HEME B) as the prosthetic group.
Cytochromes of the b group that are found bound to cytoplasmic side of ENDOPLASMIC RETICULUM. They serve as electron carrier proteins for a variety of membrane-bound OXYGENASES. They are reduced by the enzyme CYTOCHROME-B(5) REDUCTASE.
Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed)
The process by which ELECTRONS are transported from a reduced substrate to molecular OXYGEN. (From Bennington, Saunders Dictionary and Encyclopedia of Laboratory Medicine and Technology, 1984, p270)
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).
The color-furnishing portion of hemoglobin. It is found free in tissues and as the prosthetic group in many hemeproteins.
Cytochromes f are found as components of the CYTOCHROME B6F COMPLEX. They play important role in the transfer of electrons from PHOTOSYSTEM I to PHOTOSYSTEM II.
A hemeprotein which catalyzes the oxidation of ferrocytochrome c to ferricytochrome c in the presence of hydrogen peroxide. EC 1.11.1.5.
Cytochromes of the c type that are involved in the transfer of electrons from CYTOCHROME B6F COMPLEX and PHOTOSYSTEM I.
The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.
A cytochrome P-450 suptype that has specificity for a broad variety of lipophilic compounds, including STEROIDS; FATTY ACIDS; and XENOBIOTICS. This enzyme has clinical significance due to its ability to metabolize a diverse array of clinically important drugs such as CYCLOSPORINE; VERAPAMIL; and MIDAZOLAM. This enzyme also catalyzes the N-demethylation of ERYTHROMYCIN.
Cytochromes of the b group that have alpha-band absorption of 563-564 nm. They occur as subunits in MITOCHONDRIAL ELECTRON TRANSPORT COMPLEX III.
Large, hoofed mammals of the family EQUIDAE. Horses are active day and night with most of the day spent seeking and consuming food. Feeding peaks occur in the early morning and late afternoon, and there are several daily periods of rest.
An ethanol-inducible cytochrome P450 enzyme that metabolizes several precarcinogens, drugs, and solvents to reactive metabolites. Substrates include ETHANOL; INHALATION ANESTHETICS; BENZENE; ACETAMINOPHEN and other low molecular weight compounds. CYP2E1 has been used as an enzyme marker in the study of alcohol abuse.
A family of intracellular CYSTEINE ENDOPEPTIDASES that play a role in regulating INFLAMMATION and APOPTOSIS. They specifically cleave peptides at a CYSTEINE amino acid that follows an ASPARTIC ACID residue. Caspases are activated by proteolytic cleavage of a precursor form to yield large and small subunits that form the enzyme. Since the cleavage site within precursors matches the specificity of caspases, sequential activation of precursors by activated caspases can occur.
A protein complex that includes CYTOCHROME B6 and CYTOCHROME F. It is found in the THYLAKOID MEMBRANE and plays an important role in process of PHOTOSYNTHESIS by transferring electrons from PLASTOQUINONE to PLASTOCYANIN or CYTOCHROME C6. The transfer of electrons is coupled to the transport of PROTONS across the membrane.
One of the mechanisms by which CELL DEATH occurs (compare with NECROSIS and AUTOPHAGOCYTOSIS). Apoptosis is the mechanism responsible for the physiological deletion of cells and appears to be intrinsically programmed. It is characterized by distinctive morphologic changes in the nucleus and cytoplasm, chromatin cleavage at regularly spaced sites, and the endonucleolytic cleavage of genomic DNA; (DNA FRAGMENTATION); at internucleosomal sites. This mode of cell death serves as a balance to mitosis in regulating the size of animal tissues and in mediating pathologic processes associated with tumor growth.
A flavoprotein that catalyzes the reduction of heme-thiolate-dependent monooxygenases and is part of the microsomal hydroxylating system. EC 1.6.2.4.
A cytochrome P450 enzyme subtype that has specificity for relatively planar heteroaromatic small molecules, such as CAFFEINE and ACETAMINOPHEN.
The rate dynamics in chemical or physical systems.
A species of bacteria isolated from soil.
A liver microsomal cytochrome P-450 monooxygenase capable of biotransforming xenobiotics such as polycyclic hydrocarbons and halogenated aromatic hydrocarbons into carcinogenic or mutagenic compounds. They have been found in mammals and fish. This enzyme, encoded by CYP1A1 gene, can be measured by using ethoxyresorufin as a substrate for the ethoxyresorufin O-deethylase activity.
Closed vesicles of fragmented endoplasmic reticulum created when liver cells or tissue are disrupted by homogenization. They may be smooth or rough.
A subclass of heme a containing cytochromes have a reduced alpha-band absorption of 587-592 nm. They are primarily found in microorganisms.
A major cytochrome P-450 enzyme which is inducible by PHENOBARBITAL in both the LIVER and SMALL INTESTINE. It is active in the metabolism of compounds like pentoxyresorufin, TESTOSTERONE, and ANDROSTENEDIONE. This enzyme, encoded by CYP2B1 gene, also mediates the activation of CYCLOPHOSPHAMIDE and IFOSFAMIDE to MUTAGENS.
A long pro-domain caspase that contains a caspase recruitment domain in its pro-domain region. Caspase 9 is activated during cell stress by mitochondria-derived proapoptotic factors and by CARD SIGNALING ADAPTOR PROTEINS such as APOPTOTIC PROTEASE-ACTIVATING FACTOR 1. It activates APOPTOSIS by cleaving and activating EFFECTOR CASPASES.
A short pro-domain caspase that plays an effector role in APOPTOSIS. It is activated by INITIATOR CASPASES such as CASPASE 9. Isoforms of this protein exist due to multiple alternative splicing of its MESSENGER RNA.
An electron transport chain complex that catalyzes the transfer of electrons from SUCCINATE to CYTOCHROME C. It includes ELECTRON TRANSPORT COMPLEX II and ELECTRON TRANSPORT COMPLEX III.
The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)
A cytochrome P450 enzyme that catalyzes the hydroxylation of many drugs and environmental chemicals, such as DEBRISOQUINE; ADRENERGIC RECEPTOR ANTAGONISTS; and TRICYCLIC ANTIDEPRESSANTS. This enzyme is deficient in up to 10 percent of the Caucasian population.
A member of the Bcl-2 protein family and homologous partner of C-BCL-2 PROTO-ONCOGENE PROTEIN. It regulates the release of CYTOCHROME C and APOPTOSIS INDUCING FACTOR from the MITOCHONDRIA. Several isoforms of BCL2-associated X protein occur due to ALTERNATIVE SPLICING of the mRNA for this protein.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
A six carbon compound related to glucose. It is found naturally in citrus fruits and many vegetables. Ascorbic acid is an essential nutrient in human diets, and necessary to maintain connective tissue and bone. Its biologically active form, vitamin C, functions as a reducing agent and coenzyme in several metabolic pathways. Vitamin C is considered an antioxidant.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Membrane proteins encoded by the BCL-2 GENES and serving as potent inhibitors of cell death by APOPTOSIS. The proteins are found on mitochondrial, microsomal, and NUCLEAR MEMBRANE sites within many cell types. Overexpression of bcl-2 proteins, due to a translocation of the gene, is associated with follicular lymphoma.
A strain of albino rat developed at the Wistar Institute that has spread widely at other institutions. This has markedly diluted the original strain.
Abnormally low BODY TEMPERATURE that is intentionally induced in warm-blooded animals by artificial means. In humans, mild or moderate hypothermia has been used to reduce tissue damages, particularly after cardiac or spinal cord injuries and during subsequent surgeries.
A subclass of heme a containing cytochromes that have two imidazole nitrogens as axial ligands and an alpha-band absorption of 605 nm. They are found in a variety of microorganisms and in eucaryotes as a low-spin cytochrome component of MITOCHONDRIAL ELECTRON TRANSPORT COMPLEX IV.
A strain of albino rat used widely for experimental purposes because of its calmness and ease of handling. It was developed by the Sprague-Dawley Animal Company.
Used in the form of the hydrochloride as a reagent in ANALYTICAL CHEMISTRY TECHNIQUES.
A CARD signaling adaptor protein that plays a role in the mitochondria-stimulated apoptosis (APOPTOSIS, INTRINSIC PATHWAY). It binds to CYTOCHROME C in the CYTOSOL to form an APOPTOSOMAL PROTEIN COMPLEX and activates INITIATOR CASPASES such as CASPASE 9.
Inorganic salts of HYDROGEN CYANIDE containing the -CN radical. The concept also includes isocyanides. It is distinguished from NITRILES, which denotes organic compounds containing the -CN radical.
Cytochromes (electron-transporting proteins) with a tetrapyrrolic chelate of iron as a prosthetic group in which the degree of conjugation of double bonds is less than in porphyrin. (From Enzyme Nomenclature, 1992, p539)
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
A technique applicable to the wide variety of substances which exhibit paramagnetism because of the magnetic moments of unpaired electrons. The spectra are useful for detection and identification, for determination of electron structure, for study of interactions between molecules, and for measurement of nuclear spins and moments. (From McGraw-Hill Encyclopedia of Science and Technology, 7th edition) Electron nuclear double resonance (ENDOR) spectroscopy is a variant of the technique which can give enhanced resolution. Electron spin resonance analysis can now be used in vivo, including imaging applications such as MAGNETIC RESONANCE IMAGING.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
Carbon monoxide (CO). A poisonous colorless, odorless, tasteless gas. It combines with hemoglobin to form carboxyhemoglobin, which has no oxygen carrying capacity. The resultant oxygen deprivation causes headache, dizziness, decreased pulse and respiratory rates, unconsciousness, and death. (From Merck Index, 11th ed)
The mitochondria of the myocardium.
Elements of limited time intervals, contributing to particular results or situations.
The measurement of the amplitude of the components of a complex waveform throughout the frequency range of the waveform. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
Widely distributed enzymes that carry out oxidation-reduction reactions in which one atom of the oxygen molecule is incorporated into the organic substrate; the other oxygen atom is reduced and combined with hydrogen ions to form water. They are also known as monooxygenases or hydroxylases. These reactions require two substrates as reductants for each of the two oxygen atoms. There are different classes of monooxygenases depending on the type of hydrogen-providing cosubstrate (COENZYMES) required in the mixed-function oxidation.
Thin structures that encapsulate subcellular structures or ORGANELLES in EUKARYOTIC CELLS. They include a variety of membranes associated with the CELL NUCLEUS; the MITOCHONDRIA; the GOLGI APPARATUS; the ENDOPLASMIC RETICULUM; LYSOSOMES; PLASTIDS; and VACUOLES.
Spherical phototrophic bacteria found in mud and stagnant water exposed to light.
A member of the Bcl-2 protein family that reversibly binds MEMBRANES. It is a pro-apoptotic protein that is activated by caspase cleavage.
A disease that results from a congenital defect in ELECTRON TRANSPORT COMPLEX IV. Defects in ELECTRON TRANSPORT COMPLEX IV can be caused by mutations in the SURF1, SCO2, COX10, or SCO1 genes. ELECTRON TRANSPORT COMPLEX IV deficiency caused by mutation in SURF1 manifests itself as LEIGH DISEASE; that caused by mutation in SCO2 as fatal infantile cardioencephalomyopathy; that caused by mutation in COX10 as tubulopathy and leukodystrophy; and that caused by mutation in SCO1 as early-onset hepatic failure and neurologic disorder. (from Online Mendelian Inheritance in Man, http://www.ncbi.nlm.nih.gov/Omim, MIM#220110, May 17, 2001)
An antibiotic substance produced by Streptomyces species. It inhibits mitochondrial respiration and may deplete cellular levels of ATP. Antimycin A1 has been used as a fungicide, insecticide, and miticide. (From Merck Index, 12th ed)
A large group of cytochrome P-450 (heme-thiolate) monooxygenases that complex with NAD(P)H-FLAVIN OXIDOREDUCTASE in numerous mixed-function oxidations of aromatic compounds. They catalyze hydroxylation of a broad spectrum of substrates and are important in the metabolism of steroids, drugs, and toxins such as PHENOBARBITAL, carcinogens, and insecticides.
An element with atomic symbol O, atomic number 8, and atomic weight [15.99903; 15.99977]. It is the most abundant element on earth and essential for respiration.
A severe form of acute INFLAMMATION of the PANCREAS characterized by one or more areas of NECROSIS in the pancreas with varying degree of involvement of the surrounding tissues or organ systems. Massive pancreatic necrosis may lead to DIABETES MELLITUS, and malabsorption.
Inorganic salts of the hypothetical acid, H3Fe(CN)6.
Mitochondria in hepatocytes. As in all mitochondria, there are an outer membrane and an inner membrane, together creating two separate mitochondrial compartments: the internal matrix space and a much narrower intermembrane space. In the liver mitochondrion, an estimated 67% of the total mitochondrial proteins is located in the matrix. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p343-4)
A copper-containing plant protein that is a fundamental link in the electron transport chain of green plants during the photosynthetic conversion of light energy by photophosphorylation into the potential energy of chemical bonds.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.
A multisubunit enzyme complex that contains CYTOCHROME B GROUP; CYTOCHROME C1; and iron-sulfur centers. It catalyzes the oxidation of ubiquinol to UBIQUINONE, and transfers the electrons to CYTOCHROME C. In MITOCHONDRIA the redox reaction is coupled to the transport of PROTONS across the inner mitochondrial membrane.
A genus of gram-negative, anaerobic, rod-shaped bacteria capable of reducing sulfur compounds to hydrogen sulfide. Organisms are isolated from anaerobic mud of fresh and salt water, animal intestines, manure, and feces.
Stable elementary particles having the smallest known negative charge, present in all elements; also called negatrons. Positively charged electrons are called positrons. The numbers, energies and arrangement of electrons around atomic nuclei determine the chemical identities of elements. Beams of electrons are called CATHODE RAYS.
A heavy metal trace element with the atomic symbol Cu, atomic number 29, and atomic weight 63.55.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
Proteins encoded by the mitochondrial genome or proteins encoded by the nuclear genome that are imported to and resident in the MITOCHONDRIA.
Dithionite. The dithionous acid ion and its salts.
Stable elementary particles having the smallest known positive charge, found in the nuclei of all elements. The proton mass is less than that of a neutron. A proton is the nucleus of the light hydrogen atom, i.e., the hydrogen ion.
Acidic phospholipids composed of two molecules of phosphatidic acid covalently linked to a molecule of glycerol. They occur primarily in mitochondrial inner membranes and in bacterial plasma membranes. They are the main antigenic components of the Wassermann-type antigen that is used in nontreponemal SYPHILIS SERODIAGNOSIS.
The rate at which oxygen is used by a tissue; microliters of oxygen STPD used per milligram of tissue per hour; the rate at which oxygen enters the blood from alveolar gas, equal in the steady state to the consumption of oxygen by tissue metabolism throughout the body. (Stedman, 25th ed, p346)
A cytochrome form of lactate dehydrogenase found in the MITOCHONDRIA. It catalyzes the oxidation of L-lactate to PYRUVATE with transfer of electrons to CYTOCHROME C. The enzyme utilizes FMN and PROTOHEME IX as cofactors.
A flavoprotein and iron sulfur-containing oxidoreductase that catalyzes the oxidation of NADH to NAD. In eukaryotes the enzyme can be found as a component of mitochondrial electron transport complex I. Under experimental conditions the enzyme can use CYTOCHROME C GROUP as the reducing cofactor. The enzyme was formerly listed as EC 1.6.2.1.
Endogenous and exogenous compounds and that either inhibit CASPASES or prevent their activation.
Non-pathogenic ovoid to rod-shaped bacteria that are widely distributed and found in fresh water as well as marine and hypersaline habitats.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Low-molecular-weight end products, probably malondialdehyde, that are formed during the decomposition of lipid peroxidation products. These compounds react with thiobarbituric acid to form a fluorescent red adduct.
A highly poisonous compound that is an inhibitor of many metabolic processes, but has been shown to be an especially potent inhibitor of heme enzymes and hemeproteins. It is used in many industrial processes.
Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.
Cytochromes (electron-transporting proteins) in which the heme prosthetic group is heme a, i.e., the iron chelate of cytoporphyrin IX. (From Enzyme Nomenclature, 1992, p539)
The parts of a macromolecule that directly participate in its specific combination with another molecule.
A process involving chance used in therapeutic trials or other research endeavor for allocating experimental subjects, human or animal, between treatment and control groups, or among treatment groups. It may also apply to experiments on inanimate objects.
Placing of a hydroxyl group on a compound in a position where one did not exist before. (Stedman, 26th ed)
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
A barbituric acid derivative that acts as a nonselective central nervous system depressant. It potentiates GAMMA-AMINOBUTYRIC ACID action on GABA-A RECEPTORS, and modulates chloride currents through receptor channels. It also inhibits glutamate induced depolarizations.
The two lipoprotein layers in the MITOCHONDRION. The outer membrane encloses the entire mitochondrion and contains channels with TRANSPORT PROTEINS to move molecules and ions in and out of the organelle. The inner membrane folds into cristae and contains many ENZYMES important to cell METABOLISM and energy production (MITOCHONDRIAL ATP SYNTHASE).
Proteins that contain an iron-porphyrin, or heme, prosthetic group resembling that of hemoglobin. (From Lehninger, Principles of Biochemistry, 1982, p480)
NAD(P)H:(quinone acceptor) oxidoreductases. A family that includes three enzymes which are distinguished by their sensitivity to various inhibitors. EC 1.6.99.2 (NAD(P)H DEHYDROGENASE (QUINONE);) is a flavoprotein which reduces various quinones in the presence of NADH or NADPH and is inhibited by dicoumarol. EC 1.6.99.5 (NADH dehydrogenase (quinone)) requires NADH, is inhibited by AMP and 2,4-dinitrophenol but not by dicoumarol or folic acid derivatives. EC 1.6.99.6 (NADPH dehydrogenase (quinone)) requires NADPH and is inhibited by dicoumarol and folic acid derivatives but not by 2,4-dinitrophenol.
Integral membrane proteins that transport protons across a membrane. This transport can be linked to the hydrolysis of ADENOSINE TRIPHOSPHATE. What is referred to as proton pump inhibitors frequently is about POTASSIUM HYDROGEN ATPASE.
The measurement of an organ in volume, mass, or heaviness.
Solution titration in which the end point is read from the electrode-potential variations with the concentrations of potential determining ions. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
A group of oxidoreductases that act on NADH or NADPH. In general, enzymes using NADH or NADPH to reduce a substrate are classified according to the reverse reaction, in which NAD+ or NADP+ is formally regarded as an acceptor. This subclass includes only those enzymes in which some other redox carrier is the acceptor. (Enzyme Nomenclature, 1992, p100) EC 1.6.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
A widely occurring subclass of c type cytochromes which function as electron carriers in the electron transport chain in photosynthetic and denitrifying BACTERIA.
A lipid-soluble benzoquinone which is involved in ELECTRON TRANSPORT in mitochondrial preparations. The compound occurs in the majority of aerobic organisms, from bacteria to higher plants and animals.
A FLAVOPROTEIN oxidoreductase that occurs both as a soluble enzyme and a membrane-bound enzyme due to ALTERNATIVE SPLICING of a single mRNA. The soluble form is present mainly in ERYTHROCYTES and is involved in the reduction of METHEMOGLOBIN. The membrane-bound form of the enzyme is found primarily in the ENDOPLASMIC RETICULUM and outer mitochondrial membrane, where it participates in the desaturation of FATTY ACIDS; CHOLESTEROL biosynthesis and drug metabolism. A deficiency in the enzyme can result in METHEMOGLOBINEMIA.
Hypertension due to RENAL ARTERY OBSTRUCTION or compression.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
The protein components of a number of complexes, such as enzymes (APOENZYMES), ferritin (APOFERRITINS), or lipoproteins (APOLIPOPROTEINS).
Products in capsule, tablet or liquid form that provide dietary ingredients, and that are intended to be taken by mouth to increase the intake of nutrients. Dietary supplements can include macronutrients, such as proteins, carbohydrates, and fats; and/or MICRONUTRIENTS, such as VITAMINS; MINERALS; and PHYTOCHEMICALS.
A species of gram-negative, anaerobic, rod-shaped bacteria isolated from soil, animal intestines and feces, and fresh and salt water.
Naturally occurring or synthetic substances that inhibit or retard the oxidation of a substance to which it is added. They counteract the harmful and damaging effects of oxidation in animal tissues.
A complex of enzymes and PROTON PUMPS located on the inner membrane of the MITOCHONDRIA and in bacterial membranes. The protein complex provides energy in the form of an electrochemical gradient, which may be used by either MITOCHONDRIAL PROTON-TRANSLOCATING ATPASES or BACTERIAL PROTON-TRANSLOCATING ATPASES.
The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.
The mass or quantity of heaviness of an individual. It is expressed by units of pounds or kilograms.
Double-stranded DNA of MITOCHONDRIA. In eukaryotes, the mitochondrial GENOME is circular and codes for ribosomal RNAs, transfer RNAs, and about 10 proteins.
The various filaments, granules, tubules or other inclusions within mitochondria.
Naturally occurring or experimentally induced animal diseases with pathological processes sufficiently similar to those of human diseases. They are used as study models for human diseases.
The muscle tissue of the HEART. It is composed of striated, involuntary muscle cells (MYOCYTES, CARDIAC) connected to form the contractile pump to generate blood flow.
The voltage difference, normally maintained at approximately -180mV, across the INNER MITOCHONDRIAL MEMBRANE, by a net movement of positive charge across the membrane. It is a major component of the PROTON MOTIVE FORCE in MITOCHONDRIA used to drive the synthesis of ATP.
Inhibitors of SERINE ENDOPEPTIDASES and sulfhydryl group-containing enzymes. They act as alkylating agents and are known to interfere in the translation process.
Artifactual vesicles formed from the endoplasmic reticulum when cells are disrupted. They are isolated by differential centrifugation and are composed of three structural features: rough vesicles, smooth vesicles, and ribosomes. Numerous enzyme activities are associated with the microsomal fraction. (Glick, Glossary of Biochemistry and Molecular Biology, 1990; from Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)
Splitting the DNA into shorter pieces by endonucleolytic DNA CLEAVAGE at multiple sites. It includes the internucleosomal DNA fragmentation, which along with chromatin condensation, are considered to be the hallmarks of APOPTOSIS.
Analysis of the intensity of Raman scattering of monochromatic light as a function of frequency of the scattered light.
A multi-domain mitochondrial membrane protein and member of the bcl-2 Protein family. Bak protein interacts with TUMOR SUPPRESSOR PROTEIN P53 and promotes APOPTOSIS.
A member of the bcl-2 protein family that plays a role in the regulation of APOPTOSIS. Two major isoforms of the protein exist due to ALTERNATIVE SPLICING of the BCL2L1 mRNA and are referred to as Bcl-XS and Bcl-XL.
Inorganic salts of the hypothetical acid ferrocyanic acid (H4Fe(CN)6).
The study of chemical changes resulting from electrical action and electrical activity resulting from chemical changes.
Proteins found in any species of bacterium.
An increase in the rate of synthesis of an enzyme due to the presence of an inducer which acts to derepress the gene responsible for enzyme synthesis.
An antioxidant flavonoid, occurring especially in woody plants as both (+)-catechin and (-)-epicatechin (cis) forms.
Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.
Molecules or ions formed by the incomplete one-electron reduction of oxygen. These reactive oxygen intermediates include SINGLET OXYGEN; SUPEROXIDES; PEROXIDES; HYDROXYL RADICAL; and HYPOCHLOROUS ACID. They contribute to the microbicidal activity of PHAGOCYTES, regulation of signal transduction and gene expression, and the oxidative damage to NUCLEIC ACIDS; PROTEINS; and LIPIDS.
The relationship between the dose of an administered drug and the response of the organism to the drug.
A long pro-domain caspase that contains a death effector domain in its pro-domain region. Caspase 8 plays a role in APOPTOSIS by cleaving and activating EFFECTOR CASPASES. Activation of this enzyme can occur via the interaction of its N-terminal death effector domain with DEATH DOMAIN RECEPTOR SIGNALING ADAPTOR PROTEINS.
Determination of the spectra of ultraviolet absorption by specific molecules in gases or liquids, for example Cl2, SO2, NO2, CS2, ozone, mercury vapor, and various unsaturated compounds. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.
Cytochrome P-450 monooxygenases (MIXED FUNCTION OXYGENASES) that are important in steroid biosynthesis and metabolism.
The chemical alteration of an exogenous substance by or in a biological system. The alteration may inactivate the compound or it may result in the production of an active metabolite of an inactive parent compound. The alterations may be divided into METABOLIC DETOXICATION, PHASE I and METABOLIC DETOXICATION, PHASE II.
A subclass of heme a containing cytochromes with an alpha-band absorption of 605 nm. They are found in a variety of microorganisms and in eukaryotes as a high-spin cytochrome component of MITOCHONDRIAL ELECTRON TRANSPORT COMPLEX IV.
Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.
Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.
A strong oxidizing agent used in aqueous solution as a ripening agent, bleach, and topical anti-infective. It is relatively unstable and solutions deteriorate over time unless stabilized by the addition of acetanilide or similar organic materials.
Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
Chemical bond cleavage reactions resulting from absorption of radiant energy.
A flavoprotein that functions as a powerful antioxidant in the MITOCHONDRIA and promotes APOPTOSIS when released from the mitochondria. In mammalian cells AIF is released in response to pro-apoptotic protein members of the bcl-2 protein family. It translocates to the CELL NUCLEUS and binds DNA to stimulate CASPASE-independent CHROMATIN condensation.
The infusion of leaves of CAMELLIA SINENSIS (formerly Thea sinensis) as a beverage, the familiar Asian tea, which contains CATECHIN (especially epigallocatechin gallate) and CAFFEINE.
An unstable intermediate between the prostaglandin endoperoxides and thromboxane B2. The compound has a bicyclic oxaneoxetane structure. It is a potent inducer of platelet aggregation and causes vasoconstriction. It is the principal component of rabbit aorta contracting substance (RCS).
Multimeric protein complexes formed in the CYTOSOL that play a role in the activation of APOPTOSIS. They can occur when MITOCHONDRIA become damaged due to cell stress and release CYTOCHROME C. Cytosolic cytochrome C associates with APOPTOTIC PROTEASE-ACTIVATING FACTOR 1 to form the apoptosomal protein complex. The apoptosome signals apoptosis by binding to and activating specific INITIATOR CASPASES such as CASPASE 9.
A flavoprotein containing oxidoreductase that catalyzes the dehydrogenation of SUCCINATE to fumarate. In most eukaryotic organisms this enzyme is a component of mitochondrial electron transport complex II.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
A soluble cytochrome P-450 enzyme that catalyzes camphor monooxygenation in the presence of putidaredoxin, putidaredoxin reductase, and molecular oxygen. This enzyme, encoded by the CAMC gene also known as CYP101, has been crystallized from bacteria and the structure is well defined. Under anaerobic conditions, this enzyme reduces the polyhalogenated compounds bound at the camphor-binding site.
Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).
A metallic element with atomic symbol Fe, atomic number 26, and atomic weight 55.85. It is an essential constituent of HEMOGLOBINS; CYTOCHROMES; and IRON-BINDING PROTEINS. It plays a role in cellular redox reactions and in the transport of OXYGEN.
Organic compounds containing a BENZENE ring attached to a flavone group. Some of these are potent arylhydrocarbon hydroxylase inhibitors. They may also inhibit the binding of NUCLEIC ACIDS to BENZOPYRENES and related compounds. The designation includes all isomers; the 7,8-isomer is most frequently encountered.
A rigorously mathematical analysis of energy relationships (heat, work, temperature, and equilibrium). It describes systems whose states are determined by thermal parameters, such as temperature, in addition to mechanical and electromagnetic parameters. (From Hawley's Condensed Chemical Dictionary, 12th ed)
The voltage differences across a membrane. For cellular membranes they are computed by subtracting the voltage measured outside the membrane from the voltage measured inside the membrane. They result from differences of inside versus outside concentration of potassium, sodium, chloride, and other ions across cells' or ORGANELLES membranes. For excitable cells, the resting membrane potentials range between -30 and -100 millivolts. Physical, chemical, or electrical stimuli can make a membrane potential more negative (hyperpolarization), or less negative (depolarization).
The concentration of osmotically active particles in solution expressed in terms of osmoles of solute per liter of solution. Osmolality is expressed in terms of osmoles of solute per kilogram of solvent.
The restriction of a characteristic behavior, anatomical structure or physical system, such as immune response; metabolic response, or gene or gene variant to the members of one species. It refers to that property which differentiates one species from another but it is also used for phylogenetic levels higher or lower than the species.
Proteins prepared by recombinant DNA technology.
A generic descriptor for all TOCOPHEROLS and TOCOTRIENOLS that exhibit ALPHA-TOCOPHEROL activity. By virtue of the phenolic hydrogen on the 2H-1-benzopyran-6-ol nucleus, these compounds exhibit varying degree of antioxidant activity, depending on the site and number of methyl groups and the type of ISOPRENOIDS.
The sum of the weight of all the atoms in a molecule.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
An increase in MITOCHONDRIAL VOLUME due to an influx of fluid; it occurs in hypotonic solutions due to osmotic pressure and in isotonic solutions as a result of altered permeability of the membranes of respiring mitochondria.
Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed)
A group of enzymes that oxidize diverse nitrogenous substances to yield nitrite. (Enzyme Nomenclature, 1992) EC 1.
Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES.
Life or metabolic reactions occurring in an environment containing oxygen.
An iron-sulfur protein which serves as an electron carrier in enzymatic steroid hydroxylation reactions in adrenal cortex mitochondria. The electron transport system which catalyzes this reaction consists of adrenodoxin reductase, NADP, adrenodoxin, and cytochrome P-450.
A genus of gram-negative, rod-shaped, phototrophic bacteria found in aquatic environments. Internal photosynthetic membranes are present as lamellae underlying the cytoplasmic membrane.
Electron transfer through the cytochrome system liberating free energy which is transformed into high-energy phosphate bonds.
A subtype of striated muscle, attached by TENDONS to the SKELETON. Skeletal muscles are innervated and their movement can be consciously controlled. They are also called voluntary muscles.
Histochemical localization of immunoreactive substances using labeled antibodies as reagents.
Mitochondria of skeletal and smooth muscle. It does not include myocardial mitochondria for which MITOCHONDRIA, HEART is available.
A liver microsomal cytochrome P450 enzyme that catalyzes the 16-alpha-hydroxylation of a broad spectrum of steroids, fatty acids, and xenobiotics in the presence of molecular oxygen and NADPH-FERRIHEMOPROTEIN REDUCTASE. This enzyme is encoded by a number of genes from several CYP2 subfamilies.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
A bacterial protein from Pseudomonas, Bordetella, or Alcaligenes which operates as an electron transfer unit associated with the cytochrome chain. The protein has a molecular weight of approximately 16,000, contains a single copper atom, is intensively blue, and has a fluorescence emission band centered at 308nm.
Cytochromes of the b group that are found as components of the CYTOCHROME B6F COMPLEX. They contain two non-covalently bound HEME B groups.
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
A group of proteins possessing only the iron-sulfur complex as the prosthetic group. These proteins participate in all major pathways of electron transport: photosynthesis, respiration, hydroxylation and bacterial hydrogen and nitrogen fixation.
A carcinogen that is often used in experimental cancer studies.
The complete absence, or (loosely) the paucity, of gaseous or dissolved elemental oxygen in a given place or environment. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.
Property of membranes and other structures to permit passage of light, heat, gases, liquids, metabolites, and mineral ions.
An indolocarbazole that is a potent PROTEIN KINASE C inhibitor which enhances cAMP-mediated responses in human neuroblastoma cells. (Biochem Biophys Res Commun 1995;214(3):1114-20)
An electrochemical technique for measuring the current that flows in solution as a function of an applied voltage. The observed polarographic wave, resulting from the electrochemical response, depends on the way voltage is applied (linear sweep or differential pulse) and the type of electrode used. Usually a mercury drop electrode is used.
A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.
Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.
Highly reactive compounds produced when oxygen is reduced by a single electron. In biological systems, they may be generated during the normal catalytic function of a number of enzymes and during the oxidation of hemoglobin to METHEMOGLOBIN. In living organisms, SUPEROXIDE DISMUTASE protects the cell from the deleterious effects of superoxides.
An essential amino acid that is required for the production of HISTAMINE.
The section of the alimentary canal from the STOMACH to the ANAL CANAL. It includes the LARGE INTESTINE and SMALL INTESTINE.

Bcl-2 regulates amplification of caspase activation by cytochrome c. (1/3703)

Caspases, a family of specific proteases, have central roles in apoptosis [1]. Caspase activation in response to diverse apoptotic stimuli involves the relocalisation of cytochrome c from mitochondria to the cytoplasm where it stimulates the proteolytic processing of caspase precursors. Cytochrome c release is controlled by members of the Bcl-2 family of apoptosis regulators [2] [3]. The anti-apoptotic members Bcl-2 and Bcl-xL may also control caspase activation independently of cytochrome c relocalisation or may inhibit a positive feedback mechanism [4] [5] [6] [7]. Here, we investigate the role of Bcl-2 family proteins in the regulation of caspase activation using a model cell-free system. We found that Bcl-2 and Bcl-xL set a threshold in the amount of cytochrome c required to activate caspases, even in soluble extracts lacking mitochondria. Addition of dATP (which stimulates the procaspase-processing factor Apaf-1 [8] [9]) overcame inhibition of caspase activation by Bcl-2, but did not prevent the control of cytochrome c release from mitochondria by Bcl-2. Cytochrome c release was accelerated by active caspase-3 and this positive feedback was negatively regulated by Bcl-2. These results provide evidence for a mechanism to amplify caspase activation that is suppressed at several distinct steps by Bcl-2, even after cytochrome c is released from mitochondria.  (+info)

Mitochondrial depolarization accompanies cytochrome c release during apoptosis in PC6 cells. (2/3703)

Cytochrome c is released from mitochondria into the cytosol in cells undergoing apoptosis. The temporal relationship between cytochrome c release and loss of mitochondrial membrane potential was monitored by laser-scanning confocal microscopy in single living pheochromocytoma-6 cells undergoing apoptosis induced by staurosporine. Mitochondrial membrane potential monitored by tetramethylrhodamine methyl ester decreased abruptly in individual cells from 2 to 7 h after treatment with staurosporine. Depolarization was accompanied by cytochrome c release documented by release of transfected green fluorescent protein-tagged cytochrome c in these cells. The results show that mitochondrial depolarization accompanies cytochrome c release in pheochromocytoma-6 cells undergoing apoptosis.  (+info)

Role of hypoxia-induced Bax translocation and cytochrome c release in reoxygenation injury. (3/3703)

We investigated mechanisms of cell death during hypoxia/reoxygenation of cultured kidney cells. During glucose-free hypoxia, cell ATP levels declined steeply resulting in the translocation of Bax from cytosol to mitochondria. Concurrently, there was cytochrome c release and caspase activation. Cells that leaked cytochrome c underwent apoptosis after reoxygenation. ATP depletion induced by a mitochondrial uncoupler resulted in similar alterations even in the presence of oxygen. Moreover, inclusion of glucose during hypoxia prevented protein translocations and reoxygenation injury by maintaining intracellular ATP. Thus, ATP depletion, rather than hypoxia per se, was the cause of protein translocations. Overexpression of Bcl-2 prevented cytochrome c release and reoxygenation injury without ameliorating ATP depletion or Bax translocation. On the other hand, caspase inhibitors did not prevent protein translocations, but inhibited apoptosis during reoxygenation. Nevertheless, they could not confer long-term viability, since mitochondria had been damaged. Omission of glucose during reoxygenation resulted in continued failure of ATP production, and cell death with necrotic morphology. In contrast, cells expressing Bcl-2 had functional mitochondria and remained viable during reoxygenation even without glucose. Therefore, Bax translocation during hypoxia is a molecular trigger for cell death during reoxygenation. If ATP is available during reoxygenation, apoptosis develops; otherwise, death occurs by necrosis. By preserving mitochondrial integrity, BCL-2 prevents both forms of cell death and ensures cell viability.  (+info)

Ceramide induces cytochrome c release from isolated mitochondria. Importance of mitochondrial redox state. (4/3703)

In the present study we show that N-acetylsphingosine (C2-ceramide), N-hexanoylsphingosine (C6-ceramide), and, to a much lesser extent, C2-dihydroceramide induce cytochrome c (cyto c) release from isolated rat liver mitochondria. Ceramide-induced cyto c release is prevented by preincubation of mitochondria with a low concentration (40 nM) of Bcl-2. The release takes place when cyto c is oxidized but not when it is reduced. Upon cyto c loss, mitochondrial oxygen consumption, mitochondrial transmembrane potential (Delta Psi), and Ca2+ retention are diminished. Incubation with Bcl-2 prevents, and addition of cyto c reverses the alteration of these mitochondrial functions. In ATP-energized mitochondria, ceramides do not alter Delta Psi, neither when cyto c is oxidized nor when it is reduced, ruling out a nonspecific disturbance by ceramides of mitochondrial membrane integrity. Furthermore, ceramides decrease the reducibility of cyto c. We conclude that the apoptogenic properties of ceramides are in part mediated via their interaction with mitochondrial cyto c followed by its release and that the redox state of cyto c influences its detachment by ceramide from the inner mitochondrial membrane.  (+info)

Altered cytochrome c display precedes apoptotic cell death in Drosophila. (5/3703)

Drosophila affords a genetically well-defined system to study apoptosis in vivo. It offers a powerful extension to in vitro models that have implicated a requirement for cytochrome c in caspase activation and apoptosis. We found that an overt alteration in cytochrome c anticipates programmed cell death (PCD) in Drosophila tissues, occurring at a time that considerably precedes other known indicators of apoptosis. The altered configuration is manifested by display of an otherwise hidden epitope and occurs without release of the protein into the cytosol. Conditional expression of the Drosophila death activators, reaper or grim, provoked apoptogenic cytochrome c display and, surprisingly, caspase activity was necessary and sufficient to induce this alteration. In cell-free studies, cytosolic caspase activation was triggered by mitochondria from apoptotic cells but identical preparations from healthy cells were inactive. Our observations provide compelling validation of an early role for altered cytochrome c in PCD and suggest propagation of apoptotic physiology through reciprocal, feed-forward amplification involving cytochrome c and caspases.  (+info)

Folding of apocytochrome c induced by the interaction with negatively charged lipid micelles proceeds via a collapsed intermediate state. (6/3703)

Unfolded apocytochrome c acquires an alpha-helical conformation upon interaction with lipid. Folding kinetic results below and above the lipid's CMC, together with energy transfer measurements of lipid bound states, and salt-induced compact states in solution, show that the folding transition of apocytochrome c from the unfolded state in solution to a lipid-inserted helical conformation proceeds via a collapsed intermediate state (I(C)). This initial compact state is driven by a hydrophobic collapse of the polypeptide chain in the absence of the heme group and may represent a heme-free analogue of an early compact intermediate detected on the folding pathway of cytochrome c in solution. Insertion into the lipid phase occurs via an unfolding step of I(C) through a more extended state associated with the membrane surface (I(S)). While I(C) appears to be as compact as salt-induced compact states in solution with substantial alpha-helix content, the final lipid-inserted state (Hmic) is as compact as the unfolded state in solution at pH 5 and has an alpha-helix content which resembles that of native cytochrome c.  (+info)

Balanced regulation of expression of the gene for cytochrome cM and that of genes for plastocyanin and cytochrome c6 in Synechocystis. (7/3703)

The cytM gene for cytochrome cM was previously found in Synechocystis sp. PCC 6803. Northern blotting analysis revealed that the cytM gene was scarcely expressed under normal growth conditions but its expression was enhanced when cells were exposed to low temperature or high-intensity light. By contrast, the expression of the genes for cytochrome c6 and plastocyanin was suppressed at low temperature or under high-intensity light. These observations suggest that plastocyanin and/or cytochrome c6, which are dominant under non-stressed conditions, are replaced by cytochrome cM under the stress conditions.  (+info)

p27Kip1 induces drug resistance by preventing apoptosis upstream of cytochrome c release and procaspase-3 activation in leukemic cells. (8/3703)

The cyclin-dependent kinase inhibitor p27Kip1 has been implicated as a drug resistance factor in tumor cells grown as spheroids or confluent monolayers. Here, we show that p27Kip1 overexpression also induces resistance to drug-induced apoptosis and cytotoxicity in human leukemic cells growing in suspension. The anti-apoptotic effect of p27Kip1 is not restricted to DNA-damaging agents but extends to the tubulin poison vinblastin, agonistic anti-Fas antibodies and macromolecule synthesis inhibitors. To further identify at which level this protein interferes with the cell death pathway, we investigated its influence on caspase activation and mitochondrial changes. Exposure of mock-transfected U937 cells to 50 microm etoposide activates procaspase-3 and the long isoform of procaspase-2 and induces mitochondrial potential decrease and cytochrome c release from mitochondria to the cytosol. All these events are prevented by p27Kip1 overexpression. p27Kip1 does not modulate Bcl-2, Bcl-X(L), Mcl-1 and Bax protein level in leukemic cells but suppresses Mcl-1 expression decrease observed in mock-transfected U937 cells undergoing etoposide-induced cell death. We conclude that p27Kip1 prevents cell death upstream of the final pathway common to many apoptotic stimuli that involves cytochrome c release from mitochondria and activation of downstream caspases.  (+info)

Conversion of Hydrogenobacter thermophilus cytochrome c(552) into a b-type cytochrome by mutagenesis of both heme-binding cysteines to alanines significantly reduces the stability of the protein (Tomlinson, E. J., and Ferguson, S. J. (2000) Proc. Natl. Acad. Sci. U. S. A. 97, 5156-5160). To understand the effects of this change on the structure and dynamics of the protein, hetero-nuclear (15)N-edited NMR techniques have been used to characterize this b-type variant. The backbone (15)N, (1)H(N), and (1)H(alpha), and (1)H(beta) resonances of the protein have been assigned. Analysis of (3)J(HN)alpha coupling constants, nuclear Overhauser enhancement intensities, and chemical shift index data demonstrates that the four alpha-helices present in the wild-type protein are retained in the b-type variant. Comparison of the chemical shifts for the b-type and wild-type proteins indicates that the tertiary structures of the two proteins are closely similar. Some subtle differences are, however, observed for
Steinberg, M. Z., Elber, R., McLafferty, F. W., Gerber, R. B. and Breuker, K. (2008), Early Structural Evolution of Native Cytochrome c after Solvent Removal. ChemBioChem, 9: 2417-2423. doi: 10.1002/cbic.200800167 ...
Cytochrome c plays an important role in apoptosis. The protein is located in the space between the inner and outer mitochondrial membranes. An apoptotic stimulus triggers the release of cytochrome c from the mitochondria into cytosol where it binds to Apaf-1. The cytochrome c/Apaf-1 complex activates caspase-9, which then activates caspase-3 and other downstream caspases. GeneTexs Cytochrome c Releasing Apoptosis Assay Kit provides an effective means for detecting cytochrome c translocation from mitochondria into cytosol during apoptosis. The kit provides unique formulations of reagents to isolate a highly enriched mitochondria fraction from cytosol. The procedure is so simple and easy to perform, no ultracentrifugation is required and no toxic chemicals are involved. Cytochrome c releasing from mitochondria into cytosol is then determined by Western blotting using the cytochrome c antibody provided in the kit. |p>|br />|br />‧ Detection method- Western blotting|br>|br />‧ Sample type- Cells and
TY - JOUR. T1 - Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. AU - Luo, Xu. AU - Budihardjo, Imawati. AU - Zou, Hua. AU - Slaughter, Clive. AU - Wang, Xiaodong. PY - 1998/8/21. Y1 - 1998/8/21. N2 - We report here the purification of a cytosolic protein that induces cytochrome c release from mitochondria in response to caspase-8, the apical caspase activated by cell surface death receptors such as Fas and TNF. Peptide mass fingerprinting identified this protein as Bid, a BH3 domain- containing protein known to interact with both Bcl2 and Bax. Caspase-8 cleaves Bid, and the COOH-terminal part translocates to mitochondria where it triggers cytochrome c release. Immunodepletion of Bid from cell extracts eliminated the cytochrome c releasing activity. The cytochrome c releasing activity of Bid was antagonized by Bcl2. A mutation at the BH3 domain diminished its cytochrome c releasing activity. Bid, ...
c-Type cytochromes are widespread proteins, fundamental for respiration or photosynthesis in most cells. They contain heme covalently bound to protein in a highly conserved, highly stereospecific post-translational modification. In many bacteria, mitochondria, and archaea this heme attachment is catalyzed by the cytochrome c maturation (Ccm) proteins. Here we identify and characterize a covalent, ternary complex between the heme chaperone CcmE, heme, and cytochrome c. Formation of the complex from holo-CcmE occurs in vivo and in vitro and involves the specific heme-binding residues of both CcmE and apocytochrome c. The enhancement and attenuation of the amounts of this complex correlates completely with known consequences of mutations in genes for other Ccm proteins. We propose the complex is a trapped catalytic intermediate in the cytochrome c biogenesis process, at the point of heme transfer from CcmE to the cytochrome, the key step in the maturation pathway.
Conformational transitions of proteins play a crucial role in many biochemical and biophysical reactions. Understanding the conformational changes of a protein upon adsorption to a substrate is very important in biotechnology, e.g. the development of modern protein chip technology, biocompatibility of implants, and many other ones. This research program used cytochrome c, an electron carrier in the respiratory chain, as a model to probe how surface adsorption affects the folding of a protein. My work investigates the interaction of protein horse heart cytochrome c when it is electrostatically adsorbed or covalently attached onto a 1 nm thick monolayer film, which covers an Au surface. After changing the pH value of the solutions or adding the denaturants into the solutions, the conformation of cytochrome c changes and causes a change of the peak current of cyclic voltammgram. In addition, the denatured cytochrome c¡¯s peroxidase activity will be studied and compared with the peroxidase ...
Cytochrome c also has an intermediate role in apoptosis, a controlled form of cell death used to kill cells in the process of development or in response to infection or DNA damage.[17] Cytochrome c binds to cardiolipin in the inner mitochondrial membrane, thus anchoring its presence and keeping it from releasing out of the mitochondria and initiating apoptosis. While the initial attraction between cardiolipin and cytochrome c is electrostatic due to the extreme positive charge on cytochrome c, the final interaction is hydrophobic, where a hydrophobic tail from cardiolipin inserts itself into the hydrophobic portion of cytochrome c. During the early phase of apoptosis, mitochondrial ROS production is stimulated, and cardiolipin is oxidized by a peroxidase function of the cardiolipin-cytochrome c complex. The hemoprotein is then detached from the mitochondrial inner membrane and can be extruded into the soluble cytoplasm through pores in the outer membrane.[18] The sustained elevation in calcium ...
Cytochrome c also has an intermediate role in apoptosis, a controlled form of cell death used to kill cells in the process of development or in response to infection or DNA damage.[20]. Cytochrome c binds to cardiolipin in the inner mitochondrial membrane, thus anchoring its presence and keeping it from releasing out of the mitochondria and initiating apoptosis. While the initial attraction between cardiolipin and cytochrome c is electrostatic due to the extreme positive charge on cytochrome c, the final interaction is hydrophobic, where a hydrophobic tail from cardiolipin inserts itself into the hydrophobic portion of cytochrome c.. During the early phase of apoptosis, mitochondrial ROS production is stimulated, and cardiolipin is oxidized by a peroxidase function of the cardiolipin-cytochrome c complex. The hemoprotein is then detached from the mitochondrial inner membrane and can be extruded into the soluble cytoplasm through pores in the outer membrane.[21]. The sustained elevation in ...
TY - JOUR. T1 - Dissociation of Cytochrome c from the Inner Mitochondrial Membrane during Cardiac Ischemia. AU - Czerski, Lech W.. AU - Szweda, Pamela A.. AU - Szweda, Luke I.. PY - 2003/9/5. Y1 - 2003/9/5. N2 - Mitochondria isolated from ischemic cardiac tissue exhibit diminished rates of respiration and ATP synthesis. The present study was undertaken to determine whether cytochrome c release was responsible for ischemia-induced loss in mitochondrial function. Rat hearts were perfused in Langendorff fashion for 60 min (control) or for 30 min followed by 30 min of no flow ischemia. Mitochondria isolated from ischemic hearts in a buffer containing KCl exhibited depressed rates of maximum respiration and a lower cytochrome c content relative to control mitochondria. The addition of cytochrome c restored maximum rates of respiration, indicating that the release of cytochrome c is responsible for observed declines in function. However, mitochondria isolated in a mannitol/sucrose buffer exhibited no ...
Induction of mitochondrial permeability transition (MPT) and cytosolic translocation of cytochrome C are considered essential components of the apoptotic pathway. Hence, there is the realization that mitochondrial- specific drugs could have potential for use as chemotherapeutic agents to trigger apoptosis In tumor cells. Recently, we showed that photoproducts of merocyanine 540 (pMC540) induced tumor cell apoptosis. In this study, we focused on identifying mitochondrial-specific compounds from pMC540 and studied their apoptotic potential. One purified fraction, C5, induced a drop In mitochondrial transmembrane potential and cytosolic translocation of cytochrome C in HL60 human leukemia cells. Moreover, the addition of C5 to purified rat liver mitochondria induced MPT as indicated by mitochondrial matrix swelling, which was completely inhibited by cyclosporin A, an inhibitor of the inner-membrane pore. Supernatant of C5-treated mitochondria showed a dose-dependent increase in cytochrome C, which ...
BioAssay record AID 294693 submitted by ChEMBL: Effect on apoptosis in Ac-IETD-cho treated HL60 cells assessed as mitochondrial cytochrome C release at 5 uM by Western blot analysis.
Balanced amounts of apoptotic cell death are essential for health; its deregulation plays key roles in neurodegeneration, autoimmunity, and cancer. Mitochondria orchestrate apoptosis through a process called mitochondrial outer-membrane permeabilization (MOMP). After MOMP, mitochondrial cytochrome c is released into the cytoplasm, where it binds the adaptor molecule APAF1, triggering caspase protease activation and cell death. In this issue of Science Signaling, Deshmukh and colleagues define a new survival mechanism downstream of mitochondrial permeabilization. Specifically, they identify proteasomal degradation of cytochrome c as a major determinant of cell survival. In an unbiased approach, PARC (also known as CUL9) was found to be the ubiquitin ligase responsible for the ubiquitination and proteasomal degradation of cytochrome c. The consequences of this survival process may be double-edged because both cancer cells and postmitotic cells use PARC/CUL9-mediated cytochrome c degradation to ...
Cytochrome c Cytochrome c, somatic Cytochrome c with heme Available structures: 1j3s, 2b4z Identifiers Symbol(s) CYCS; HCS; CYC External IDs OMIM: 123970
The results of the present study demonstrate that CSA inhibits oxLDL-induced apoptosis of human endothelial cells. The mechanism underlying the protective effect of CSA appears to involve stabilization of mitochondria, thereby preventing the release of the mitochondrial protein cytochrome C into the cytosol. Cytosolic cytochrome C has been shown to be necessary to activate the apoptosome complex leading to caspase activation and apoptosis induction. The findings of the present study may give mechanistic insights into CSA action and may support the results of several experimental studies that demonstrate an antiatherosclerotic effect of CSA in transplant atherosclerosis as well as hyperlipidemia-induced atherosclerosis.8 9 16 In cardiac heart transplants, accelerated coronary atherosclerosis has become the principal cause of late death and allograft dysfunction.17 Accelerated atherosclerosis is assumed to be mediated by alloimmunity; however, additional antigen-independent mechanisms may also ...
Substitution with all naturally occurring L-amino acids at each of 11 residues of the IEk-restricted month cytochrome c (93-103) epitope has allowed us to analyze the requirements for MHC binding and T cell recognition to a level of definition not previously possible. Substitutions at only three positions systematically affect MHC binding and three others appear to be the major TCR contacts. Interestingly, changing residues involved in MHC binding can ablate T cell recognition without altering MHC association. Additionally, residue identity at two positions that do not appear critical for MHC binding, nor to be involved in specific T cell contact, nonetheless dramatically affect T cell responses. This suggests that peptides differing only slightly in sequence can have significantly altered conformations within the class II MHC binding groove. We have also developed a simple scoring program that uses the binding data to quantitate how well a given peptide fits the MCC motif. All strongly ...
Abstract: Oxidative phosphorylation in mitochondria of small intestinal mucosa was studied after repeated overheating of rats. The hyperthermia affected the respiratory chains of mitochondrial membranes, facilitating the penetration of ADP, succinate, alpha-ketoglutarate and NADH across the membranes. Under these conditions thermostability of the respiratory chain multienzyme system was decreased and the rate of exogenous cytochrome c incorporation into mitochondrial membranes was altered. In the mitochondrial membranes from small intestinal mucosa there was noted development of latent impairments, the reversibility of which depended on the intensity and duration of hyperthermia ...
TY - JOUR. T1 - Increased cytochrome c correlates with poor survival in aggressive lymphoma. AU - Wilkinson, Saraht. AU - Johnson, David B F. AU - Tardif, Heather L.. AU - Tome, Margaret E. AU - Briehl, Margaret M. PY - 2010/3. Y1 - 2010/3. N2 - Mitochondria are central to a variety of cellular processes, from metabolism to cell death. In this study, we demonstrated that an increase in the critical mitochondrial protein, cytochrome c, correlated with drug resistance in a cell culture model of aggressive lymphoma. Increased cytochrome c expression was also correlated with decreased survival in the aggressive diffuse large B-cell and mantle cell lymphomas, but not in the indolent follicular lymphoma. This suggests that an increased reliance on the mitochondria for energy allows tumor cells to be metabolic opportunists and contribute to tumor development and drug resistance.. AB - Mitochondria are central to a variety of cellular processes, from metabolism to cell death. In this study, we ...
Cytochrome c, or Cyt c, is a small heme protein and a component of the oxidative phosphorylation electron transport chain. The heme group of cytochrome c accepts electrons from the Cytochrome b-c1 complex (Complex III) and transfers electrons to the Cytochrome oxidase complex (Complex IV). Cyt c is capable of undergoing oxidation and reduction, but does not bind oxygen. Cytochrome c is a highly conserved protein across the spectrum of species, found in plants, animals, and many unicellular organisms. This, along with its small size (molecular weight about 12,000 daltons), makes it useful in studies of cladistics. Its primary structure consists of a chain of about 100 amino acids. (Wikipedia ...
1M1R: Crystal structures at atomic resolution reveal the novel concept of electron-harvesting as a role for the small tetraheme cytochrome c
Platini Kwok wrote: , Recently, I was involved in the immunostaining of cytochrome c in embryo , tissue. The tissue was fixed in 4% paraformaldehyde and dehydrated in , graded alcohol, xylene and finally it was embared in wax block. It is , found that only few positive signals were found in heart and bone tissue The harsh treatment during tissue processing may or may not prevent proper staining of an antigen. The risk is obviously greatest with monoclonal antibodies, which have only a single binding epitope. Polyclonal antibodies, with their multiple binding sites, are less susceptible. There are several ways to control for this effect. One is to use frozen sections from unfixed tissues instead of parafine embedding. This avoids a lot of the denaturing processes. The second experiment you can perform is to carefully trypsinize the sections before antibody exposure to recover blocked antigenic sites. Works sometimes and sometimes not. Briefly microwaving sections in citrate buffer has also been ...
Interleukin-5 inhibits translocation of Bax to the mitochondria, cytochrome c release, and activation of caspases in human eosinophils ...
Oxidative Medicine and Cellular Longevity is a unique peer-reviewed, Open Access journal that publishes original research and review articles dealing with the cellular and molecular mechanisms of oxidative stress in the nervous system and related organ systems in relation to aging, immune function, vascular biology, metabolism, cellular survival and cellular longevity. Oxidative stress impacts almost all acute and chronic progressive disorders and on a cellular basis is intimately linked to aging, cardiovascular disease, cancer, immune function, metabolism and neurodegeneration. The journal fills a significant void in todays scientific literature and serves as an international forum for the scientific community worldwide to translate pioneering
Cytochrome C, molecular model. Cytochrome molecules perform oxidation and reduction reactions for electron transport, a chain of reactions used to power cellular processes that require energy. As cytochromes perform a key step in the production of energy they are found in all living organisms, however simple or complex. - Stock Image F006/9696
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Hydrogen peroxide (H(2)O(2)) is the major reactive oxygen species (ROS) produced in sperm. High concentrations of H(2)O(2) in sperm induce nuclear DNA fragmentation and lipid peroxidation and result in cell death. The respiratory chain of the mitochondrion is one of the most productive ROS generating systems in sperm, and thus the destruction of ROS in mitochondria is critical for the cell. It was recently reported that H(2)O(2) generated by the respiratory chain of the mitochondrion can be efficiently destroyed by the cytochrome c-mediated electron-leak pathway where the electron of ferrocytochrome c migrates directly to H(2)O(2) instead of to cytochrome c oxidase. In our studies, we found that mouse testis-specific cytochrome c (T-Cc) can catalyze the reduction of H(2)O(2) three times faster than its counterpart in somatic cells (S-Cc) and that the T-Cc heme has the greater resistance to being degraded by H(2)O(2). Together, these findings strongly imply that T-Cc can protect sperm from the ...
Probable electron donor to membrane cytochrome oxidase and to periplasmic nitrite reductase. Membrane-binding site participates in protein-protein interaction ...
Biogenesis of respiratory cytochromes is defined as consisting of the posttranslational processes that are necessary to assemble apoprotein, heme, and sometimes additional cofactors into mature enzyme complexes with electron transfer functions. Different biochemical reactions take place during maturation: (i) targeting of the apoprotein to or through the cytoplasmic membrane to its subcellular destination; (ii) proteolytic processing of precursor forms; (iii) assembly of subunits in the membrane and oligomerization; (iv) translocation and/or modification of heme and covalent or noncovalent binding to the protein moiety; (v) transport, processing, and incorporation of other cofactors; and (vi) folding and stabilization of the protein. These steps are discussed for the maturation of different oxidoreductase complexes, and they are arranged in a linear pathway to best account for experimental findings from studies concerning cytochrome biogenesis. The example of the best-studied case, i.e., ...
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Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B ...
Remember when I told you that some genes are found in all living things. These core genes pick up changes very slowly because they are so critical for lifes functions. If you compare the DNA sequences for one of these genes, say cytochrome c, you will see that there are fewer differences between humans humans, apes, monkeys, and other primates than there are between humans and other mammals. The number of differences increases as you go from mammals to reptiles to amphibians to fish to protozoa to archeabacteria to bacteria. This gene has the same function in all of these organisms, so you cant say that you expect the gene to be more similar in organisms that look alike than in those that dont. The only logical explanation is that the orginal cytochrome c gene has changed slowly over time and that those organisms that have more similar sequences shared a common ancestor more recently than those organisms with more differences ...
In this report, we have established the mechanism of the apoptotic effect of a Bcl-2-interacting small molecule, HA14-1. HA14-1 binds Bcl-2 and neutralizes the antiapoptotic effect of Bcl-2. However, our cell-free mitochondrial study revealed that it is not enough to induce cytochrome c release by just blocking Bcl-2 with HA14-1. The translocation of Bax from the cytosol to the mitochondria is essential for the subsequent cytochrome c release. This study therefore provides an important clue regarding the primary effector in induction of cell death. Bcl-2 and Bax not only function through antagonizing each other but also have independent functions (22). Is the blocking of Bcl-2 or the activation of Bax more critical in triggering apoptosis? It has been very difficult to separate these two events due to the lack of critical tools. With the availability of HA14-1, we were able to achieve blockage of Bcl-2 in cell-free mitochondria to study the consequence of Bcl-2 blockage alone. Our result ...
With ActivStyles personalized service, you can spend more time caring for your loved one and less time worrying about their medical supplies. ActivStyle is here to provide an easy way to collar the home medical supplies you call, when you requisite them. We pay over 30 jillion dollars pa on dieting products purchase gyne-lotrimin 100mg fast delivery antifungal drink. While the 5-year survival of the patients in the chemoradiation arm was 62 % and the sur- vival toll was 58 % in the emission unattended arm, this difference failed to reach statistical significance. The Bcl-2 kinsfolk proteins can be divided into three significant subgroups: (1) Anti-apoptotic proteins, such as Bcl-2, Bcl-XL, and Mcl-1, which typically interest four conserved motifs termed Bcl-2 homology (BH) domains and can species heterodimers with Bax, inhibiting mitochondrial cytochrome c release and protecting against chamber destruction; (2) The pro-apoptotic proteins, such as Bax, Bak, and Bok, which typically entertain ...
Reactome is pathway database which provides intuitive bioinformatics tools for the visualisation, interpretation and analysis of pathway knowledge.
On May 17, 2016, the U.S. Energy Information Administration (EIA) published an early release of its Annual Energy Outlook (AEO) for 2016. This early release contains projections for two scenarios: a Reference case, which includes the effects of the Clean Power Plan, and a No Clean Power Plan case, which examines a future in which there is no Clean Power Plan. Final versions of each of these cases, along with projections for numerous other scenarios, will be available on July 7, 2016. Until then, here are some of the key highlights in the latest AEO: ...
Creation.com Cytochrome-c is a protein and is a gene product. It functions as a key enzyme in oxidation reactions and seems to occur in practically every living organism. There are 20 different amino acids. Cytochrome-c consists of a chain of 112 amino acids, 19 of which occur in exactly the same sequential order positions in all…
Use spells to attack enemies and defend yourself. So far theres only a flamethrower and leaf shield, but more are planned. Controls are as follows: D and A move left and right, Space jumps, and O and P unleash your attacks. NOTE: This is a VERY early release, so graphics are pretty terrible at the moment. The player is currently a log, but thatll be changed someday if I decide to continue working on it. I ask that you give me LOADS of suggestions on how to make it better. I feel like a lot needs to be improved, but I cant really pinpoint what. Tell me any cool enemy ideas, how I should improve AI, how to improve level design, etc. Any and all criticism is good ...
A pretty early release of a game Ive been wanting to work on (Ive always wanted to make a shmup). When its completed itll have 100% hand drawn graphics, but for now its still borrowing a few bits and pieces from a scrapped earlier project ...
If there is no Gene record for this gene and organism, perform an All databases search with the gene name, product name, symbol, or accession number. For names, include the organism in the search to find the most relevant results, for example: Cytochrome c AND bullfrog[orgn] AND mrna[filter ...
The pro-apoptotic protein Bax plays a key role in the mitochondrial signalling pathway. Upon induction of apoptosis, Bax undergoes a conformational change and translocates to mitochondrial membranes, where it inserts and mediates the release of cytochrome c from the intermembrane space into the cytosol. However, the domains of Bax that are essential for the induction of cytochrome c release are still elusive. Therefore various Bax deletion mutants were generated and expressed in Escherichia coli. The proteins were then purified in order to delineate the function of the transmembrane domain, the BH3 (Bcl-2 homology 3) domain and the putative pore-forming α-helices-5 and -6. These proteins were used to analyse the mechanism of Bax-induced cytochrome c release from mitochondria. None of the Bax proteins caused cytochrome c release merely through physical perturbation of the mitochondrial outer membrane. The α-helices-5 and -6 of Bax were shown to mediate the insertion of the protein into ...
We have cloned, sequenced, and heterologously expressed a periplasmic cytochrome c from a lupanine-utilizing Pseudomonas putida strain. Aerobic batch cultivation of Escherichia coli TB1 harboring the cytochrome c gene placed downstream of the lac promoter in pUC9 vector resulted in significant production of the holo-cytochrome c in the periplasm (4 mg of hemoprotein/liter of culture). The recombinant cytochrome c was purified to homogeneity and was found to be functional in accepting electrons from lupanine hydroxylase while catalyzing hydroxylation of lupanine. Comparison of the N-terminal amino acid sequence of the isolated cytochrome c with that deduced from the DNA sequence indicated that the signal sequence was processed at the bond position predicted by the SigPep program. The molecular size of the cytochrome c determined by electrospray mass spectrometry (9,595) was in precise agreement with that predicted from the nucleotide sequence ...
TY - JOUR. T1 - Differential Apaf-1 levels allow cytochrome c to induce apoptosis in brain tumors but not in normal neural tissues. AU - Johnson, Carrie E.. AU - Huang, Yolanda Y.. AU - Parrish, Amanda B.. AU - Smith, Michelle I.. AU - Vaughn, Allyson E.. AU - Zhang, Qian. AU - Wright, Kevin M.. AU - Van Dyke, Terry. AU - Wechsler-Reya, Robert J.. AU - Kornbluth, Sally. AU - Deshmukh, Mohanish. N1 - Copyright: Copyright 2008 Elsevier B.V., All rights reserved.. PY - 2007/12/26. Y1 - 2007/12/26. N2 - Brain tumors are typically resistant to conventional chemotherapeutics, most of which initiate apoptosis upstream of mitochondrial cytochrome c release. In this study, we demonstrate that directly activating apoptosis downstream of the mitochondria, with cytosolic cytochrome c, kills brain tumor cells but not normal brain tissue. Specifically, cytosolic cytochrome c is sufficient to induce apoptosis in glioblastoma and medulloblastoma cell lines. In contrast, primary neurons from the cerebellum and ...
A series of experiments were performed to explore the role of complementing major histocompatability complex (MHC)-linked immune response Ir genes in the murine T cell proliferative response to the globular protein antigen pigeon cytochrome c. The functional equivalence of I-E-subregion-encoded, structurally homologous E(a) chains from different haplotypes bearing the serologic specificity Ia.7 was demonstrated by the complementation for high responsiveness to pigeon cytochrome c of F(1) hybrids between low responder B 10.A(4R) (I-A (k)) or B 10.S (I-A(8)) mice and four low responder E(a)- bearing haplotypes. Moreover, this Ir gene function correlated directly with both the ability of antigen-pulsed spleen cells from these same F(1) strains to stimulate pigeon cytochrome c-primed T cells from B10.A or B10.S(9R) mice, and with the cell surface expression of the two-chain Ia antigenic complex, A(e):E(a), bearing the conformational or combinatorial determinant recognized by the monoclonal anti-Ia ...
Cytochromes of c-type contain covalently bound haem and in bacteria are located on the periplasmic side of the cytoplasmic membrane. More than eight different gene products have been identified as being specifically required for the synthesis of cytochromes c in Gram-negative bacteria. Corresponding genes are not found in the genome sequences of Gram-positive bacteria. Using two random mutagenesis approaches, we have searched for cytochrome c biogenesis genes in the Gram-positive bacterium Bacillus subtilis. Three genes, resB, resC and ccdA, were identified. CcdA has been found previously and is required for a late step in cytochrome c synthesis and also plays a role in spore synthesis. No function has previously been assigned for ResB and ResC but these predicted membrane proteins show sequence similarity to proteins required for cytochrome c synthesis in chloroplasts. Attempts to inactivate resB and resC in B. subtilis have indicated that these genes are essential for growth. We demonstrate ...
The coenzyme Q : cytochrome c - oxidoreductase, sometimes called the cytochrome bc1 complex, and at other times complex III, is the third complex in the electron transport chain (EC 1.10.2.2), playing a critical role in biochemical generation of ATP (oxidative phosphorylation). Complex III is a multisubunit transmembrane protein encoded by both the mitochondrial (cytochrome b) and the nuclear genomes (all other subunits). Complex III is present in the mitochondria of all animals and all aerobic eukaryotes and the inner membranes of most eubacteria. Mutations in Complex III cause exercise intolerance as well as multisystem disorders. The bc1 complex contains 11 subunits, 3 respiratory subunits (cytochrome B, cytochrome C1, Rieske protein), 2 core proteins and 6 low-molecular weight proteins. Ubiquinol-cytochrome-c reductase catalyzes the chemical reaction QH2 + 2 ferricytochrome c ⇌ {\displaystyle \rightleftharpoons } Q + 2 ferrocytochrome c + 2 H+ Thus, the two substrates of this enzyme are ...
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Cytochrome c oxidase was isolated from human hearts and separated by SDS gel electrophoresis. The identity of polypeptide bands with known subunits was demonstrated by immunoblotting with monospecific antisera to rat liver cytochrome c oxidase subunits. The polarographically determined kinetics of cytochrome c oxidation were similar to those reported for the bovine heart enzyme.
Fingerprint Dive into the research topics of Induction of apoptosis by the oolong tea polyphenol theasinensin A through cytochrome c release and activation of caspase-9 and caspase-3 in human u937 cells. Together they form a unique fingerprint. ...
The amino acid sequence of rattlesnake cytochrome c was originally reported in 1965, and was one of the earlier sequences to be studied. When compared with other mitochondrial cytochromes c, the snake sequence was soon seen to be anomalous. There were several positions in which the snake protein resembled human cytochrome c, although comparable anomalies were not reported for the protein from other reptiles such as lizard and turtle. Explanations of these results have included accelerated evolution in the snake lineage, paralogy rather than orthology, and faulty determination of the sequence, and the rattlesnake is now often omitted from cytochrome c phylogenetic trees. We have re-investigated the sequence of the snake protein, and believe that the correct sequence differs in nine places from that used for evolutionary theorizing since 1965. Four of these differences are near the haem-attachment site, in a region that was only analysed for amino acid composition in the original investigation. ...
TY - JOUR. T1 - Energetic mechanism of cytochrome c-cytochrome c oxidase electron transfer complex formation under turnover conditions revealed by mutational effects and docking simulation. AU - Sato, Wataru. AU - Hitaoka, Seiji. AU - Inoue, Kaoru. AU - Imai, Mizue. AU - Saio, Tomohide. AU - Uchida, Takeshi. AU - Shinzawa-Itoh, Kyoko. AU - Yoshikawa, Shinya. AU - Yoshizawa, Kazunari. AU - Ishimori, Koichiro. PY - 2016/7/15. Y1 - 2016/7/15. N2 - Based on the mutational effects on the steady-state kinetics of the electron transfer reaction and our NMR analysis of the interaction site (Sakamoto, K., Kamiya, M., Imai, M., Shinzawa-Itoh, K., Uchida, T., Kawano, K., Yoshikawa, S., and Ishimori, K. (2011) Proc. Natl. Acad. Sci. U.S.A. 108, 12271-12276), we determined the structure of the electron transfer complex between cytochrome c (Cyt c) and cytochrome c oxidase (CcO) under turnover conditions and energetically characterized the interactions essential for complex formation. The complex structures ...
Molecular Basis Behind Inability of Mitochondrial Holocytochrome c Synthase to Mature Bacterial Cytochromes: Defining a Critical Role for Cytochrome c Alpha Helix-1. Babbitt SE, Hsu J, Kranz RG. J Biol Chem. 2016 Jul 6. Heme Trafficking and Modifications during System I Cytochrome c Biogenesis: Insights from Heme Redox Potentials of Ccm Proteins. Sutherland MC, Rankin JA, Kranz RG. Biochemistry. 2016 Jun 7;55(22):3150-6. Mitochondrial cytochrome c biogenesis: no longer an enigma. Babbitt SE, Sutherland MC, San Francisco B, Mendez DL, Kranz RG. Trends Biochem Sci. 2015 Aug;40(8):446-55. Review.. Mechanisms of mitochondrial holocytochrome c synthase and the key roles played by cysteines and histidine of the heme attachment site, Cys-XX-Cys-His. Babbitt SE, San Francisco B, Mendez DL, Lukat-Rodgers GS, Rodgers KR, Bretsnyder EC, Kranz RG. J Biol Chem. 2014 289(42):28795-807.. Conserved residues of the human mitochondrial holocytochrome c synthase, HCCS, mediate interactions with heme. Babbitt SE, ...
article{15a70f88-5605-4029-8620-57102abad8ae, abstract = {Little is known about c-type cytochromosomes in Gram-positive bacteria in contrast to the wealth of information available on this type of cytochrome in Gram-negative bacteria and in eucaryotes. In the present work, the strictly aerobic bacterium Bacillus subtilis was analyzed for subcellular localization and number of different cytochromes c. In vivo labeling with radioactive 5-aminolevulinic acid, a precursor to heme, showed that the proteins containing covalently bound heme are predominantly found in the membranes fraction. One major membrane-bound cytochrome c of about 15 kDa and with an .alpha.-band absorption peak in the reduced state at 550 nm was analyzed in more detail. Cytochrome c-550 has the properties of an integral membrane protein. The physiological function of this relatively high redox potential cytochrome is not known. Its structural gene, cccA, was cloned, sequenced, and overexpressed in B. subtilis. The gene maps ...
Cytochrome c6A is a unique dithio-cytochrome present in land plants and some green algae. Its sequence and occurrence in the thylakoid lumen suggest that it is derived from cytochrome c6, which functions in photosynthetic electron transfer between the cytochrome b6f complex and photosystem I. Its known properties, however, and a strong indication that the disulfide group is not purely structural, indicate that it has a different, unidentified function. To help in the elucidation of this function the crystal structure of cytochrome c6A from Arabidopsis thaliana has been determined in the two redox states of the heme group, at resolutions of 1.2 A (ferric) and 1.4 A (ferrous). These two structures were virtually identical, leading to the functionally important conclusion that the heme and disulfide groups do not communicate by conformational change. They also show, however, that electron transfer between the reduced disulfide and the heme is feasible. We therefore suggest that the role of ...
One innovative thought in biomolecular electronics is the exploitation of electron transfer proteins. Using natures self assembly techniques, proteins can build highly organized edifices with retained functional activity, and they can serve as platforms for biosensors. In this research work, Yeast Cytochrome C (YCC) is immobilized with a help of a linker molecule, 3-Mercaptopropyltrimethoxysilane (3-MPTS) on a hydroxylated surface of a silicon substrate. Atomic Force Microscopy (AFM) is used for characterization. AFM data shows immobilization of one YCC molecule in between eight grids that are formed by the linker molecules. 3-MPTS monolayers are organized in grids that are 1.2 nm apart. Immobilization of 3-MPTS was optimized using a concentration of 5 mM in a completely dehydrated state for 30 minutes. The functionally active grids of YCC can now be incorporated with Cytochrome C oxidase on a Platinum electrode surface for transfer of electrons in development of biosensors, such as nitrate sensor,
TY - JOUR. T1 - Lack of cytochrome c in mouse fibroblasts disrupts assembly/stability of respiratory complexes I and IV. AU - Vempati, Uma D.. AU - Han, Xianlin. AU - Moraes, Carlos T.. PY - 2009/2/13. Y1 - 2009/2/13. N2 - Cytochrome c (cyt c) is a heme-containing protein that participates in electron transport in the respiratory chain and as a signaling molecule in the apoptotic cascade. Hereweaddressed the effect of removing mammalian cyt c on the integrity of the respiratory complexes in mammalian cells. Mitochondria from cyt c knockout mouse cells lacked fully assembled complexes I and IV and had reduced levels of complex III. Aredox-deficient mutant of cyt c was unable to rescue the levels of complexes I and IV. We found that cyt c is associated with both complex IV and respiratory supercomplexes, providing a potential mechanism for the requirement for cyt c in the assembly/stability of complex IV.. AB - Cytochrome c (cyt c) is a heme-containing protein that participates in electron ...
Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.
Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.
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Overexpression of SOD1 protects vulnerable motor neurons after spinal cord injury by attenuating mitochondrial cytochrome c release ...
The periplasmic nitrite reductase system from Escherichia coli and the extracellular Fe(III) reductase system from Shewanella oneidensis contain multihaem c-type cytochromes as electron carriers and terminal reductases. The position and orientation of the haem cofactors in multihaem cytochromes from different bacteria often show significant conservation despite different arrangements of the polypeptide chain. We propose that the decahaem cytochromes of the iron reductase system MtrA, MtrC and OmcA comprise pentahaem modules similar to the electron donor protein, NrfB, from E. coli. To demonstrate this, we have isolated and characterized the N-terminal pentahaem module of MtrA by preparing a truncated form containing five covalently attached haems. UV-visible spectroscopy indicated that all five haems were low-spin, consistent with the presence of bis-His ligand co-ordination as found in full-length MtrA. ...
Cytochrome C oxidase (COX) is the terminal enzyme of the mitochondrial respiratory chain. It is a multi-subunit enzyme complex that couples the transfer of electrons from cytochrome c to molecular oxygen and contributes to a proton electrochemical gradient across the inner mitochondrial membrane. The complex consists of 13 mitochondrial- and nuclear-encoded subunits. The mitochondrially-encoded subunits perform the electron transfer and proton pumping activities. The functions of the nuclear-encoded subunits are unknown but they may play a role in the regulation and assembly of the complex. This gene encodes the nuclear-encoded subunit Vb of the human mitochondrial respiratory chain enzyme. [provided by RefSeq, Jul 2008 ...
As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
Bionanoprobes were created using cytochromes c isolated from horse heart (HCc) or yeast (YCc); and citrate-stabilized AuNPs. The two cytochromes c generated bionanoprobes with remarkably distinct surface properties. The combination of spectrophotometric pH-titrations and circular dichroism spectroscopy provided information on the protein layer of the bionanoprobes, revealing distinct protonation patterns for the two systems as reflected by its pH-induced aggregation. The YCc bionanoprobe revealed changes in the secondary structure of its protein layer that were practically absent in the protein layer of the HCc bionanoprobes. Atomic force microscopy and dynamic light scattering and determination of -potencial, provided insights on the layer structure and surface coverage and potential. These techniques confirmed a thick protein layer for the YCc bionanoprobe of ca. 4 nm whereas the HCc bionanoprobe presented a protein layer with ca. 2 nm that can be removed by sample drying. The surface potential of
Folding of cytochrome c from its low pH guanidine hydrochloride (Gdn-HCl) denatured state revealed a new intermediate, a five-coordinate high spin species with a water molecule coordinated to the heme. Incorporation of this five-coordinated intermediate into the previously reported ligand exchange model can quantitatively account for the observed folding kinetics. In this new model, unfolded cytochrome c is converted to its native structure through an obligatory folding intermediate, the histidine-water coordination state, whereas the five-coordinate state and a bis-histidine state are off-pathway intermediates. When the concentration of Gdn-HCl in the refolding solution was increased, an acceleration of the conversion from the bis-histidine coordinated state to the histidine-water coordinated state was observed, demonstrating that the reaction requires unfolding of the mis-organized polypeptide structure associated with the bis-histidine state.
Read Preservation of Mitochondrial Structure and Function after Bid- or Bax-Mediated Cytochrome c Release, The Journal of Cell Biology on DeepDyve, the largest online rental service for scholarly research with thousands of academic publications available at your fingertips.
Cytochrome c-2; Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain (By similarity) (112 aa ...
The initial batch of gold-cytochrome solution had a rosy red hue and a pH value of 10--about the same as an over-the-counter heartburn medication. But when drops of hydrochloric acid were added, the solution began to change color, turning purple when the pH reached 5.8 and light blue at pH 4, which is close to the acidity of wine. Lab analysis revealed that additional hydrochloric acid was causing the cytochrome c molecules to unfold. As a result, gold nanoparticles coated with cytochrome c began clumping together--a process that caused the solution to quickly change from red to blue as the acidity increased ...
plant Anti-Cyt c | cytochrome c antibodies, At1g22840,At4g10040, AS08 343, plant cyt c antibodyCytochrome c is located in inner mitochondrial membrane. It is a small heme protein which unlike other cytochromes is highly soluble. This proteinn is an essent
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As Ohios inmate population once again approaches record levels, with no money available for bricks and mortar, prisons chief Gary Mohr is looking at something never used here before - emergency early release of prisoners.
There is no a priori (to imply or indipendent of implications in fact) reason for two different species to have the same, or even mildly similar, cytochrome c protein sequences1In that case, there is no countervailing selection and we see positive values. For the three components which are significantly different for the cytochrome c2.Cytochrome c oxidase « » CytC_oxdse_ I subunit I is the most conserved hence COI, II,( 1.9.3.1 ) III. Theoretically possible is the uncertainty in the experimental ratio null hypothesisof common species descent. Homo sapiens have three genes COI ? coitus interruptus. Where (The floor plate plays important roles) and cubitus interruptus (cI protein), ( ci) prevents multiple phages from infecting a single host , defined as the multiplex syndrome as a clinical frame encompassing an unknown number of genetic and/or nongenetic [barcodes] as nuclear encoded context-dependent positive and negative functions. The results for the second and third codon position that ...
The 10th Nitrogen Cycle Meeting 2004: Focused Meeting held at the University of East Anglia, Norwich, U.K., 2-4 September 2004. Edited by C.S. Butler (Newcastle upon Tyne, U.K.) and D.J. Richardson (Norwich, U.K.). Sponsored by the COST (European Cooperation in the field of Scientific and Technical Research) Office and the ESF (European Science Foundation). ...
1. The intracellular distribution of nitrogen, DPNH cytochrome c reductase, succinic dehydrogenase, and cytochrome c oxidase has been studied in fractions derived by differential centrifugation from rat and guinea pig spleen homogenates.. 2. In the spleens of each species, the nuclear fraction accounted for 40 to 50 per cent of the total nitrogen content of the homogenate, and the mitochondrial, microsome, and supernatant fractions contained about 8, 12, and 30 per cent of the total nitrogen, respectively.. 3. Per mg. of nitrogen, DPNH cytochrome c reductase was concentrated in the mitochondria and microsomes of both rat and guinea pig spleens. Seventy per cent of the total DPNH cytochrome c reductase activity was recovered in these two fractions. The reductase activity associated with the nuclear fraction was lowered markedly by isolating nuclei from rat spleens with the sucrose-CaCl2 layering technique. The lowered activity was accompanied by the recovery of about 90 per cent of the homogenate ...
Definition of cytochrome c reductase. Provided by Stedmans medical dictionary and Drugs.com. Includes medical terms and definitions.
Cytochrome c oxidase subunit 1; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1- 3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B (513 aa ...
Lohmann (1936) pointed out in a recent review that ultimately the energy for the contractile process of muscles is derived in preference from the combustion of carbohydrate. The term combustion of carbohydrate, until recently difficult to define, can now be precisely described. According to Warburg (1935; 1936), its basic feature is the transfer of electrons (or hydrogen atoms) from hexosephosphate to the pyridine ring of the aerobic co-ferment triphosphopyridine nucleotide, and to the anaerobic co-ferment diphosphopyridine nucleotide (co-zymase). These nucleotides transfer the electrons to yellow ferment (flavoprotein), and also to cytochrome c (Theorell, 1936). ...
Targeting mitochondrial cardiolipin and the cytochrome c/cardiolipin complex to promote electron transport and optimize mitochondrial ATP synthesis. Academic Article ...
Cytochrome c oxidase subunit; has a role in assembly of respiratory supercomplexes; similar to Rcf1p, and either Rcf1p or Rcf2p is required for late-stage assembly of the Cox12p and Cox13p subunits and for cytochrome c oxidase activity; associates with the cytochrome c oxidase - cytochrome bc1 supercomplex; null mutant accumulates reactive oxygen species; member of the conserved hypoxia induced gene family; C. elegans homolog is functional in yeast ...
Cytochrome C (Mitochondrial Marker) Antibody, Mouse Monoclonal Antibody [Clone CYCS/1010 ] validated in WB, IHC, IF, FC (AH12101-7), Abgent
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The protein encoded by this gene is an enzyme that covalently links a heme group to the apoprotein of cytochrome c. Defects in this gene are a cause of microphthalmia syndromic type 7 (MCOPS7). Three transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jan 2010 ...
Cytochrome p450 structure mechanism and biochemistry pdf - the structure, mechanism, and biochemistry of cytochrome P enzymes, with Included format: EPUB, PDF; ebooks can be used on all reading devices. Request PDF | Cytochrome P Structure, mechanism, and biochemistry: Third edition | In this third edition of Cytochrome P Structure.
SCO2, 0.1 mg. Synthesis of cytochrome c oxidase 2 was initially identified in yeast as one of two cytochrome c oxidase (COX) assembly proteins that enable the assembly of cytochrome c holoenzyme, a complex that catalyzes the transfer of reducing
With monoclonal antibodies against cytochrome P-450(5) and P-450(4,5,6), 52 and 54 kDa bands are visualized in microsomes from proximal as well as distal human small intestine. These bands most probably correspond to cytochrome P-450(5) and P-450(4), respectively. This and several other cytochrome P …
Cytochrome c; FUNCTIONS IN: electron carrier activity, iron ion binding, heme binding; EXPRESSED IN: 21 plant structures; EXPRESSED DURING: 13 growth stages; CONTAINS InterPro DOMAIN/s: Cytochrome c, class I (InterPro:IPR003088), Cytochrome c domain (InterPro:IPR009056); Has 30201 Blast hits to 17322 proteins in 780 species: Archae - 12; Bacteria - 1396; Metazoa - 17338; Fungi - 3422; Plants - 5037; Viruses - 0; Other Eukaryotes - 2996 (source: NCBI BLink ...
... as well as to describe individual protein-bound heme groups (for example, cytochrome bc, and aa3 complexes, cytochrome b5, heme ... Puustinen A, Wikström M. (1991). "The heme groups of cytochrome o from Escherichia coli". Proc. Natl. Acad. Sci. U.S.A. 88 (14 ... Heme S is related to heme B by having a formal group at position 2 in place of the 2-vinyl group. Heme S is found in the ... Cytochrome a refers to the heme A in specific combination with membrane protein forming a portion of cytochrome c oxidase. The ...
"Our Research , Wilson Tox Lab - Aquatic Toxicology, Cytochrome P450 Enzymes". "Group Photos : Stegeman Laboratory". www.whoi. ... Her research focuses on studying cytochrome P450 enzymes and the effects of environmental contaminants on marine and freshwater ... where she started investigating the roles that different families of cytochrome P450 play in detoxification of various ...
Hill, R.; Bendall, F. (1960). "Function of the Two Cytochrome Components in Chloroplasts: A Working Hypothesis". Nature. 186 ( ... http://robert-hill-institute.group.shef.ac.uk "EC/1946/12 Hill, Robert". London: The Royal Society. Archived from the original ... subscription required) Bendall, D.S. (1971). "[33] Cytochrome components in chloroplasts of the higher plants". Methods in ... and in 1926 he began to work with David Keilin on the haem containing protein cytochrome c. In 1932, he commenced work on plant ...
Nature Publishing Group. Archived from the original on 13 May 2018. Retrieved 18 April 2015. Loose DS, Kan PB, Hirst MA, Marcus ... As with all azole antifungal agents, ketoconazole works principally by inhibiting the enzyme cytochrome P450 14α-demethylase ( ... Ketoconazole was introduced as the prototypical medication of the imidazole group of antifungals. Oral ketoconazole has been ... Dutch South-Eastern Urological Cooperative Group". Urology. 33 (5): 411-5. doi:10.1016/0090-4295(89)90037-X. PMID 2652864. De ...
Enzyme is a member of cytochrome P450 protein family (P450s). It is a very diverse group of heme-containing oxidases, which ... one hydroxyl group in the B-ring) responsible for orange colour and delphinidin type (three hydroxyl groups in the B-ring) ... The main difference in the structure of listed anthocyanins type is the number of hydroxyl groups in the B-ring of the ... We can diversify three main classes of anthocyanin pigments: cyaniding type (two hydroxyl groups in the B-ring) responsible for ...
... is an important precursor to biologically essential prosthetic groups such as heme, cytochrome c, and ... two vinyl groups −CH=CH 2 (V), and two propionic acid groups −CH 2−CH 2−COOH (P). The Roman numeral "IX" indicates that these ... Hemes are prosthetic groups in some important proteins. These heme-containing proteins include hemoglobin, myoglobin, and ... cytochrome c. Complexes can also be formed with other metal ions, such as zinc. The compound is synthesized from acyclic ...
The CYP3A group of enzymes are the most abundantly expressed members of the cytochrome P450 family in liver. They are ... CYP3A7 is an enzyme belonging to the cytochrome P450 family. It is 503 amino acids in size and shares 87% of its sequence with ... "Cytochrome P450, Subfamily IIIA, Polypeptide 7". OMIM. Retrieved March 14, 2013. CS1 maint: discouraged parameter (link) ... "Molecular cloning and sequence analysis of cDNA containing the entire coding region for human fetal liver cytochrome P-450". J ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with NAD+ or NADP+ ... This enzyme participates in metabolism of xenobiotics by cytochrome p450. As of late 2007, 14 structures have been solved for ...
C-type cytochromes was found in cells. Pelobacter is unique group of fermentative microorganisms belonging to the class of ... Wolin MJ, Wolin EA, Jacobs NJ (June 1961). "Cytochrome-producing anaerobic Vibrio succinogenes, sp. n". Journal of Bacteriology ... June 2018). "Expanded diversity of microbial groups that shape the dissimilatory sulfur cycle". The ISME Journal. 12 (7): 1715- ... The Gammaproteobacteria class include several medically, ecologically and scientifically important groups of bacteria. They are ...
Cytochrome P450 2B6 is an enzyme that in humans is encoded by the CYP2B6 gene. CYP2B6 is a member of the cytochrome P450 group ... This gene, CYP2B6, encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are ... Both the gene and the pseudogene are located in the middle of a CYP2A pseudogene found in a large cluster of cytochrome P450 ... "Entrez Gene: cytochrome P450". Center for Drug Evaluation and Research. "Drug Interactions & Labeling - Drug Development and ...
Hydroperoxides are highly reactive functional groups since they contain an oxidant (O-O bond) adjacent to a reductant (C-H ... They belong to the cytochrome P450 enzyme family (CYP74C and CYP74B). Polyunsaturated fatty acids such as linolenic and ... Noordermeer MA, Veldink GA, Vliegenthart JF (2001). "Fatty acid hydroperoxide lyase: a plant cytochrome p450 enzyme involved in ...
It has 2 cofactors: FAD, and Cytochrome c. As of late 2007, 4 structures have been solved for this class of enzymes, with PDB ... This enzyme belongs to the family of oxidoreductases, specifically those acting on CH or CH2 groups with other acceptors. The ...
... is a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases ... The enzyme catalyzes sequential hydroxylations of the steroid angular methyl group at C18 after initial 11β-hydroxylation (the ... Here are some of the substrates, grouped by catalytic activity of the enzyme: strong: 11-deoxycorticosterone to corticosterone ... November 1990). "Cloning and expression of a cDNA for human cytochrome P-450aldo as related to primary aldosteronism". ...
... s are proteins that contain one or more copper ions as prosthetic groups. Copper proteins are found in all forms ... A prominent copper proteins in humans is in cytochrome c oxidase (cco). The enzyme cco mediates the controlled combustion that ... Copper B centres (CuB) are found in cytochrome c oxidase. The copper atom is coordinated by three histidines in trigonal ... are found in cytochrome c oxidase and nitrous-oxide reductase (EC 1.7.99.6). The two copper atoms are coordinated by two ...
1] Potent inhibition of human cytochrome P450 3A isoforms by cannabidiol: Role of phenolic hydroxyl groups in the resorcinol ... This gene is part of a cluster of cytochrome P450 genes on chromosome 7q22.1. CYP3A4 is a member of the cytochrome P450 ... "In vitro evaluation of valproic acid as an inhibitor of human cytochrome P450 isoforms: preferential inhibition of cytochrome ... Cytochrome P450 3A4 (abbreviated CYP3A4) (EC 1.14.13.97) is an important enzyme in the body, mainly found in the liver and in ...
For example, it affects heme and cytochrome P450, and decreases their effectiveness. Organotin compounds can be very toxic. " ... "Tri-n-alkyltins" are phytotoxic and, depending on the organic groups, can be powerful bactericides and fungicides. Other ... CS1 maint: discouraged parameter (link) Westrum, Bente; Thomassen, Yngvar (2002). The Nordic Expert Group for Criteria ...
The final step was to remove the iodine protective group via Pd(OAc)2 to ultimately produce bergapten (product 9) with 90% ... Bergapten, alongside other furanocoumarins, has also been implicated in Cytochrome P450 inhibition. Bergapten is a natural ... The synthesis described here involves Iodine as a removable group to insure regiochemical integrity and convergence. As shown ...
Cytochromes are conjugate proteins that contain a haem group. The iron atom from this group undergoes redox reactions: Fe 3 ...
... as well as to describe individual protein-bound heme groups (for example, cytochrome bc, and aa3 complexes, cytochrome b5, heme ... Heme S is related to heme B by having a formal group at position 2 in place of the 2-vinyl group. Heme S is found in the ... Cytochrome a refers to the heme A in specific combination with membrane protein forming a portion of cytochrome c oxidase.[13] ... The names of cytochromes typically (but not always) reflect the kinds of hemes they contain: cytochrome a contains heme A, ...
A polymer formed from epoxide precursors is called an epoxy, but such materials do not contain epoxide groups (or contain only ... They arise usually via oxygenation of alkenes by the action of cytochrome P450. (but see also the short-lived ... This carbanion then attacks the same oxygen atom, displacing a leaving group from it, to close the epoxide ring. Epoxides are ... In this reaction, a sulfonium is the leaving group instead of chloride. Electron-deficient olefins, such as enones and acryl ...
Like other cytochrome P450 enzymes, 21-hydroxylase participates in the cytochrome P450 catalytic cycle and engages in one- ... The iron(III) heme group that defines the active site resides in the center of each subunit. The human enzyme binds one ... The enzyme is a member of the cytochrome P450 superfamily of monooxygenase enzymes. The cytochrome P450 enzymes catalyze many ... This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which ...
... the copper ions and the closely associated protein cytochrome c. Both the formyl group and the isoprenoid side chain are ... as published by the influential group of S. Yoshikawa. Heme Hemoprotein Cytochrome c oxidase (Complex IV of cellular ... the iron-free prosthetic group of cytochrome c oxidase". Journal of the Chemical Society, Perkin Transactions 1: 135. doi: ... Heme A is similar to heme o, in that both have this farnesyl addition at position 2 but heme O does not have the formyl group ...
For the hydroxylation, the cytochrome p450 enzyme complex is suggested to be involved. T-2 triol and T-2 tetraol are most ... This compound has an epoxide ring, and several acetyl and hydroxyl groups on its side chains. These features are mainly ... In vivo studies showed that the most occurring reactions are ester hydrolysis and hydroxylation of the isovaleryl group. ... The mycotoxin T-2 inhibits hepatic cytochrome P4503A activity in pigs. Food and Chemical Toxicology 2013, 57, 54-6. Bamburg, J. ...
Clenbuterol (CLEN) was attached to BSA molecules through amide bond, between the carboxylic group of BSA and the amine group of ... Then Thrombin is co-injected with excess of cytochrome C for signal specificity. Concentration of free thrombin is determined ... Hence, thiols groups have to be introduced at the terminals of dendrimers so that dendrimers can be attached on the gold ... Functional groups (amide, amino and carboxyl) act as ionic pumps capturing calcium ions from the test fluids; then calcium ...
... and cytochrome Cc1 haem-lyase (CC1HL) are mitochondrial enzymes that catalyse the covalent attachment of a haem group on two ... The human enzyme, HCCS, processes both cytochromes c and c1. Zollner A, Rodel G, Haid A (August 1992). "Molecular cloning and ... Dumont ME, Ernst JF, Hampsey DM, Sherman F (1987). "Identification and sequence of the gene encoding cytochrome c heme lyase in ... Other names in common use include cytochrome c heme-lyase, holocytochrome c synthetase, and holocytochrome-c apocytochrome-c- ...
First, the 3β-hydroxyl group is oxidized to a keto group and second, the double bond is moved to C4, from C5 through a keto/ ... In addition, progesterone can be hydroxylated in the liver by other cytochrome P450 enzymes which are not steroid-specific. 6β- ... It has a double bond (4-ene) between the C4 and C5 positions and two ketone groups (3,20-dione), one at the C3 position and the ... It belongs to a group of steroid hormones called the progestogens, and is the major progestogen in the body. Progesterone has a ...
Various revolutionary anarchist groups adopted the bird's name, either as a group identifier, as in the Spanish Civil War, or ... ISBN 978-84-87334-10-8. Nunn, G.B.; Stanley, S.E. (1998). "Body size effects and rates of cytochrome b evolution in tube-nosed ... The family is an ancient group of small species that is thought to have diverged early from the rest of the tubenoses; the ... Erratum: Nunn, G.B.; Stanley, S.E. (2000). "Corrigendum for: Body size effects and rates of cytochrome b evolution in tube- ...
Metabolism of the methylenedioxy group to a carbene allows the molecule to form ligand complexes with cytochrome P450 and P448 ... It remained to be determined whether the molecule's C3H5 group was a propenyl group (R−CH=CH−CH3) or an allyl group (R−CH2−CH= ... The allyl group thus directly contributes to mutagenicity, while the methylenedioxy group is associated with changes in the ... determined that the C3H5 group was an allyl group. Safrole is the principal component of brown camphor oil made from Ocotea ...
These group-transfer intermediates are called coenzymes. Each class of group-transfer reactions is carried out by a particular ... The electrons then flow to the cytochrome b6f complex, which uses their energy to pump protons across the thylakoid membrane in ... The oxidation pathway starts with the removal of the amino group by a transaminase. The amino group is fed into the urea cycle ... to an acceptor hydroxyl group on the growing polysaccharide. As any of the hydroxyl groups on the ring of the substrate can be ...
The dihaem cytochrome folds into two domains, each of which resembles mitochondrial cytochrome c, with the two haem groups ... Electrons are transferred from the flavin to one of the haem groups in the cytochrome. Both FAD and heme C are covalently bound ... roles of cytochrome c-551 and cytochrome c-553". Biochimica et Biophysica Acta (BBA) - Bioenergetics. 325 (2): 304-14. doi: ... and a dihaem cytochrome (fccA; Q06529) that carry out hydrogen sulfide-dependent cytochrome C reduction. ...
UDCA-PBC Study Group". N. Engl. J. Med. 324 (22): 1548-54. doi:10.1056/NEJM199105303242204. PMID 1674105.. ... via cytochrome P450-mediated oxidation of cholesterol in a multi-step process. Approximately 600 mg of bile salts are ... The hydroxyl groups can be in either of two configurations: either up (or out), termed beta (β; often drawn by convention as a ... The British-Italian Gallstone Study group". Aliment. Pharmacol. Ther. 15 (1): 123-8. doi:10.1046/j.1365-2036.2001.00853.x. PMID ...
Females do not seem to be territorial outside the breeding season and can be seen in small groups, although individual deer do ... studies of mitochondrial control region and cytochrome b DNA sequences placed it near Capreolus within an Old World section of ... "New phylogenetic perspectives on the Cervidae (Artiodactyla) are provided by the mitochondrial cytochrome b gene". Proceedings ...
At the left is the N-terminus, with its amino (H2N) group in green. The blue C-terminus, with its carboxyl group (CO2H) is at ... A protein kinase drifting around on the outer chloroplast membrane can use ATP to add a phosphate group to the Toc34 protein, ... are often the amino acids that accept the phosphate group.[43][45] The enzyme that carries out the phosphorylation is specific ... or add a phosphate group to many (but not all) of them in their transit sequences.[38] Serine and threonine (both very common ...
The two cyano groups are bonded together at their carbon atoms: N≡C−C≡N, although other isomers have been detected.[6] The name ... Like other cyanides, cyanogen is very toxic, as it readily undergoes reduction to cyanide, which poisons the cytochrome c ... Cyanogen molecules consist of two CN groups - analogous to diatomic halogen molecules, such as Cl2, but far less oxidizing. ...
A mitochondrial cytochrome b phylogeny of cardueline finches. Journal für Ornithologie, 135: 31. ... "Mitochondrial DNA Phylogenetic Definition of a Group of 'Arid-Zone' Carduelini Finches" (PDF). Open Ornithology Journal 1: 1-7 ...
However, at 12-month follow-up the difference between the placebo group and the moclobemide group was no longer significant.[42 ... August 1996). "The role of cytochrome P450 2D6 in the metabolism of moclobemide". European Neuropsychopharmacology. 6 (3): 225- ... Danish University Antidepressant Group". Br J Clin Pharmacol. 35 (6): 649-52. doi:10.1111/j.1365-2125.1993.tb04196.x. PMC ... Danish University Antidepressant Group". J Affect Disord. 28 (2): 105-16. June 1993. doi:10.1016/0165-0327(93)90039-M. PMID ...
The detoxification enzymes cytochrome P450 1A1 (CYP1A1) and cytochrome P450 1B1 (CYP1B1) are both protective and necessary for ... It is listed as a Group 1 carcinogen by the IARC. In the 18th century a scrotal cancer of chimney sweepers, the chimney sweeps ... BaP induces cytochrome P4501A1 (CYP1A1) by binding to the AHR (aryl hydrocarbon receptor) in the cytosol.[28] Upon binding the ... Benzo[a]pyrene is first oxidized by cytochrome P450 1A1 to form a variety of products, including (+)benzo[a]pyrene-7,8-epoxide. ...
As a group, minerals are one of the four groups of essential nutrients, the others of which are vitamins, essential fatty acids ... Required component of many redox enzymes, including cytochrome c oxidase Liver, seafood, oysters, nuts, seeds; some: whole ...
Groups consist of females with calves, or of up to six subadults. Such groups congregate at wallows and grazing areas. They are ... based on mitochondrial cytochrome b and 12s rRNA genes". Molecular Phylogenetics and Evolution. 19 (1): 34-44. doi:10.1006/mpev ... Kathmandu: Wildlife Watch Group. ISBN 978-99946-820-9-6. .. External links[edit]. Wikispecies has information related to ... Groups of up to 10 rhinos may gather in wallows-typically a dominant male with females and calves, but no subadult males.[15] ...
1. Hamlyn Publishing Group.. ,volume=. has extra text (help) *^ Smárason, Hjörtur (29 March 2011). "World's Largest White- ... Evolutionary history of New and Old World vultures inferred from nucleotide sequences of the mitochondrial cytochrome b gene. ... Ridgway, R., & Friedmann, H. (1919). The birds of North and Middle America: a descriptive catalogue of the higher groups, ... The latter group, comprised by the lesser (Haliaeetus humilis) and the grey-headed fish eagle (Haliaeetus ichthyaetus), differ ...
transferase activity, transferring acyl groups other than amino-acyl groups. • enoyl-CoA hydratase activity. • long-chain-3- ... Cytochrome b6f complex. *Electron transport chain. *Fatty acid synthetase complex. *Glycine decarboxylase complex ... transferase activity, transferring acyl groups. • 3-hydroxyacyl-CoA dehydrogenase activity. • RNA binding. • acetyl-CoA C- ... The HADHB protein catalyzes the final step of beta-oxidation, in which 3-ketoacyl CoA is cleaved by the thiol group of another ...
... contains a loosely bound FAD flavin and obtains electrons from NADPH-cytochrome P450 reductase, rather ... differs from other flavin monooxygenases in that the oxygen is inserted as an epoxide rather than as a hydroxyl group. ...
"Agreement on the Conservation of Polar Bears". Oslo, Norway: IUCN/ Polar Bear Specialist Group. 1973. Archived from the ... Phylogenetic relationships of artiodactyls and cetaceans as deduced from the comparison of cytochrome b and 12S rRNA ... and the remarkable promise of cytochrome b to provide reliable species-level phylogenies". Molecular Phylogenetics and ...
Hydrogen sulfide is also a potent cellular toxin, blocking the cytochrome system and inhibiting cellular respiration. More ... Phosgene directly reacts with amine, sulfhydryl, and alcohol groups, adversely affecting cell macromolecules and metabolism. ...
The dimethylallyl group in 7 then undergoes cyclization with the phenol group to give 8. This transformation is catalysed by a ... cytochrome P-450-dependent monooxygenase17 (psoralen 5-monooxygenase), and cofactors (NADPH) and molecular oxygen.[19] ... The aromatic ring in 6 is activated at positions ortho to the hydroxyl group, and is alkylated by 5, an alkylating agent. ...
This enzyme belongs to the superfamily of short-chain oxidoreductases, specifically those acting on the CH-OH group of donor ... 1.1.2: cytochrome acceptor. *D-lactate dehydrogenase (cytochrome). *D-lactate dehydrogenase (cytochrome c-553) ...
... is an important precursor to biologically essential prosthetic groups such as heme, cytochrome c, and ... These heme-containing proteins include hemoglobin, myoglobin, and cytochrome c. Complexes can also be formed with other metal ... Hemes are prosthetic groups in some important proteins. ...
Watanabe K, Yamaori S, Funahashi T, Kimura T, Yamamoto I (March 2007). "Cytochrome P450 enzymes involved in the metabolism of ... THC, as well as other cannabinoids that contain a phenol group, possesses mild antioxidant activity sufficient to protect ... Metabolism occurs mainly in the liver by cytochrome P450 enzymes CYP2C9, CYP2C19, CYP2D6, and CYP3A4.[28][29] More than 55% of ...
They are able to leap a distance of some 50 times their body length, a feat second only to jumps made by another group of ... cytochrome oxidase II, and elongation factor 1-alpha) for 128 flea taxa from around the world. The Boreidae (snow scorpionflies ... One of the seven orders into which he divided them was "Aptera", meaning wingless, a group in which as well as fleas, he ... Fleas normally specialise in one host species or group of species, but can often feed but not reproduce on other species. ...
The final step was to remove the iodine protective group via Pd(OAc)2 to ultimately produce bergapten (product 9) with 90% ... Bergapten, alongside other furanocoumarins, has also been implicated in Cytochrome P450 inhibition.[12] ... The synthesis described here involves Iodine as a removable group to insure regiochemical integrity and convergence.[13] As ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ ... 1.1.2: cytochrome acceptor. *D-lactate dehydrogenase (cytochrome). *D-lactate dehydrogenase (cytochrome c-553) ...
The division into two groups is based on Turner et al. (2017). "Red leg" group = Brachypelma sensu stricto Brachypelma albiceps ... In this approach, a portion of about 650 base pairs of the mitochondrial gene cytochrome oxidase I (COI) is used, primarily to ... B. kahlenbergi is one of the smaller species, with body lengths around 30-40 mm (1 1⁄4-1 1⁄2 in). The "red leg" group contains ... All the species in the cladogram below belong to the "red leg" group. In 2017, Steven Turner and colleagues reported on a ...
A group of other ERα agonists that included ethinylestradiol, diethylstilbestrol, tamoxifen, clomifene, and raloxifene were ... Cytochrome P450 oxidoreductase deficiency. *Cytochrome b5 deficiency. *Androgen-dependent condition. *Aromatase deficiency ... the C3 and C17 hydroxyl groups of estradiol are anchored by the Glu353 and Arg394, and His524 residues of the ERα protein, ...
Often grouped under the labels of compassionate use, expanded access, or named patient supply, these programs are governed by ... SuperCYP: Database for Drug-Cytochrome- and Drug-Drug-interactions. Retrieved from "https://en.wikipedia.org/w/index.php?title= ... In the United States, ACT UP formed in the 1980s, and eventually formed its Treatment Action Group in part to pressure the US ... Drug use among elderly Americans has been studied; in a group of 2377 people with average age of 71 surveyed between 2005 and ...
Group B). Mean milk volumes at the beginning of the intervention were similar between the 2 groups. After the first 14 days, 78 ... Simard, C.; Michaud, V.; Gibbs, B.; Massé, R.; Lessard, É; Turgeon, J. (2008). "Identification of the cytochrome P450 enzymes ... DOM-USA-5 Study Group". Clinical Therapeutics. 20 (3): 438-53. doi:10.1016/S0149-2918(98)80054-4. PMID 9663360.. ... EMPOWER Study Collaborative Group) (2017). "Enhancing human milk production with Domperidone in mothers of preterm infants". ...
The known vectors belong to the genus Anopheles, subgenus Cellia, series Neomyzomyia and group Leucosphyrus.[4] Mosquitoes of ... J. Schall (2002). "A molecular phylogeny of malarial parasites recovered from cytochrome b gene sequences". Journal of ... this group are typically found in forest areas in South East Asia but with a greater clearing of forest areas for farmland, ...
Northeast Pacific resident groups tend to be much more vocal than transient groups in the same waters.[146] Residents feed ... Air pollutants that bind with exhaust fumes are responsible for the activation of the cytochrome P450 1A gene family.[227] ... Offshores typically congregate in groups of 20-75, with occasional sightings of larger groups of up to 200.[30] Little is known ... Groups even attack larger cetaceans such as minke whales, grey whales,[116] and, rarely, sperm whales or blue whales.[34][117][ ...
The final phase of testing began on 27 July with up to 30,000 volunteers assigned to one of two groups - one receiving the mRNA ... 1950s - Julius Axelrod discovered a new class of enzymes, cytochrome P450 monooxygenases, a fundamental of drug metabolism. ... On February 13, 2012, the National Institutes of Health (NIH) announced a new group of individuals assigned to research pain. ... and individuals have formed patient advocacy groups to represent their own interests.[57] ...
Meeting of the Ad Hoc Working Group on West African Coastal Pelagic Fish from Mauritania to Liberia (26gr N to 5gr N). Dakar ( ... Using mitochondrial cytochrome b sequences, the species (which was labelled Decapterus rhoncus) was found to be strongly ... The false scad is classified within the genus Caranx, one of a number of groups known as the jacks or trevallies. Caranx itself ... based on mitochondrial cytochrome b sequences using parsimony, likelihood, and Bayesian approaches". Molecular Phylogenetics ...
... s should be applied only when absolutely necessary, especially if they are in an at-risk group. Lowering the amount of ... Sierotzki, Helge (2000) Mode of resistance to respiration inhibitors at the cytochrome bc1 enzyme complex of Mycosphaerella ... Fungicide Resistance Action Group, United Kingdom. *General Pesticide Information - National Pesticide Information Center, ... cytochrome b.[16] It is presumed that this disrupts the binding of the fungicide to the protein, rendering the fungicide ...
"Cytochrome b Group" by people in this website by year, and whether "Cytochrome b Group" was a major or minor topic of these ... "Cytochrome b Group" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ... Cytochromes (electron-transporting proteins) with protoheme (HEME B) as the prosthetic group. ... Below are the most recent publications written about "Cytochrome b Group" by people in Profiles. ...
Haem a compounds as models for cytochromes of group a III. Schiffs bases of haem a and other formylhaems and formyl-porphyrins ... Haem a compounds as models for cytochromes of group a III. Schiffs bases of haem a and other formylhaems and formyl-porphyrins ... Haem a compounds as models for cytochromes of group a III. Schiffs bases of haem a and other formylhaems and formyl-porphyrins ... Haem a compounds as models for cytochromes of group a III. Schiffs bases of haem a and other formylhaems and formyl-porphyrins ...
... complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ... Component of the ubiquinol-cytochrome c reductase complex ( ... Protein family/group databases. TCDBi. 3.E.2.1.1, the ... Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory ... cd00290, cytochrome_b_C, 1 hit. cd00284, Cytochrome_b_N, 1 hit. ...
... cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons ... Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons ... The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c ... The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the ...
It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.,p>,a href=/help ... Cytochrome b-245 heavy chainAdd BLAST. 570. Amino acid modifications. Feature key. Position(s). DescriptionActions. Graphical ... Cytochrome b-245 heavy chain (EC:1.-.-.-*Search proteins in UniProtKB for this EC number. ... sp,Q61093,CY24B_MOUSE Cytochrome b-245 heavy chain OS=Mus musculus OX=10090 GN=Cybb PE=1 SV=1 ...
Four types of cytochromes are distinguished by their prosthetic groups: There is no "cytochrome e," but cytochrome f, found in ... cytochromes b, cytochromes c and cytochrome d. Cytochrome function is linked to the reversible redox change from ferrous (Fe(II ... Cytochrome+c+Group at the US National Library of Medicine Medical Subject Headings (MeSH). Murshudov, G.; Grebenko, A.; Barynin ... Several kinds of cytochrome exist and can be distinguished by spectroscopy, exact structure of the heme group, inhibitor ...
Cytochrome c oxidases (Cox) are among these metalloproteins whose assembly and activity involves incorporation of Cu cofactor ... Characterization of these mutants by genetic complementations revealed mutations in cytochrome c maturation (CCM) genes. These ... mutations are not directly involved in the Cu trafficking to CcoN but involved in the production of membrane bound cytochrome c ... Cytochrome c oxidases (Cox) are among these metalloproteins whose assembly and activity involves incorporation of Cu cofactor ...
"ortholog_gene_1537[group]". National Center for Biotechnology Information. U.S. National Library of Medicine. Retrieved 2016-07 ... Cytochrome c1 belongs to the cytochrome c family of proteins. Cytochrome C1 plays a role in the electron transfer during ... the cytochrome b-c1 complex bears extensive analogy to the cytochrome b6f complex of chloroplasts and cyanobacteria; cytochrome ... Cytochrome C1 (also known as Complex III subunit 4) is a protein encoded by the CYC1 gene. Cytochrome is a heme-containing ...
Group. Score. Points. 1. Paulo Roque 117 4648 Go Science. 8,843. 100. ...
Nature Publishing Group. Other Literature Sources. *Cited by Patents in - The Lens ... We have used a full length cDNA clone (2.2 kb) for the human cytochrome P-450 nifedipine oxidase (CYP3A4) enzyme as a probe to ... Assignment of the human cytochrome P-450 nifedipine oxidase gene (CYP3A4) to chromosome 7 at band q22.1 by fluorescence in situ ...
Structure at 2.7 Angstrom Resolution of the Paracoccus Denitrificans two-subunit Cytochrome C Oxidase Complexed with an ... Sub Group: Electron Transport Chain Complexes: Complex IV (Cytochrome C Oxidase). Protein: Cytochrome C Oxidase, aa3. ... Sub Group: Electron Transport Chain Complexes: Complex IV (Cytochrome C Oxidase). Protein: Cytochrome C Oxidase, aa3. ... Sub Group: Electron Transport Chain Complexes: Complex IV (Cytochrome C Oxidase). Protein: Cytochrome C Oxidase, aa3. ...
Space Group: P 65 2 2. Unit Cell:. Length ( Å ). Angle ( ˚ ). ... The gene encoding the cytochrome P450 CYP121 is essential for ... Cytochrome P450 121. A. 396. Mycobacterium tuberculosis. Mutation(s): 0 EC: 1.14 (PDB Primary Data), 1.14.19.70 (UniProt). ... Identification and structural basis of the reaction catalyzed by CYP121, an essential cytochrome P450 in Mycobacterium ... The gene encoding the cytochrome P450 CYP121 is essential for Mycobacterium tuberculosis. However, the CYP121 catalytic ...
The peroxo group formed in step 4 is rapidly protonated twice, releasing one molecule of water and forming the highly reactive ... Cytochrome P450 oxidoreductase deficiency. References[edit]. *^ Gonzalez FJ, Gelboin HV (November 1992). "Human cytochromes ... Cytochrome P450cam (CYP101) originally from Pseudomonas putida has been used as a model for many cytochromes P450 and was the ... Wikimedia Commons has media related to Cytochrome P450.. *. Preissner S (2010). "Cytochrome P450 database". Nucleic Acids ...
... the heme group is in green. Ribbon representations of cyt b5 (B) and ferricyt c (D) show the buried residues affected upon the ... Protein-protein docking simulations have been performed for the binary cytochrome b5-cytochrome c and ternary (cytochrome b5)-( ... The orientations of cytochrome c in the highly dynamic complex with cytochrome b5 visualized by NMR and docking using HADDOCK. ... The orientations of cytochrome c in the highly dynamic complex with cytochrome b5 visualized by NMR and docking using HADDOCK ...
Cytochrome P450 oxidoreductase deficiency is a disorder of hormone production. Explore symptoms, inheritance, genetics of this ... This group of hormones includes testosterone. and estrogen, which are essential for normal sexual development and reproduction ... The breakdown of retinoic acid requires cytochrome P450 oxidoreductase; if a shortage of cytochrome P450 oxidoreductase ... Cytochrome P450 oxidoreductase deficiency is caused by mutations in the POR gene. This gene provides instructions for making ...
Three subunits have prosthetic groups. The cytochrome b subunit has two b-type hemes (bL and bH), the cytochrome c subunit has ... Cytochrome c1 transfers its electron to cytochrome c (not to be confused with cytochrome c1), and the BH Heme transfers its ... It has four cofactors: cytochrome c1, cytochrome b-562, cytochrome b-566, and a 2-Iron ferredoxin of the Rieske type. The ... mtDNA encoded cytochrome b; mutations associated with exercise intolerance CYC1:cytochrome c1 CYCS: cytochrome c UQCRFS1: ...
... groups I-V, each of which may contain more than one cytochrome P450 family (eg, CYP1 and CYP2 are both found in group I). The ... Cytochrome P450 (IPR001128) *Cytochrome P450, B-class (IPR002397). *Cytochrome P450, E-class, CYP24A, mitochondrial (IPR002949) ... Cytochrome P450 proteins can also be grouped by two different schemes. One scheme was based on a taxonomic split: class I ( ... Cytochrome P450 (IPR001128). Short name: Cyt_P450 Overlapping homologous superfamilies *Cytochrome P450 superfamily (IPR036396) ...
Cytochrome P450 (IPR001128)*Cytochrome P450, E-class, group I (IPR002401). Homologous superfamilies. ...
... a novel 130 kd protein from HeLa cell cytosol that participates in the cytochrome c-dependent activation of caspase-3. The NH2- ... Cytochrome c Group / metabolism* * Cytosol / metabolism * DNA, Complementary * Enzyme Activation * Enzyme Precursors / ... Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3 Cell. ... Cytochrome c binds to Apaf-1, an event that may trigger the activation of caspase-3, leading to apoptosis. ...
... and complex III deficiency in skeletal muscle had a missense mutation in the cytochrome b gene of mitochondrial DNA (G15762A). ... Cytochrome b Group / genetics* * DNA, Mitochondrial / genetics* * Electron Transport Complex III / deficiency ... Missense mutation in the mtDNA cytochrome b gene in a patient with myopathy Neurology. 1998 Nov;51(5):1444-7. doi: 10.1212/wnl. ... and complex III deficiency in skeletal muscle had a missense mutation in the cytochrome b gene of mitochondrial DNA (G15762A). ...
African Ancestry Continental Group. Cytochrome a. Cytochrome a Group. Cytochromes a. Mannosidosis. alpha-Mannosidosis. ... For 2003 the MeSH heading Actinobacteria Group was deleted and all occurrences of that term in MEDLINE were replaced by the new ... Blacks was a 2003 MeSH Heading that became an entry term to the new 2004 heading African Continental Ancestry Group, but all ... The old heading, Actinobacteria Group, was not retained as an entry term so beginning with the 2003 version of PubMed, that ...
Time Course of Cytochrome c Release. Rats were divided into six groups (n = 3 rats per group) that were defined as preinjury, ... and 8 sections per group for a total of 3.84 million pixels per group) of each group, plotted against luminosity units (x axis ... We first evaluated cytochrome c release at the injury epicenter after a T10 contusive SCI in rats. Cytochrome c release peaked ... For each group, spinal tissue from T9-T11 segments [with the injured group receiving a T10 contusive SCI (10 g × 12.5 mm)] was ...
A group of evolutionary biologists sees evidence for a hologenome. Others dismiss it entirely. One things certain: The debate ... P-glycoprotein: a major determinant of rifampicin-inducible expression of cytochrome P4503A in mice and humans. E G Schuetz, A ... P-glycoprotein: a major determinant of rifampicin-inducible expression of cytochrome P4503A in mice and humans ... P-glycoprotein: a major determinant of rifampicin-inducible expression of cytochrome P4503A in mice and humans ...
They were grouped into two main clusters. The first cluster consisted of Aceh, North Toraja, West Nusa Tenggara, Banten, Kolaka ... The cytochrome b gene sequence and genetic variation parameters were analyzed in MEGA software (ver 6), and DnaSP software (ver ... Genetic Variation of Eight Indonesian Swamp-Buffalo Populations Based on Cytochrome b Gene Marker *M. Rusdin, ... The results of the study were concluded that eight Indonesian local swamp-buffalo populations were grouped into two main ...
Cytochrome c Group / physiology. HIV Envelope Protein gp120 / physiology*. HIV Infections / pathology, virology*. HIV-1 / ... 0/Antigens, CD95; 0/Cytochrome c Group; 0/HIV Envelope Protein gp120; 0/Receptors, CXCR4 ... Binding of human immunodeficiency virus type 1 gp120 to CXCR4 induces mitochondrial transmembrane depolarization and cytochrome ... triggers a rapid dissipation of the mitochondrial transmembrane potential resulting in the cytosolic release of cytochrome c ...
Upon incubation of detergent-solubilized NADPH-cytochrome P-450 reductase and either cytochrome b5 or cytochrome c in the ... Cytochrome P-450 Enzyme System / metabolism. Cytochrome b Group / metabolism. Cytochrome c Group / metabolism. Cytochromes b5. ... 0/Cross-Linking Reagents; 0/Cytochrome b Group; 0/Cytochrome c Group; 0/Liposomes; 146-17-8/Flavin Mononucleotide; 1892-57-5/ ... Upon incubation of detergent-solubilized NADPH-cytochrome P-450 reductase and either cytochrome b5 or cytochrome c in the ...
Cytochrome b6f complex. The 220 kDa dimeric cytochrome b6f complex of oxygenic photosynthesis provides the electronic ... The nucleophilic attack results in transfer of the phosphoryl group directly to the metal center. This mechanism has been ... Some other proteins in this class include tetraheme cytochrome c554, fumarate reductase, pentaheme nitrite reductase, and ... groups, three hemes (f, two hemes b, bp and bn), one [2Fe-2S] cluster, and one molecule each of chlorophyll-a and carotene. ...
Drug group. Pharmacological action?. Actions. Details. DB03317. Heme C. experimental. unknown. Details. ... Cytochrome c7. Gene Name. cyd. Organism. Desulfuromonas acetoxidans. Amino acid sequence. ,lcl,BSEQ0016972,Cytochrome c3 ... Ambler RP: The amino acid sequence of cytochrome c-551.5 (Cytochrome c(7)) from the green photosynthetic bacterium ... Assfalg M, Banci L, Bertini I, Bruschi M, Turano P: 800 MHz 1H NMR solution structure refinement of oxidized cytochrome c7 from ...
Drug group. Pharmacological action?. Actions. Details. DB03317. Ferroheme C. experimental. unknown. Details. ... Cytochrome c3, 13 kDa. Details. Name. Cytochrome c3, 13 kDa. Synonyms. Not Available. Gene Name. Not Available. Organism. ... Haser R, Pierrot M, Frey M, Payan F, Astier JP, Bruschi M, Le Gall J: Structure and sequence of the multihaem cytochrome c3. ... Pierrot M, Haser R, Frey M, Payan F, Astier JP: Crystal structure and electron transfer properties of cytochrome c3. J Biol ...
  • Many hydroxylation reactions (insertion of hydroxyl groups) use CYP enzymes. (wikipedia.org)
  • Cytochrome P450 enzymes are a superfamily of haem-containing mono-oxygenases that are found in all kingdoms of life, and which show extraordinary diversity in their reaction chemistry. (ebi.ac.uk)
  • Cytochrome P450 enzymes use haem to oxidise their substrates, using protons derived from NADH or NADPH to split the oxygen so a single atom can be added to a substrate. (ebi.ac.uk)
  • Organisms produce many different cytochrome P450 enzymes (at least 58 in humans), which together with alternative splicing can provide a wide array of enzymes with different substrate and tissue specificities. (ebi.ac.uk)
  • The class E enzymes can be further subdivided into five sequence clusters, groups I-V, each of which may contain more than one cytochrome P450 family (eg, CYP1 and CYP2 are both found in group I). The divergence of the cytochrome P450 superfamily into B- and E-classes, and further divergence into stable clusters within the E-class, appears to be very ancient, occurring before the appearance of eukaryotes. (ebi.ac.uk)
  • Cytochrome P450--redox partner fusion enzymes. (ebi.ac.uk)
  • A large group of xenobiotic-metabolizing enzymes (XMEs), like the cytochrome P450 monooxygenases (CYPs), esterases and transferases, are extremely indicated in mammalian olfactory mucosa (OM). (themodernsolution.com)
  • Initial, stage I enzymes (e.g., cytochrome P450 monooxygenases (CYPs), carboxylesterases, etc.) functionalize xenobiotics by developing polar metabolites. (themodernsolution.com)
  • In human, induction of cytochrome P450 (CYP) family of enzymes is well documented. (bmj.com)
  • Genetic Polymorphisms of Cytochrome P450 Enzymes and Transport Proteins in a Russian Population and Three Ethnic Groups of Dagestan. (cdc.gov)
  • Genetic polymorphism for cytochrome 450 (P450) enzymes leads to interindividual variability in the plasma concentrations of many drugs. (dovepress.com)
  • Biotransformation of drugs and other xenobiotic compounds involves a myriad of drug-metabolizing enzymes, of which the cytochrome P450 (P450) monooxygenases are important members ( Porter and Coon, 1991 ). (aspetjournals.org)
  • A family of enzymes called cytochrome P450s have the ability to break down certain medicines. (stjude.org)
  • By metabolizing a medicine, cytochrome P450 enzymes make the medicine either more or less active, depending upon the medicine. (stjude.org)
  • Normal metabolizer - People in this group have normal working CYP2C9 enzymes. (stjude.org)
  • This previously unknown biological function extends the group of carbohydrate-active enzymes to include the class of cytochrome P450 monooxygenases. (nature.com)
  • The primary enzymes involved are aldehyde dehydrogenase (ALDH), alcohol dehydrogenase (ADH), cytochrome P450 (CYP2E1), and catalase. (nih.gov)
  • Several cytochrome P450 enzymes catalyze the regio- and stereo-specific hydroxylation of alkanes. (mdpi.com)
  • One of these enzymes is called Cytochrome P450 2D6. (clinicaltrials.gov)
  • Cytochromes (electron-transporting proteins) with protoheme (HEME B) as the prosthetic group. (umassmed.edu)
  • Cytochromes are redox-active proteins containing a heme, with a central Fe atom at its core, as a cofactor. (wikipedia.org)
  • He classified these heme proteins on the basis of the position of their lowest energy absorption band in their reduced state, as cytochromes a (605 nm), b (≈565 nm), and c (550 nm). (wikipedia.org)
  • Cytochrome c1 belongs to the cytochrome c family of proteins. (wikipedia.org)
  • Cytochromes P450 ( CYPs ) are proteins of the superfamily containing heme as a cofactor and, therefore, are hemeproteins . (wikipedia.org)
  • Chemical-shift perturbations for 1H and 15N nuclei of both cytochromes, arising from the interactions with the unlabeled partner proteins, were used for mapping the interacting surfaces on both proteins. (nih.gov)
  • The bc1 complex contains 11 subunits, 3 respiratory subunits (cytochrome B, cytochrome C1, Rieske protein), 2 core proteins and 6 low-molecular weight proteins. (wikipedia.org)
  • Cytochrome P450 proteins can also be grouped by two different schemes. (ebi.ac.uk)
  • The binary covalent complex between the flavoprotein and cytochrome b5 was exclusively observed following incubation of all three proteins including NADPH-cytochrome P-450 reductase, cytochrome b5, and cytochrome c in L-alpha-dimyristoylphosphatidylcholine vesicles, and no heterotrimer could be identified. (biomedsearch.com)
  • Cytochromes P450 (CYPs) comprise a large superfamily of proteins that are of central importance in the detoxification or activation of a tremendous number of natural and synthetic hydrophobic xenobiotics, including many therapeutic drugs, chemical carcinogens and environmental pollutants. (springer.com)
  • Cytochrome P450 2C9 (CYP2C9) is part of the cytochrome P450 family of proteins in the body. (stjude.org)
  • Here, we describe cytochrome P450 monooxygenases from marine bacteria that, together with appropriate redox-partner proteins, catalyze the oxidative demethylation of 6- O -methyl- d -galactose, which is an abundant monosaccharide of the algal polysaccharides agarose and porphyran. (nature.com)
  • It is found that this is due to the formation of Schiff's bases, the formyl side chain of haem a being condensed with amino groups of the protein. (royalsocietypublishing.org)
  • In the process of oxidative phosphorylation, a globular cytochrome cc protein is involved in the electron transfer from the membrane-bound complex III to complex IV. (wikipedia.org)
  • Photosystem II, the first protein complex in the light-dependent reactions of oxygenic photosynthesis, contains a cytochrome b subunit. (wikipedia.org)
  • Cyclooxygenase 2, an enzyme involved in inflammation, is a cytochrome b protein. (wikipedia.org)
  • Cytochrome C1 (also known as Complex III subunit 4) is a protein encoded by the CYC1 gene. (wikipedia.org)
  • Cytochrome is a heme-containing subunit of the cytochrome b-c1 complex, which accepts electrons from Rieske protein and transfers electrons to cytochrome c in the mitochondrial respiratory chain. (wikipedia.org)
  • As an iron-sulfur protein approaches the b-c1 complex, it accepts an electron from the cytochrome b subunit, then undergoes a conformational change to attach to cytochrome c1. (wikipedia.org)
  • There, the electron carried by the iron-sulfur protein is transferred to the heme carried by cytochrome c1. (wikipedia.org)
  • Protein-protein docking simulations have been performed for the binary cytochrome b5-cytochrome c and ternary (cytochrome b5)-(cytochrome c)2 complexes using a novel HADDOCK approach. (nih.gov)
  • Complex III is a multisubunit transmembrane protein encoded by both the mitochondrial (cytochrome b) and the nuclear genomes (all other subunits). (wikipedia.org)
  • In certain cases, cytochrome P450 can be fused to its redox partner to produce a bi-functional protein, such as with P450BM-3 from Bacillus megaterium [ PMID: 17023115 ], which has haem and flavin domains. (ebi.ac.uk)
  • We report here the purification and cDNA cloning of Apaf-1, a novel 130 kd protein from HeLa cell cytosol that participates in the cytochrome c-dependent activation of caspase-3. (nih.gov)
  • The electron transport functions of the b6f complex are coupled to proton transfer and generation of a trans-membrane proton electrochemical gradient, by mechanisms similar to those of the cytochrome bc1 complex of the respiratory chain and the photosynthetic bacteria, whose protein core is similar to that of the b6f complex. (cmu.edu)
  • Our results point to a molecular mechanism by which this microRNA participates in the regulation of axonal respiration and function by modulating the levels of COXIV, a protein which plays a key role in the assembly of the mitochondrial cytochrome c oxidase complex IV. (jneurosci.org)
  • 19(4):499-504, 1995 Oct. Abstract The objective of this study was to further elucidate the role of oxidative stress in the aging process by determining whether or not the rates of mitochondrial superoxide anion radical and hydrogen peroxide (H2O2) production, the activity of cytochrome c oxidase, and the concentration of protein carbonyls are correlated with the life span potential of different species. (bio.net)
  • The average life span potential of these species was found to be inversely correlated with the rates of mitochondrial superoxide and H2O2 production and with the level of protein carbonyls, and to be directly related to the activity of cytochrome c oxidase. (bio.net)
  • Intron alpha is the first intron of the cytochrome c oxidase subunit I gene (COX1). (bio.net)
  • We surveyed mitochondrial DNA variation within the abietella species group by sequencing 451 bp of cytochrome oxidase subunit 1 (COI) and 572 bp of cytochrome oxidase subunit 2 (COII. (usda.gov)
  • The cytochrome b gene sequence and genetic variation parameters were analyzed in MEGA software (ver 6), and DnaSP software (ver 5.10.01). (doaj.org)
  • Ambler RP: The amino acid sequence of cytochrome c-551.5 (Cytochrome c(7)) from the green photosynthetic bacterium Chloropseudomonas ethylica. (drugbank.ca)
  • Bruschi M, Leroy G, Guerlesquin F, Bonicel J: Amino-acid sequence of the cytochrome c3 (M(r) 26,000) from Desulfovibrio desulfuricans Norway and a comparison with those of the other polyhemic cytochromes from Desulfovibrio. (drugbank.ca)
  • We describe here the first mutant of P. anserina that has the alpha sequence precisely deleted and whose cytochrome c oxidase activity is identical to that of wild-type cells. (bio.net)
  • 2004), based on cytochrome oxidase I sequence data. (tolweb.org)
  • Specimens were ovani spotted on fi lter paper as revealed by single-strand conformation polymor- these vectors may be misidentifi ed grouped by ITS2 sequence. (cdc.gov)
  • Sequence groups of caught specimens arbitrarily named species A-J are ranked by abundance. (cdc.gov)
  • The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. (uniprot.org)
  • The heme group is a highly conjugated ring system (which allows its electrons to be very mobile) surrounding an iron ion. (wikipedia.org)
  • Complex IV contains a cytochrome a/a3-domain that transfers electrons and catalyzes the reaction of oxygen to water. (wikipedia.org)
  • Microsomal P450 systems , in which electrons are transferred from NADPH via cytochrome P450 reductase (variously CPR, POR, or CYPOR). (wikipedia.org)
  • CYB 5 R/cyb 5 /P450 systems , in which both electrons required by the CYP come from cytochrome b 5 . (wikipedia.org)
  • In the complete mechanism, two electrons are transferred from ubiquinol to ubiquinone, via two cytochrome c intermediates. (wikipedia.org)
  • It is the terminal oxidase complex of the RESPIRATORY CHAIN and collects electrons that are transferred from the reduced CYTOCHROME C GROUP and donates them to molecular OXYGEN, which is then reduced to water. (bioportfolio.com)
  • Electrons are transferred from respiratory complexes III to IV (CIII and CIV) by water-soluble cytochrome (cyt. (pdbj.org)
  • Drugs that inhibit alprazolam metabolism via cytochrome P450 3A The initial step in alprazolam metabolism is hydroxylation catalyzed by. (drugs-forum.com)
  • The utility of CL-LCN mice for in vivo drug metabolism studies was explored using the cytochrome P450 (P450) prodrug cyclophosphamide (CPA). (aspetjournals.org)
  • Oxidative and reductive metabolism by cytochrome P450 2E1. (semanticscholar.org)
  • NADPH oxidase activity and cytochrome b558 content of human Epstein-Barr-virus-transformed B lymphocytes correlate with expression of genes encoding components of the oxidase system. (umassmed.edu)
  • In order to dissect the mechanism of Cu acquisition in the absence of CcoA, we isolated ΔccoA mutants that were cbb 3 -Cox defective after addition of Cu. Characterization of these mutants by genetic complementations revealed mutations in cytochrome c maturation (CCM) genes. (upenn.edu)
  • Comparison of cytochrome P450 (CYP) genes from the mouse and human genomes, including nomenclature recommendations for genes, pseudogenes and alternative-splice variants. (ebi.ac.uk)
  • The objective of this study was to investigate the prevalence of polymorphic markers of the CYP2C19, CYP2C9, CYP2D6, SLCO1B1, and ABCB1 genes among the three ethnic groups in Dagestan and compare it with the carrier frequency of these markers among the Russian population living in Moscow. (cdc.gov)
  • Aubert C, Lojou E, Bianco P, Rousset M, Durand MC, Bruschi M, Dolla A: The Desulfuromonas acetoxidans triheme cytochrome c7 produced in Desulfovibrio desulfuricans retains its metal reductase activity. (drugbank.ca)
  • Assfalg M, Bertini I, Bruschi M, Michel C, Turano P: The metal reductase activity of some multiheme cytochromes c: NMR structural characterization of the reduction of chromium(VI) to chromium(III) by cytochrome c(7). (drugbank.ca)
  • Succinate- cytochrome c reductase activity, but not the activities of NADH-coenzyme Q 1 reductase or cytochrome c oxidase, was inhibited by 32% by glutamate treatment, an effect that was abolished by incubation with D-glucose. (wiley.com)
  • Here we show that these mutations are not directly involved in the Cu trafficking to CcoN but involved in the production of membrane bound cytochrome c subunits of cbb 3 -Cox. (upenn.edu)
  • Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. (uniprot.org)
  • Cytochrome C1 plays a role in the electron transfer during oxidative phosphorylation. (wikipedia.org)
  • Mutation of CYC1 was observed to cause instability in the cytochrome b-c1 complex, which decreased its ability to create energy through oxidative phosphorylation. (wikipedia.org)
  • The coenzyme Q : cytochrome c - oxidoreductase, sometimes called the cytochrome bc1 complex, and at other times complex III, is the third complex in the electron transport chain (EC 1.10.2.2), playing a critical role in biochemical generation of ATP (oxidative phosphorylation). (wikipedia.org)
  • Cytochromes P450 are a group of heme-thiolate monooxygenases. (abcam.com)
  • Cytochrome P450 oxidoreductase deficiency is a disorder of hormone production. (medlineplus.gov)
  • The hormonal changes associated with cytochrome P450 oxidoreductase deficiency can affect the development of the reproductive system, skeleton, and other parts of the body. (medlineplus.gov)
  • The signs and symptoms of cytochrome P450 oxidoreductase deficiency vary from mild to severe. (medlineplus.gov)
  • People with moderate cytochrome P450 oxidoreductase deficiency usually do not have skeletal abnormalities. (medlineplus.gov)
  • The severe form of cytochrome P450 oxidoreductase deficiency is sometimes called Antley-Bixler syndrome with genital anomalies and disordered steroidogenesis. (medlineplus.gov)
  • Some women who are pregnant with fetuses affected by cytochrome P450 oxidoreductase deficiency experience mild symptoms of the disorder even though they themselves do not have the disorder. (medlineplus.gov)
  • The prevalence of cytochrome P450 oxidoreductase deficiency is unknown. (medlineplus.gov)
  • Researchers suspect that cytochrome P450 oxidoreductase deficiency is underdiagnosed and that mild cases of this disorder may be relatively common. (medlineplus.gov)
  • Because the signs and symptoms can be difficult to detect, people with mild cytochrome P450 oxidoreductase deficiency may never come to medical attention. (medlineplus.gov)
  • Cytochrome P450 oxidoreductase deficiency is caused by mutations in the POR gene. (medlineplus.gov)
  • This gene provides instructions for making the enzyme cytochrome P450 oxidoreductase, which plays a critical role in the formation of steroid hormones . (medlineplus.gov)
  • Mutations in the POR gene reduce the activity of cytochrome P450 oxidoreductase, which disrupts the production of steroid hormones. (medlineplus.gov)
  • In a woman who is pregnant with an affected fetus, abnormal levels of sex hormones in the fetus may cause her to have mild, temporary signs and symptoms of cytochrome P450 oxidoreductase deficiency. (medlineplus.gov)
  • Cytochrome P450 oxidoreductase is also needed for the production of cholesterol. (medlineplus.gov)
  • Mutations in the POR gene can disrupt the production of cholesterol, which likely impairs normal bone formation in the severe form of cytochrome P450 oxidoreductase deficiency. (medlineplus.gov)
  • if a shortage of cytochrome P450 oxidoreductase prevents retinoic acid from being broken down, the resulting excess of that molecule can stimulate the abnormal growth and fusion of bones. (medlineplus.gov)
  • The reaction mechanism for complex III (cytochrome bc1, coenzyme Q: cytochrome C oxidoreductase) is known as the ubiquinone ("Q") cycle. (wikipedia.org)
  • Overall: 2 x QH2 oxidised to Q 1 x Q reduced to QH2 2 x Cyt c1 reduced 4 x H+ released into intermembrane space 2 x H+ picked up from matrix The reaction proceeds according to the following steps: Round 1: Cytochrome b binds a ubiquinol and a ubiquinone. (wikipedia.org)
  • We present a phylogenetic hypothesis for 40 species in the bird family Paridae, based on comparisons of nucleotide sequences of the mitochondrial cytochrome- b gene. (bioone.org)
  • Maternal ancestry of the Rutilus alburnoides complex (Teleostei, Cyprinidae) as determined by analysis of cytochrome b sequences. (thefreelibrary.com)
  • The present study was designed to investigate the role of cytochrome P450 inhibitors, SKF 525A, and curcumin pretreatment on the cytotoxicity of antifungal drugs fluconazole and itraconazole. (hindawi.com)
  • Thapliyal and Maru [ 14 ] reported curcumins inhibited the activity of cytochrome P450 in vitro and in vivo. (hindawi.com)
  • These results showed that in the greater part of the complexes, the flavin-mediated pathway for reduction of cytochrome c or cytochrome b5 by pyridine nucleotide was intact. (biomedsearch.com)
  • Mutations in the promoter region of the gene for gp91-phox in X-linked chronic granulomatous disease with decreased expression of cytochrome b558. (umassmed.edu)
  • There are nomenclature committees that assign and track both base gene names ( Cytochrome P450 Homepage ) and allele names ( CYP Allele Nomenclature Committee ). (wikipedia.org)
  • Meanwhile, a similar proportion of CYP2C19*3 allele was observed in all ethnic groups (p=0.071). (bmj.com)
  • Cytochrome c oxidases (Cox) are among these metalloproteins whose assembly and activity involves incorporation of Cu cofactor into their catalytic subunits in addition to the maturation of other subunits. (upenn.edu)
  • The crystallization procedure is well reproducible and will allow for the analysis of the structures of mechanistically interesting mutant cytochrome c oxidases. (rcsb.org)
  • The α-band absorption maximum of the reduced minus oxidized enzyme is shifted by 5-7 nm to the blue relative to most other aa3-type oxidases, and accordingly, we designate the Bacillus enzyme as cytochrome aa3-600. (cut.ac.cy)
  • The shifted optical spectrum cannot be ascribed to an alteration in the strength of the hydrogen bond between the formyl group of the low-spin heme and its environment, as the Raman line assigned to this mode in aa3-600 has the same frequency and degree of resonance enhancement as the low-spin heme a formyl mode in most other aa3-type oxidases. (cut.ac.cy)
  • In the course of an infection, Salmonella enterica occupies diverse anatomical sites with various concentrations of oxygen (O ) and nitric oxide (NO). These diatomic gases compete for binding to catalytic metal groups of quinol oxidases. (bireme.br)
  • The cytochrome bd oxidases are terminal oxidases that are present in bacteria and archaea. (bireme.br)
  • Four types of cytochromes are distinguished by their prosthetic groups: There is no "cytochrome e," but cytochrome f, found in the cytochrome b6f complex of plants is a c-type cytochrome. (wikipedia.org)
  • Three subunits have prosthetic groups. (wikipedia.org)
  • Prior to X-ray crystal structure analysis, each monomeric unit of the complex was known to contain six bound prosthetic groups, three hemes (f, two hemes b, bp and bn), one [2Fe-2S] cluster, and one molecule each of chlorophyll-a and carotene. (cmu.edu)
  • Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. (uniprot.org)
  • Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. (uniprot.org)
  • Sapshead, L. M., Wimpenny, J. W. T.: The influence of oxygen and nitrate on the formation of the cytochrome pigments of the aerobic and anaerobic respiratory chain of Micrococcus denitrificans . (springer.com)
  • The investigations presented here have revealed that cytochrome bd potentiates virulence of a clinically relevant bacterial pathogen by fueling bioenergetics of prokaryotic cells while protecting the respiratory chain against NO toxicity. (bireme.br)
  • Assignment of the human cytochrome P-450 nifedipine oxidase gene (CYP3A4) to chromosome 7 at band q22.1 by fluorescence in situ hybridization. (nih.gov)
  • We have used a full length cDNA clone (2.2 kb) for the human cytochrome P-450 nifedipine oxidase (CYP3A4) enzyme as a probe to determine its chromosome localization by fluorescence in situ hybridization. (nih.gov)
  • Studies to assess the enzyme kinetic behavior and to identify the cytochrome P450 (CYP) isoform(s) involved in the major metabolic pathway ( N -demethylation) for citalopram (CIT), a selective serotonin reuptake inhibitor, were performed using human liver microsomes and cDNA-expressed human cytochrome P450 isoforms. (aspetjournals.org)
  • The 220 kDa dimeric cytochrome b6f complex of oxygenic photosynthesis provides the electronic connection between the two reaction centers, Photosystems I and II that are, respectively, coupled to NADP+ reduction and oxygen evolution. (cmu.edu)
  • A fragment of 808 base pairs within the mtDNA gene cytochrome oxidase I (COI) was analyzed for 15 species of Anastrepha 12 within the fraterculus group, one unplaced species and two outgroups. (bvsalud.org)
  • Phylogenetic analyses of the mtDNA 12S rDNA, cytochrome. (usda.gov)
  • Complex III itself is composed of several subunits, one of which is a b-type cytochrome while another one is a c-type cytochrome. (wikipedia.org)
  • The aa3 type cytochrome c oxidase consisting of the core subunits I and II only was isolated from the soil bacterium Paracoccus denitrificans and crystallized as complex with a monoclonal antibody Fv fragment. (rcsb.org)
  • The iron in cytochromes usually exists in a ferrous (Fe2+) and a ferric (Fe3+) state with a ferroxo (Fe4+) state found in catalytic intermediates. (wikipedia.org)
  • One atr complementation group consisted of mutations in the cytochrome P450 gene CYP83B1 . (genetics.org)
  • In mitochondria and chloroplasts, these cytochromes are often combined in electron transport and related metabolic pathways: A distinct family of cytochromes is the cytochrome P450 family, so named for the characteristic Soret peak formed by absorbance of light at wavelengths near 450 nm when the heme iron is reduced (with sodium dithionite) and complexed to carbon monoxide. (wikipedia.org)
  • This study aimed to analyze genetic variation and phylogeography of eight Indonesian swamp-buffalo populations based on cytochrome b gene marker. (doaj.org)
  • Genetic: Cytochrome P450 2D6 (CYP2D6) genetic screening. (clinicaltrials.gov)
  • Codeine was originally considered safe to use while breastfeeding however, increased risk of adverse drug reactions has been demonstrated in mothers taking codeine, as well as their breastfed infants, when the mother possesses a genetic variation resulting in cytochrome P450 2D6 (CYP2D6) ultra-rapid metabolizer (UM) phenotype. (clinicaltrials.gov)
  • Genetic screening for cytochrome P450 2D6 (CYP2D6) polymorphism will be conducted on genetic information obtained from non-invasive salivary samples. (clinicaltrials.gov)
  • Individuals within the prospective group will receive their CYP2D6 genotype results prior to pharmacotherapy and their analgesic regimen will be tailored to their genetic results. (clinicaltrials.gov)
  • W, Schönian G. Genetic heterogeneity responsible for maintaining malaria could be grouped into several separate of ribosomal internal transcribed spacer parasite transmission, and without clades, distinct from known vectors in clinical samples of Leishmania don- adequate discriminatory techniques, in the area (Figure). (cdc.gov)
  • Inconsistent conclusions have been reported for the genetic relationship between CYP4F2 (Cytochrome P450 Family 4 Subfamily F Member 2) polymorphisms and the susceptibility to cardiovascular and cerebrovascular diseases. (springer.com)
  • Restitution of superoxide generation in autosomal cytochrome-negative chronic granulomatous disease (A22(0) CGD)-derived B lymphocyte cell lines by transfection with p22phax cDNA. (umassmed.edu)
  • This creates a reduced species of cytochrome c, which separates from the b-c1 complex and moves to the last enzyme in the electron transport chain, cytochrome c oxidase (Complex IV). (wikipedia.org)
  • Recently, two techniques, polymerase chain reaction (PCR) amplification and sequencing of cytochrome b gene ( cyt b gene sequencing) and polymorphism-specific PCR (PS-PCR) were recommended for Leishmania species identification. (ajtmh.org)
  • Our results of COI indicate the placement of A. acris Stone, an unplaced species, in the fraterculus group. (bvsalud.org)
  • The longest cytochrome- b distances between species reach 12% in uncorrected divergence. (bioone.org)
  • The Anaxyrus boreas species group currently comprises four species in western North America including the broadly distributed A. boreas , and three localized species, Anaxyrus nelsoni , Anaxyrus exsul and Anaxyrus canorus . (usda.gov)
  • There are undescribed species and nomenclatural problems, so the taxonomy of the group is unstable. (tolweb.org)
  • 2004) have produced the first phylogeny of Latrodectus species using the mitochondrial gene cytochrome oxidase I. This analysis produced a generally well supported tree. (tolweb.org)
  • The dog family, Canidae, is a widely distributed group of species that have evolved and radiated relatively recently into 16 genera and 36 recognized species (Nowak 1999). (usda.gov)
  • Ubiquinol-cytochrome-c reductase catalyzes the chemical reaction QH2 + 2 ferricytochrome c ⇌ {\displaystyle \rightleftharpoons } Q + 2 ferrocytochrome c + 2 H+ Thus, the two substrates of this enzyme are quinol (QH2) and ferri- (Fe3+) cytochrome c, whereas its 3 products are quinone (Q), ferro- (Fe2+) cytochrome c, and H+. (wikipedia.org)
  • The P-glycoprotein (Pgp) efflux pump can influence the hepatocellular concentration of xenobiotics that are modulators and substrates of cytochrome P4503A (CYP3A). (pnas.org)
  • Cytochrome P450 Protocols, Third Edition focuses on high-throughput methods for the simultaneous analysis of multiple CYPs, substrates or ligands. (springer.com)
  • Genetics Home Reference (GHR) contains information on NADH cytochrome B5 reductase deficiency. (nih.gov)
  • Cytochrome function is linked to the reversible redox change from ferrous (Fe(II)) to the ferric (Fe(III)) oxidation state of the iron found in the heme core. (wikipedia.org)
  • Cytochromes are, thus, capable of performing electron transfer reactions and catalysis by reduction or oxidation of their heme iron. (wikipedia.org)
  • The similarity of the binding shifts observed for oxidized and reduced cytochrome c indicates that the complex formation is not influenced by the oxidation state of the cytochrome c. (nih.gov)
  • The cytochrome P450 (CYP) enzyme CYP2B6 is one of about a dozen human CYPs that are primarily involved in the biotransformation of drugs and other xenobiotics. (frontiersin.org)
  • Diethyl ether as a substrate for acetone/ethanol-inducible cytochrome P-450 and as an inducer for cytochrome(s) P-450. (semanticscholar.org)
  • The ability of diethyl ether to serve as a substrate for microsomal and purified cytochrome P-450 (P-450) and as an inducer for rat hepatic microsomal monooxygenase activities was examined. (semanticscholar.org)
  • This video highlights the importance of cytochrome P450s in academia and industry and explains how our research group broadens the substrate range of these biocatalysts through enzyme engineering. (mib.ac.uk)
  • Cytochrome b5, cytochrome c, and cytochrome P-450 interactions with NADPH-cytochrome P-450 reductase in phospholipid vesicles. (biomedsearch.com)
  • Cytochrome P450 2B6 (CYP2B6) belongs to the minor drug metabolizing P450s in human liver. (frontiersin.org)
  • Cytochrome c binds to Apaf-1, an event that may trigger the activation of caspase-3, leading to apoptosis. (nih.gov)
  • Four varieties are recognized by the International Union of Biochemistry and Molecular Biology (IUBMB), cytochromes a, cytochromes b, cytochromes c and cytochrome d. (wikipedia.org)
  • In the early 1960s, a linear evolution of cytochromes was suggested by Emanuel Margoliash that led to the molecular clock hypothesis. (wikipedia.org)
  • These compounds require activation by cytochrome P450 1A2 (CYP1A2) and N -acetyltransferase-2 (NAT2) before they can damage DNA. (bmj.com)
  • Caffeine is metabolized primarily by cytochrome CYP1A2 in the liver through an initial N3-demethylation. (hmdb.ca)
  • A dose-response study generated a safe pharmacological regimen that enabled i.p. minocycline to significantly lower cytosolic cytochrome c at the epicenter 4 h after SCI. (pnas.org)