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 and iron sulfur-containing oxidoreductase complex that catalyzes the conversion of UBIQUINONE to ubiquinol. In MITOCHONDRIA the complex also couples its reaction to the transport of PROTONS across the internal mitochondrial membrane. The NADH DEHYDROGENASE component of the complex can be isolated and is listed as EC 1.6.99.3.
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.
Hydrocarbon rings which contain two ketone moieties in any position. They can be substituted in any position except at the ketone groups.
A flavoprotein oxidase complex that contains iron-sulfur centers. It catalyzes the oxidation of SUCCINATE to fumarate and couples the reaction to the reduction of UBIQUINONE to ubiquinol.
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 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.
A genus of ascomycetous yeast in the family Dipodascaceae, order SACCHAROMYCETALES.
A flavoprotein that reversibly catalyzes the oxidation of NADH or NADPH by various quinones and oxidation-reduction dyes. The enzyme is inhibited by dicoumarol, capsaicin, and caffeine.
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.
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.
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).
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 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.
D-Glucose:1-oxidoreductases. Catalyzes the oxidation of D-glucose to D-glucono-gamma-lactone and reduced acceptor. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.47; EC 1.1.1.118; EC 1.1.1.119 and EC 1.1.99.10.
A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)
The mitochondria of the myocardium.
Constituent of 30S subunit prokaryotic ribosomes containing 1600 nucleotides and 21 proteins. 16S rRNA is involved in initiation of polypeptide synthesis.
A botanical insecticide that is an inhibitor of mitochondrial electron transport.
DNA sequences encoding RIBOSOMAL RNA and the segments of DNA separating the individual ribosomal RNA genes, referred to as RIBOSOMAL SPACER DNA.
Flavoproteins that serve as specific electron acceptors for a variety of DEHYDROGENASES. They participate in the transfer of electrons to a variety of redox acceptors that occur in the respiratory chain.
Eicosamethyl octacontanonadecasen-1-o1. Polyprenol found in animal tissues that contains about 20 isoprene residues, the one carrying the alcohol group being saturated.
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 various filaments, granules, tubules or other inclusions within mitochondria.
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.
The relative amounts of the PURINES and PYRIMIDINES in a nucleic acid.
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 glucose dehydrogenase that catalyzes the oxidation of beta-D-glucose to form D-glucono-1,5-lactone, using NAD as well as NADP as a coenzyme.
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)
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)
Organic, monobasic acids derived from hydrocarbons by the equivalent of oxidation of a methyl group to an alcohol, aldehyde, and then acid. Fatty acids are saturated and unsaturated (FATTY ACIDS, UNSATURATED). (Grant & Hackh's Chemical Dictionary, 5th ed)
The relationships of groups of organisms as reflected by their genetic makeup.
A water-soluble, colorless crystal with an acid taste that is used as a chemical intermediate, in medicine, the manufacture of lacquers, and to make perfume esters. It is also used in foods as a sequestrant, buffer, and a neutralizing agent. (Hawley's Condensed Chemical Dictionary, 12th ed, p1099; McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed, p1851)
Mevalonic acid is a crucial intermediate compound in the HMG-CoA reductase pathway, which is a metabolic route that produces cholesterol, other steroids, and isoprenoids in cells.
Cytochromes (electron-transporting proteins) with protoheme (HEME B) as the prosthetic group.
Methyl, propyl, butyl, and ethyl esters of p-hydroxybenzoic acid. They have been approved by the FDA as antimicrobial agents for foods and pharmaceuticals. (From Hawley's Condensed Chemical Dictionary, 11th ed, p872)
A family in the order Rhodobacterales, class ALPHAPROTEOBACTERIA.
Small molecules that are required for the catalytic function of ENZYMES. Many VITAMINS are coenzymes.
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.
Genes, found in both prokaryotes and eukaryotes, which are transcribed to produce the RNA which is incorporated into RIBOSOMES. Prokaryotic rRNA genes are usually found in OPERONS dispersed throughout the GENOME, whereas eukaryotic rRNA genes are clustered, multicistronic transcriptional units.
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.
Benzene rings which contain two ketone moieties in any position. They can be substituted in any position except at the ketone groups.
Derivatives of SUCCINIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain a 1,4-carboxy terminated aliphatic structure.
Deoxyribonucleic acid that makes up the genetic material of bacteria.
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.
Life or metabolic reactions occurring in an environment containing oxygen.
A family of gram-negative, asporogenous rods or ovoid cells, aerobic or facultative anaerobic chemoorganotrophs. They are commonly isolated from SOIL, activated sludge, or marine environments.
A family of gram-negative aerobic bacteria consisting of ellipsoidal to rod-shaped cells that occur singly, in pairs, or in chains.
Spherical phototrophic bacteria found in mud and stagnant water exposed to light.
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.
Procedures for identifying types and strains of bacteria. The most frequently employed typing systems are BACTERIOPHAGE TYPING and SEROTYPING as well as bacteriocin typing and biotyping.
A somewhat heterogeneous class of enzymes that catalyze the transfer of alkyl or related groups (excluding methyl groups). EC 2.5.
A class in the phylum PROTEOBACTERIA comprised mostly of two major phenotypes: purple non-sulfur bacteria and aerobic bacteriochlorophyll-containing bacteria.
A genus of gram-negative, aerobic, rod-shaped bacteria characterized by an outer membrane that contains glycosphingolipids but lacks lipopolysaccharide. They have the ability to degrade a broad range of substituted aromatic compounds.
Chemical agents that uncouple oxidation from phosphorylation in the metabolic cycle so that ATP synthesis does not occur. Included here are those IONOPHORES that disrupt electron transfer by short-circuiting the proton gradient across mitochondrial membranes.
The 8-hydroxy derivatives inhibit various enzymes and their halogenated derivatives, though neurotoxic, are used as topical anti-infective agents, among other uses.
Derivatives of the dimethylisoalloxazine (7,8-dimethylbenzo[g]pteridine-2,4(3H,10H)-dione) skeleton. Flavin derivatives serve an electron transfer function as ENZYME COFACTORS in FLAVOPROTEINS.
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.
Former kingdom, located on Korea Peninsula between Sea of Japan and Yellow Sea on east coast of Asia. In 1948, the kingdom ceased and two independent countries were formed, divided by the 38th parallel.
The presence of bacteria, viruses, and fungi in the soil. This term is not restricted to pathogenic organisms.
A family of gram-negative, aerobic, non-spore forming rods or cocci. Well known genera include ACHROMOBACTER; ALCALIGENES; and BORDETELLA.
A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.
The rate dynamics in chemical or physical systems.
Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES.
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 family of gram-negative bacteria, in the order Xanthomonadales, pathogenic to plants.
Naphthalene rings which contain two ketone moieties in any position. They can be substituted in any position except at the ketone groups.
An oral anticoagulant that interferes with the metabolism of vitamin K. It is also used in biochemical experiments as an inhibitor of reductases.
A class of compounds composed of repeating 5-carbon units of HEMITERPENES.
Compounds based on a 7-membered heterocyclic ring including an oxygen. They can be considered a medium ring ether. A natural source is the MONTANOA plant genus. Some dibenzo-dioxepins, called depsidones, are found in GARCINIA plants.
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)
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 family of gram-negative coccoid to rod-shaped bacteria in the order Rhizobiales. They are obligate parasites chiefly of warm-blooded VERTEBRATES. Many are pathogenic.
Polyunsaturated side-chain quinone derivative which is an important 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.
A species of bacteria isolated from soil.
A species of ascomycetous fungi of the family Sordariaceae, order SORDARIALES, much used in biochemical, genetic, and physiologic studies.
A species of gram-negative bacteria of the family ACETOBACTERACEAE found in FLOWERS and FRUIT. Cells are ellipsoidal to rod-shaped and straight or slightly curved.
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.
A group of substances similar to VITAMIN K 1 which contains a ring of 2-methyl-1,4-naphthoquinione and an isoprenoid side chain of varying number of isoprene units. In vitamin K 2, each isoprene unit contains a double bond. They are produced by bacteria including the normal intestinal flora.
A genus of gram-negative, rod-shaped or pleomorphic bacteria which are halotolerant. Members of this genus are capable of growth in sodium chloride concentrations of up to 20% or more. (From Bergey's Manual of Determinative Bacteriology, 9th ed)
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.
An oil-resistant synthetic rubber made by the polymerization of chloroprene.
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.
Chelating agent and inhibitor of cellular respiration.
A family of gram-negative bacteria in the class BETAPROTEOBACTERIA. There are at least eight genera.
The salinated water of OCEANS AND SEAS that provides habitat for marine organisms.
A family of gram-negative aerobic bacteria in the class BETA PROTEOBACTERIA, encompassing the acidovorans rRNA complex. Some species are pathogenic for PLANTS.
The five-carbon building blocks of TERPENES that derive from MEVALONIC ACID or deoxyxylulose phosphate.
Inorganic salts of the hypothetical acid, H3Fe(CN)6.
A coenzyme for a number of oxidative enzymes including NADH DEHYDROGENASE. It is the principal form in which RIBOFLAVIN is found in cells and tissues.
A genus of the family BRUCELLACEAE comprising obligately aerobic gram-negative rods with parallel sides and rounded ends.
Proteins encoded by the mitochondrial genome or proteins encoded by the nuclear genome that are imported to and resident in the MITOCHONDRIA.
The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.
A family in the order Rhizobiales, class ALPHAPROTEOBACTERIA comprised of many genera of budding or appendaged bacteria.
A hydroxynaphthoquinone that has antimicrobial activity and is being used in antimalarial protocols.
Single chains of amino acids that are the units of multimeric PROTEINS. Multimeric proteins can be composed of identical or non-identical subunits. One or more monomeric subunits may compose a protomer which itself is a subunit structure of a larger assembly.
A vitamin found in green vegetables. It is used in the treatment of peptic ulcers, colitis, and gastritis and has an effect on secretory, acid-forming, and enzymatic functions of the intestinal tract.
An active neurotoxic metabolite of 1-METHYL-4-PHENYL-1,2,3,6-TETRAHYDROPYRIDINE. The compound reduces dopamine levels, inhibits the biosynthesis of catecholamines, depletes cardiac norepinephrine and inactivates tyrosine hydroxylase. These and other toxic effects lead to cessation of oxidative phosphorylation, ATP depletion, and cell death. The compound, which is related to PARAQUAT, has also been used as an herbicide.
A lipid cofactor that is required for normal blood clotting. Several forms of vitamin K have been identified: VITAMIN K 1 (phytomenadione) derived from plants, VITAMIN K 2 (menaquinone) from bacteria, and synthetic naphthoquinone provitamins, VITAMIN K 3 (menadione). Vitamin K 3 provitamins, after being alkylated in vivo, exhibit the antifibrinolytic activity of vitamin K. Green leafy vegetables, liver, cheese, butter, and egg yolk are good sources of vitamin K.
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 obtained from ESCHERICHIA COLI.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Electron transfer through the cytochrome system liberating free energy which is transformed into high-energy phosphate bonds.
Five-carbon saturated hydrocarbon group of the methane series. Include isomers and derivatives.
Cytochrome reductases are enzymes that catalyze the transfer of electrons from donor molecules to cytochromes in electron transport chains, playing a crucial role in cellular respiration and energy production within cells.

Identification of quinone-binding and heme-ligating residues of the smallest membrane-anchoring subunit (QPs3) of bovine heart mitochondrial succinate:ubiquinone reductase. (1/1440)

The smallest membrane-anchoring subunit (QPs3) of bovine heart succinate:ubiquinone reductase was overexpressed in Escherichia coli JM109 as a glutathione S-transferase fusion protein using the expression vector pGEX2T/QPs3. The yield of soluble active recombinant glutathione S-transferase-QPs3 fusion protein was isopropyl-1-thio-beta-D-galactopyranoside concentration-, induction growth time-, temperature-, and medium-dependent. Maximum yield of soluble recombinant fusion protein was obtained from cells harvested 3.5 h post-isopropyl-1-thio-beta-D-galactopyranoside (0.4 mM)-induction growth at 25 degrees C in 2.0% tryptone, 0.5% yeast extract, 10 mM NaCl, 2.5 mM KCl, 10 mM MgCl2, 20 mM glucose (SOC medium) containing 440 mM sorbitol and 2.5 mM betaine. QPs3 was released from the fusion protein by proteolytic cleavage with thrombin. Isolated recombinant QPs3 shows one protein band in sodium dodecyl sulfate-polyacrylamide gel electrophoresis that corresponds to subunit V of mitochondrial succinate:ubiquinone reductase. Although purified recombinant QPs3 is dispersed in 0.01% dodecylmaltoside, it is in a highly aggregated form, with an apparent molecular mass of more than 1 million. The recombinant QPs3 binds ubiquinone, causing a spectral blue shift. Upon titration of the recombinant protein with ubiquinone, a saturation behavior is observed, suggesting that the binding is specific and that recombinant QPs3 may be in the functionally active state. Two amino acid residues, serine 33 and tyrosine 37, in the putative ubiquinone binding domain of QPs3 are involved in ubiquinone binding because the S33A- or Y37A-substituted recombinant QPs3s do not cause the spectral blue shift of ubiquinone. Although recombinant QPs3 contains little cytochrome b560 heme, the spectral characteristics of cytochrome b560 are reconstituted upon addition of hemin chloride. Reconstituted cytochrome b560 in recombinant QPs3 shows a EPR signal at g = 2.92. Histidine residues at positions 46 and 60 are responsible for heme ligation because the H46N- or H60N-substituted QPs3 fail to restore cytochrome b560 upon addition of hemin chloride.  (+info)

The interaction of coenzyme Q with phosphatidylethanolamine membranes. (2/1440)

Coenzyme Q (CoQ) is a component of the mitochondrial respiratory chain which carries out additional membrane functions, such as acting as an antioxidant. The location of CoQ in the membrane and the interaction with the phospholipid bilayer is still a subject of debate. The interaction of CoQ in the oxidized (ubiquinone-10) and reduced (ubiquinol-10) state with membrane model systems of 1,2-dielaidoyl-sn-glycero-3-phosphoethanolamine (Ela2Gro-P-Etn) has been studied by means of differential scanning calorimetry (DSC), 31P-nuclear magnetic resonance (31P-NMR) and small angle X-ray diffraction (SAXD). Ubiquinone-10 did not visibly affect the lamellar gel to lamellar liquid-crystalline phase transition of Ela2Gro-P-Etn, but it clearly perturbed the multicomponent lamellar liquid-crystalline to lamellar gel phase transition of the phospholipid. The perturbation of both transitions was more effective in the presence of ubiquinol-10. A location of CoQ forming head to head aggregates in the center of the Ela2Gro-P-Etn bilayer with the polar rings protruding toward the phospholipid acyl chains is suggested. The formation of such aggregates are compatible with the strong hexagonal HII phase promotion ability found for CoQ. This ability was evidenced by the shifting of the lamellar to hexagonal HII phase transition to lower temperatures and by the appearance of the characteristic hexagonal HII 31P-NMR resonance and SAXD pattern at temperatures at which the pure Ela2Gro-P-Etn is still organized in extended bilayer structures. The influence of CoQ on the thermotropic properties and phase behavior of Ela2Gro-P-Etn is discussed in relation to the role of CoQ in the membrane.  (+info)

The interaction of ubiquinone-3 with phospholipid membranes. (3/1440)

The effects of ubiquinone-3 (UQ) on dipalmitoylphosphatidylcholine (DPPC) membrane were studied by surface monolayer, differential scanning calorimetry (DSC) and fluorescence techniques. DPPC and UQ are proved to be freely miscible in the mixed monolayer at an air/water interface, and to be partially miscible in bulk phase, i.e. bilayer and solid phase. There is a condensing interaction between UQ and DPPC in the UQ/DPPC mixed monolayers. The solubility of UQ in the DPPC is about 20 mole% and the solubility of DPPC in UQ is about 10 mole%. The membrane fluidity of DPPC was increased by the addition of UQ and the phase transition temperature was decreased.  (+info)

The Saccharomyces cerevisiae succinate dehydrogenase anchor subunit, Sdh4p: mutations at the C-terminal lys-132 perturb the hydrophobic domain. (4/1440)

The yeast succinate dehydrogenase (SDH) is a tetramer of non-equivalent subunits, Sdh1p-Sdh4p, that couples the oxidation of succinate to the transfer of electrons to ubiquinone. One of the membrane anchor subunits, Sdh4p, has an unusual 30 amino acid extension at the C-terminus that is not present in SDH anchor subunits of other organisms. We identify Lys-132 in the Sdh4p C-terminal region as necessary for enzyme stability, ubiquinone reduction, and cytochrome b562 assembly in SDH. Five Lys-132 substituted SDH4 genes were constructed by site-directed mutagenesis and introduced into an SDH4 knockout strain. The mutants, K132E, K132G, K132Q, K132R, and K132V were characterized in vivo for respiratory growth and in vitro for ubiquinone reduction, enzyme stability, and cytochrome b562 assembly. Only the K132R substitution, which conserves the positive charge of Lys-132, produces a wild-type enzyme. The remaining four mutants do not affect the ability of SDH to oxidize succinate in the presence of the artificial electron acceptor, phenazine methosulfate, but impair quinone reductase activity, enzyme stability, and heme insertion. Our results suggest that the presence of a positive charge on residue 132 in the C-terminus of Sdh4p is critical for establishing a stable conformation in the SDH hydrophobic domain that is compatible with ubiquinone reduction and cytochrome b562 assembly. In addition, our data suggest that heme does not play an essential role in quinone reduction.  (+info)

Expression of prokaryotic 1-deoxy-D-xylulose-5-phosphatases in Escherichia coli increases carotenoid and ubiquinone biosynthesis. (5/1440)

Isopentenyl diphosphate (IPP) acts as the common, five-carbon building block in the biosynthesis of all isoprenoids. The first reaction of IPP biosynthesis in Escherichia coli is the formation of 1-deoxy-D-xylulose-5-phosphate, catalysed by 1-deoxy-D-xylulose-5-phosphate synthase (DXPS). E. coli engineered to produce lycopene, was transformed with dxps genes cloned from Bacillus subtilis and Synechocystis sp. 6803. Increases in lycopene levels were observed in strains expressing exogenous DXPS compared to controls. The recombinant strains also exhibited elevated levels of ubiquinone-8. These increases corresponded with enhanced DXP synthase activity in the recombinant E. coli strains.  (+info)

Ubiquinone is reduced by lipoamide dehydrogenase and this reaction is potently stimulated by zinc. (6/1440)

Ubiquinol is an endogenously synthesized lipid-soluble antioxidant. Regeneration of ubiquinol from the oxidized form is essential to the maintenance of its antioxidant function. We demonstrated that lipoamide dehydrogenase can reduce ubiquinone to ubiquinol. Zinc increased the rate of the NADPH-dependent reduction more than 10-fold. The concentration ubiquinone resulting in the half-maximal rate of reduction was approximately 5 microM in the presence and 4 microM in the absence of zinc. These data may explain how ubiquinone is reduced to the active antioxidant ubiquinol, which plays such an important role in protecting against oxidative stress and lipid peroxidation.  (+info)

A revised model of the active site of alternative oxidase. (7/1440)

The plant mitochondrial protein alternative oxidase catalyses dioxygen dependent ubiquinol oxidation to yield ubiquinone and water. A structure of this protein has previously been proposed based on an assumed structural homology to the di-iron carboxylate family of proteins. However, these authors suggested the protein has a very different topology than the known structures of di-iron carboxylate proteins. We have re-examined this model and based on comparison of recent sequences and structural data on di-iron carboxylate proteins we present a new model of the alternative oxidase which allows prediction of active site residues and a possible membrane binding motif.  (+info)

Legionella taurinensis sp. nov., a new species antigenically similar to Legionella spiritensis. (8/1440)

A group of 42 Legionella-like organisms reacting specifically with Legionella spiritensis serogroup 1 antisera were collected throughout Europe by the Centre National de Reference (French National Reference Centre) for Legionella. This group of isolates differed somewhat from L. spiritensis in terms of biochemical reactions, ubiquinone content and protein profile. The latter two analyses revealed that one of these L. spiritensis-like isolates, Turin I no. 1T, was highly related, but not identical to any of the red autofluorescent species of Legionella. In fact, this strain was the first of these particular isolates recognized to emit a red autofluorescence when exposed to UV light. Profile analysis of randomly amplified polymorphic DNA established that the red autofluorescent L. spiritensis-like isolates constituted a homogeneous group distinct from Legionella rubrilucens and Legionella erythra. DNA-DNA hybridization studies involving the use of S1 nuclease confirmed that the indicated group of isolates are a new species of Legionella, for which the name Legionella taurinensis is proposed with strain Turin I no. 1T (deposited as ATCC 700508T) as the type strain.  (+info)

Ubiquinone, also known as coenzyme Q10 (CoQ10), is a lipid-soluble benzoquinone that plays a crucial role in the mitochondrial electron transport chain as an essential component of Complexes I, II, and III. It functions as an electron carrier, assisting in the transfer of electrons from reduced nicotinamide adenine dinucleotide (NADH) and flavin adenine dinucleotide (FADH2) to molecular oxygen during oxidative phosphorylation, thereby contributing to the generation of adenosine triphosphate (ATP), the primary energy currency of the cell.

Additionally, ubiquinone acts as a potent antioxidant in both membranes and lipoproteins, protecting against lipid peroxidation and oxidative damage to proteins and DNA. Its antioxidant properties stem from its ability to donate electrons and regenerate other antioxidants like vitamin E. Ubiquinone is synthesized endogenously in all human cells, with the highest concentrations found in tissues with high energy demands, such as the heart, liver, kidneys, and skeletal muscles.

Deficiency in ubiquinone can result from genetic disorders, aging, or certain medications (such as statins), leading to impaired mitochondrial function and increased oxidative stress. Supplementation with ubiquinone has been explored as a potential therapeutic strategy for various conditions associated with mitochondrial dysfunction and oxidative stress, including cardiovascular diseases, neurodegenerative disorders, and cancer.

Electron Transport Complex I, also known as NADH:ubiquinone oxidoreductase, is a large protein complex located in the inner mitochondrial membrane of eukaryotic cells and the cytoplasmic membrane of prokaryotic cells. It is the first complex in the electron transport chain, a series of protein complexes that transfer electrons from NADH to oxygen, driving the synthesis of ATP through chemiosmosis.

Complex I consists of multiple subunits, including a flavin mononucleotide (FMN) cofactor and several iron-sulfur clusters, which facilitate the oxidation of NADH and the reduction of ubiquinone (coenzyme Q). The energy released during this electron transfer process is used to pump protons across the membrane, creating a proton gradient that drives ATP synthesis.

Defects in Complex I can lead to various mitochondrial diseases, including neurological disorders and muscle weakness.

Quinone reductases are a group of enzymes that catalyze the reduction of quinones to hydroquinones, using NADH or NADPH as an electron donor. This reaction is important in the detoxification of quinones, which are potentially toxic compounds produced during the metabolism of certain drugs, chemicals, and endogenous substances.

There are two main types of quinone reductases: NQO1 (NAD(P)H:quinone oxidoreductase 1) and NQO2 (NAD(P)H:quinone oxidoreductase 2). NQO1 is a cytosolic enzyme that can reduce a wide range of quinones, while NQO2 is a mitochondrial enzyme with a narrower substrate specificity.

Quinone reductases have been studied for their potential role in cancer prevention and treatment, as they may help to protect cells from oxidative stress and DNA damage caused by quinones and other toxic compounds. Additionally, some quinone reductase inhibitors have been developed as chemotherapeutic agents, as they can enhance the cytotoxicity of certain drugs that require quinone reduction for activation.

Quinones are a class of organic compounds that contain a fully conjugated diketone structure. This structure consists of two carbonyl groups (C=O) separated by a double bond (C=C). Quinones can be found in various biological systems and synthetic compounds. They play important roles in many biochemical processes, such as electron transport chains and redox reactions. Some quinones are also known for their antimicrobial and anticancer properties. However, some quinones can be toxic or mutagenic at high concentrations.

Electron Transport Complex II, also known as succinate-Q oxidoreductase, is a key component of the electron transport chain in the inner mitochondrial membrane. It plays a crucial role in the process of cellular respiration, where it facilitates the transfer of electrons from succinate to ubiquinone (Q), thereby generating a proton gradient across the membrane. This gradient drives the synthesis of ATP, which is the primary source of energy for the cell.

The complex is composed of four core subunits: flavoprotein (Fp), iron-sulfur protein (Ip), cytochrome b (Cyb), and ubiquinone-binding protein (Qp). Electrons from succinate are accepted by FAD in the Fp subunit, and then transferred to the Ip subunit containing iron-sulfur clusters. From there, the electrons are moved to heme groups in the Cyb subunit, and finally passed on to ubiquinone at the Qp subunit.

In addition to its role in the electron transport chain, Complex II has been implicated in various cellular processes such as regulation of reactive oxygen species (ROS) production and modulation of apoptosis. Mutations in genes encoding Complex II subunits have been associated with several human diseases, including neurodegenerative disorders and cancer.

The Electron Transport Chain (ETC) is a series of complexes in the inner mitochondrial membrane that are involved in the process of cellular respiration. It is the final pathway for electrons derived from the oxidation of nutrients such as glucose, fatty acids, and amino acids to be transferred to molecular oxygen. This transfer of electrons drives the generation of a proton gradient across the inner mitochondrial membrane, which is then used by ATP synthase to produce ATP, the main energy currency of the cell.

The electron transport chain consists of four complexes (I-IV) and two mobile electron carriers (ubiquinone and cytochrome c). Electrons from NADH and FADH2 are transferred to Complex I and Complex II respectively, which then pass them along to ubiquinone. Ubiquinone then transfers the electrons to Complex III, which passes them on to cytochrome c. Finally, cytochrome c transfers the electrons to Complex IV, where they combine with oxygen and protons to form water.

The transfer of electrons through the ETC is accompanied by the pumping of protons from the mitochondrial matrix to the intermembrane space, creating a proton gradient. The flow of protons back across the inner membrane through ATP synthase drives the synthesis of ATP from ADP and inorganic phosphate.

Overall, the electron transport chain is a crucial process for generating energy in the form of ATP in the cell, and it plays a key role in many metabolic pathways.

NADH, NADPH oxidoreductases are a class of enzymes that catalyze the redox reaction between NADH or NADPH and various electron acceptors. These enzymes play a crucial role in cellular metabolism by transferring electrons from NADH or NADPH to other molecules, which is essential for many biochemical reactions.

NADH (nicotinamide adenine dinucleotide hydrogen) and NADPH (nicotinamide adenine dinucleotide phosphate hydrogen) are coenzymes that act as electron carriers in redox reactions. They consist of a nicotinamide ring, which undergoes reduction or oxidation by accepting or donating electrons and a proton (H+).

NADH, NADPH oxidoreductases are classified based on their structure and mechanism of action. Some examples include:

1. Dehydrogenases: These enzymes catalyze the oxidation of NADH or NADPH to NAD+ or NADP+ while reducing an organic substrate. Examples include lactate dehydrogenase, alcohol dehydrogenase, and malate dehydrogenase.
2. Oxidases: These enzymes catalyze the oxidation of NADH or NADPH to NAD+ or NADP+ while reducing molecular oxygen (O2) to water (H2O). Examples include NADH oxidase and NADPH oxidase.
3. Reductases: These enzymes catalyze the reduction of various electron acceptors using NADH or NADPH as a source of electrons. Examples include glutathione reductase, thioredoxin reductase, and nitrate reductase.

Overall, NADH, NADPH oxidoreductases are essential for maintaining the redox balance in cells and play a critical role in various metabolic pathways, including energy production, detoxification, and biosynthesis.

Yarrowia is a genus of fungi that belongs to the family of Dipodascaceae. It is a type of yeast that is often found in various environments, including plants, soil, and water. One species, Yarrowia lipolytica, has gained attention in biotechnology applications due to its ability to break down fats and oils, produce organic acids, and express heterologous proteins. It's also known to be an opportunistic pathogen in humans, causing rare but serious infections in individuals with weakened immune systems.

Succinate cytochrome c oxidoreductase, also known as complex II or succinate-Q-reductase, is an enzyme complex in the electron transport chain that plays a crucial role in cellular respiration. It is located in the inner mitochondrial membrane of eukaryotic cells and the cytoplasmic membrane of prokaryotic cells.

Complex II consists of four subunits ( flavoprotein, iron-sulfur protein, and two cytochromes ) that catalyze the oxidation of succinate to fumarate, reducing FAD to FADH2 in the process. The FADH2 then transfers its electrons to the iron-sulfur protein and subsequently to ubiquinone (Q), reducing it to ubiquinol (QH2). This transfer of electrons drives the proton pumping across the membrane, contributing to the formation of a proton gradient that is used for ATP synthesis.

Complex II is unique among the electron transport chain complexes because it can operate independently of the other complexes and does not span the entire width of the inner mitochondrial membrane. It also plays a role in the regulation of reactive oxygen species (ROS) production, making it an important target for understanding various diseases, including neurodegenerative disorders and cancer.

NADH dehydrogenase, also known as Complex I, is an enzyme complex in the electron transport chain located in the inner mitochondrial membrane. It catalyzes the oxidation of NADH to NAD+ and the reduction of coenzyme Q to ubiquinol, playing a crucial role in cellular respiration and energy production. The reaction involves the transfer of electrons from NADH to coenzyme Q, which contributes to the generation of a proton gradient across the membrane, ultimately leading to ATP synthesis. Defects in NADH dehydrogenase can result in various mitochondrial diseases and disorders.

Oxidation-Reduction (redox) reactions are a type of chemical reaction involving a transfer of electrons between two species. The substance that loses electrons in the reaction is oxidized, and the substance that gains electrons is reduced. Oxidation and reduction always occur together in a redox reaction, hence the term "oxidation-reduction."

In biological systems, redox reactions play a crucial role in many cellular processes, including energy production, metabolism, and signaling. The transfer of electrons in these reactions is often facilitated by specialized molecules called electron carriers, such as nicotinamide adenine dinucleotide (NAD+/NADH) and flavin adenine dinucleotide (FAD/FADH2).

The oxidation state of an element in a compound is a measure of the number of electrons that have been gained or lost relative to its neutral state. In redox reactions, the oxidation state of one or more elements changes as they gain or lose electrons. The substance that is oxidized has a higher oxidation state, while the substance that is reduced has a lower oxidation state.

Overall, oxidation-reduction reactions are fundamental to the functioning of living organisms and are involved in many important biological processes.

Electron Transport Complex III, also known as cytochrome bc1 complex or ubiquinol-cytochrome c reductase, is a protein complex located in the inner mitochondrial membrane of eukaryotic cells and the cytoplasmic membrane of prokaryotic cells. It plays a crucial role in the electron transport chain (ETC), a series of complexes that generate energy in the form of ATP through a process called oxidative phosphorylation.

In ETC, Electron Transport Complex III accepts electrons from ubiquinol and transfers them to cytochrome c. This electron transfer is coupled with the translocation of protons (H+ ions) across the membrane, creating an electrochemical gradient. The energy stored in this gradient drives the synthesis of ATP by ATP synthase.

Electron Transport Complex III consists of several subunits, including cytochrome b, cytochrome c1, and the Rieske iron-sulfur protein. These subunits work together to facilitate the electron transfer and proton translocation processes.

Succinate dehydrogenase (SDH) is an enzyme complex that plays a crucial role in the process of cellular respiration, specifically in the citric acid cycle (also known as the Krebs cycle) and the electron transport chain. It is located in the inner mitochondrial membrane of eukaryotic cells.

SDH catalyzes the oxidation of succinate to fumarate, converting it into a molecule of fadaquate in the process. During this reaction, two electrons are transferred from succinate to the FAD cofactor within the SDH enzyme complex, reducing it to FADH2. These electrons are then passed on to ubiquinone (CoQ), which is a mobile electron carrier in the electron transport chain, leading to the generation of ATP, the main energy currency of the cell.

SDH is also known as mitochondrial complex II because it is the second complex in the electron transport chain. Mutations in the genes encoding SDH subunits or associated proteins have been linked to various human diseases, including hereditary paragangliomas, pheochromocytomas, gastrointestinal stromal tumors (GISTs), and some forms of neurodegenerative disorders.

Glucose dehydrogenases (GDHs) are a group of enzymes that catalyze the oxidation of glucose to generate gluconic acid or glucuronic acid. This reaction involves the transfer of electrons from glucose to an electron acceptor, most commonly nicotinamide adenine dinucleotide (NAD+) or phenazine methosulfate (PMS).

GDHs are widely distributed in nature and can be found in various organisms, including bacteria, fungi, plants, and animals. They play important roles in different biological processes, such as glucose metabolism, energy production, and detoxification of harmful substances. Based on their cofactor specificity, GDHs can be classified into two main types: NAD(P)-dependent GDHs and PQQ-dependent GDHs.

NAD(P)-dependent GDHs use NAD+ or NADP+ as a cofactor to oxidize glucose to glucono-1,5-lactone, which is then hydrolyzed to gluconic acid by an accompanying enzyme. These GDHs are involved in various metabolic pathways, such as the Entner-Doudoroff pathway and the oxidative pentose phosphate pathway.

PQQ-dependent GDHs, on the other hand, use pyrroloquinoline quinone (PQQ) as a cofactor to catalyze the oxidation of glucose to gluconic acid directly. These GDHs are typically found in bacteria and play a role in energy production and detoxification.

Overall, glucose dehydrogenases are essential enzymes that contribute to the maintenance of glucose homeostasis and energy balance in living organisms.

NAD (Nicotinamide Adenine Dinucleotide) is a coenzyme found in all living cells. It plays an essential role in cellular metabolism, particularly in redox reactions, where it acts as an electron carrier. NAD exists in two forms: NAD+, which accepts electrons and becomes reduced to NADH. This pairing of NAD+/NADH is involved in many fundamental biological processes such as generating energy in the form of ATP during cellular respiration, and serving as a critical cofactor for various enzymes that regulate cellular functions like DNA repair, gene expression, and cell death.

Maintaining optimal levels of NAD+/NADH is crucial for overall health and longevity, as it declines with age and in certain disease states. Therefore, strategies to boost NAD+ levels are being actively researched for their potential therapeutic benefits in various conditions such as aging, neurodegenerative disorders, and metabolic diseases.

I'm happy to help! However, it seems like there are two terms combined into one request: "Mitochondria" and "Heart." I will provide separate definitions for each.

Mitochondrion (singular) or Mitochondria (plural): These are specialized structures found in the cytoplasm of most eukaryotic cells (cells with a true nucleus), including human cells. They are often referred to as the "powerhouse" of the cell because they generate energy in the form of ATP (adenosine triphosphate) through a process called oxidative phosphorylation. Mitochondria contain their own DNA, which is distinct from the nuclear DNA, and are believed to have originated from ancient bacteria that established a symbiotic relationship with primitive eukaryotic cells.

Heart: In human anatomy, the heart is a muscular organ responsible for pumping blood throughout the body. It is located in the thoracic cavity, slightly left of the center, and is enclosed by the pericardium, a double-walled sac that provides protection and lubrication for the heart's movement. The human heart is divided into four chambers: two atria on the top and two ventricles on the bottom. The right side of the heart receives deoxygenated blood from the body and pumps it to the lungs, while the left side receives oxygenated blood from the lungs and pumps it to the rest of the body. The heart's pumping action is regulated by electrical signals that originate in a group of specialized cardiac muscle cells called the sinoatrial node (SA node).

Ribosomal RNA (rRNA) is a type of RNA that combines with proteins to form ribosomes, which are complex structures inside cells where protein synthesis occurs. The "16S" refers to the sedimentation coefficient of the rRNA molecule, which is a measure of its size and shape. In particular, 16S rRNA is a component of the smaller subunit of the prokaryotic ribosome (found in bacteria and archaea), and is often used as a molecular marker for identifying and classifying these organisms due to its relative stability and conservation among species. The sequence of 16S rRNA can be compared across different species to determine their evolutionary relationships and taxonomic positions.

Rotenone is not strictly a medical term, but it is a pesticide that is used in some medical situations. According to the National Pesticide Information Center, rotenone is a pesticide derived from the roots and stems of several plants, including Derris Eliptica, Lonchocarpus utilis, and Tephrosia vogelii. It is used as a pesticide to control insects, mites, and fish in both agricultural and residential settings.

In medical contexts, rotenone has been studied for its potential effects on human health, particularly in relation to Parkinson's disease. Some research suggests that exposure to rotenone may increase the risk of developing Parkinson's disease, although more studies are needed to confirm this link. Rotenone works by inhibiting the mitochondria in cells, which can lead to cell death and neurodegeneration.

It is important to note that rotenone is highly toxic and should be handled with care. It can cause skin and eye irritation, respiratory problems, and gastrointestinal symptoms if ingested or inhaled. Therefore, it is recommended to use personal protective equipment when handling rotenone and to follow all label instructions carefully.

Ribosomal DNA (rDNA) refers to the specific regions of DNA in a cell that contain the genes for ribosomal RNA (rRNA). Ribosomes are complex structures composed of proteins and rRNA, which play a crucial role in protein synthesis by translating messenger RNA (mRNA) into proteins.

In humans, there are four types of rRNA molecules: 18S, 5.8S, 28S, and 5S. These rRNAs are encoded by multiple copies of rDNA genes that are organized in clusters on specific chromosomes. In humans, the majority of rDNA genes are located on the short arms of acrocentric chromosomes 13, 14, 15, 21, and 22.

Each cluster of rDNA genes contains both transcribed and non-transcribed spacer regions. The transcribed regions contain the genes for the four types of rRNA, while the non-transcribed spacers contain regulatory elements that control the transcription of the rRNA genes.

The number of rDNA copies varies between species and even within individuals of the same species. The copy number can also change during development and in response to environmental factors. Variations in rDNA copy number have been associated with various diseases, including cancer and neurological disorders.

Electron-transferring flavoproteins (ETFs) are small protein molecules that play a crucial role in the electron transport chain in cells. They are responsible for accepting and donating electrons during various metabolic processes, particularly in the oxidation of fatty acids and amino acids.

ETFs contain a cofactor called flavin adenine dinucleotide (FAD), which can accept two electrons and two protons to form a reduced form of FAD (FADH2). When ETFs receive electrons from other molecules, they transfer these electrons to another protein called electron-transferring flavoprotein dehydrogenase (ETFDH), which then donates the electrons to the main electron transport chain.

Defects in ETFs or ETFDH can lead to serious metabolic disorders, such as multiple acyl-CoA dehydrogenase deficiency (MADD), also known as glutaric acidemia type II. This disorder affects the body's ability to break down certain fats and amino acids, leading to a buildup of toxic compounds in the body and potentially causing serious health problems.

Dolichol is a type of lipid molecule that is involved in the process of protein glycosylation within the endoplasmic reticulum of eukaryotic cells. Glycosylation is the attachment of sugar molecules to proteins, and it plays a crucial role in various biological processes such as protein folding, trafficking, and cell-cell recognition.

Dolichols are long-chain polyisoprenoid alcohols that serve as carriers for the sugars during glycosylation. They consist of a hydrophobic tail made up of many isoprene units and a hydrophilic head group. The dolichol molecule is first activated by the addition of a diphosphate group to its terminal end, forming dolichyl pyrophosphate.

The sugars that will be attached to the protein are then transferred from their nucleotide sugar donors onto the dolichyl pyrophosphate carrier, creating a dolichol-linked oligosaccharide. This oligosaccharide is then transferred en bloc to the target protein in a process called "oligosaccharyltransferase" (OST) reaction.

Defects in dolichol biosynthesis or function can lead to various genetic disorders, such as congenital disorders of glycosylation (CDG), which are characterized by abnormal protein glycosylation and a wide range of clinical manifestations, including developmental delay, neurological impairment, and multi-systemic involvement.

Mitochondria are specialized structures located inside cells that convert the energy from food into ATP (adenosine triphosphate), which is the primary form of energy used by cells. They are often referred to as the "powerhouses" of the cell because they generate most of the cell's supply of chemical energy. Mitochondria are also involved in various other cellular processes, such as signaling, differentiation, and apoptosis (programmed cell death).

Mitochondria have their own DNA, known as mitochondrial DNA (mtDNA), which is inherited maternally. This means that mtDNA is passed down from the mother to her offspring through the egg cells. Mitochondrial dysfunction has been linked to a variety of diseases and conditions, including neurodegenerative disorders, diabetes, and aging.

Submitochondrial particles, also known as "submitochondrial vesicles" or "inner membrane fragments," are small particles that consist of the inner mitochondrial membrane and the associated components. They are obtained through sonication or other methods of disrupting mitochondria, which results in breaking down the outer membrane while leaving the inner membrane intact. These particles can be used in various biochemical studies to investigate the structure, function, and composition of the inner mitochondrial membrane and its components, such as the electron transport chain and ATP synthase complexes.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Base composition in genetics refers to the relative proportion of the four nucleotide bases (adenine, thymine, guanine, and cytosine) in a DNA or RNA molecule. In DNA, adenine pairs with thymine, and guanine pairs with cytosine, so the base composition is often expressed in terms of the ratio of adenine + thymine (A-T) to guanine + cytosine (G-C). This ratio can vary between species and even between different regions of the same genome. The base composition can provide important clues about the function, evolution, and structure of genetic material.

Iron-sulfur proteins are a group of metalloproteins that contain iron and sulfur atoms in their active centers. These clusters of iron and sulfur atoms, also known as iron-sulfur clusters, can exist in various forms, including Fe-S, 2Fe-2S, 3Fe-4S, and 4Fe-4S structures. The iron atoms are coordinated to the protein through cysteine residues, while the sulfur atoms can be in the form of sulfide (S2-) or sulfane (-S-).

These proteins play crucial roles in many biological processes, such as electron transfer, redox reactions, and enzyme catalysis. They are found in various organisms, from bacteria to humans, and are involved in a wide range of cellular functions, including energy metabolism, photosynthesis, nitrogen fixation, and DNA repair.

Iron-sulfur proteins can be classified into several categories based on their structure and function, such as ferredoxins, Rieske proteins, high-potential iron-sulfur proteins (HiPIPs), and radical SAM enzymes. Dysregulation or mutations in iron-sulfur protein genes have been linked to various human diseases, including neurodegenerative disorders, cancer, and mitochondrial disorders.

Glucose 1-Dehydrogenase (G1DH) is an enzyme that catalyzes the oxidation of β-D-glucose into D-glucono-1,5-lactone and reduces the cofactor NAD+ into NADH. This reaction plays a role in various biological processes, including glucose sensing and detoxification of reactive carbonyl species. G1DH is found in many organisms, including humans, and has several isoforms with different properties and functions.

Oxidoreductases are a class of enzymes that catalyze oxidation-reduction reactions, which involve the transfer of electrons from one molecule (the reductant) to another (the oxidant). These enzymes play a crucial role in various biological processes, including energy production, metabolism, and detoxification.

The oxidoreductase-catalyzed reaction typically involves the donation of electrons from a reducing agent (donor) to an oxidizing agent (acceptor), often through the transfer of hydrogen atoms or hydride ions. The enzyme itself does not undergo any permanent chemical change during this process, but rather acts as a catalyst to lower the activation energy required for the reaction to occur.

Oxidoreductases are classified and named based on the type of electron donor or acceptor involved in the reaction. For example, oxidoreductases that act on the CH-OH group of donors are called dehydrogenases, while those that act on the aldehyde or ketone groups are called oxidases. Other examples include reductases, peroxidases, and catalases.

Understanding the function and regulation of oxidoreductases is important for understanding various physiological processes and developing therapeutic strategies for diseases associated with impaired redox homeostasis, such as cancer, neurodegenerative disorders, and cardiovascular disease.

Antimycin A is an antibiotic substance produced by various species of Streptomyces bacteria. It is known to inhibit the electron transport chain in mitochondria, which can lead to cellular dysfunction and death. Antimycin A has been used in research to study the mechanisms of cellular respiration and oxidative phosphorylation.

In a medical context, antimycin A is not used as a therapeutic agent due to its toxicity to mammalian cells. However, it may be used in laboratory settings to investigate various biological processes or to develop new therapies for diseases related to mitochondrial dysfunction.

Fatty acids are carboxylic acids with a long aliphatic chain, which are important components of lipids and are widely distributed in living organisms. They can be classified based on the length of their carbon chain, saturation level (presence or absence of double bonds), and other structural features.

The two main types of fatty acids are:

1. Saturated fatty acids: These have no double bonds in their carbon chain and are typically solid at room temperature. Examples include palmitic acid (C16:0) and stearic acid (C18:0).
2. Unsaturated fatty acids: These contain one or more double bonds in their carbon chain and can be further classified into monounsaturated (one double bond) and polyunsaturated (two or more double bonds) fatty acids. Examples of unsaturated fatty acids include oleic acid (C18:1, monounsaturated), linoleic acid (C18:2, polyunsaturated), and alpha-linolenic acid (C18:3, polyunsaturated).

Fatty acids play crucial roles in various biological processes, such as energy storage, membrane structure, and cell signaling. Some essential fatty acids cannot be synthesized by the human body and must be obtained through dietary sources.

Phylogeny is the evolutionary history and relationship among biological entities, such as species or genes, based on their shared characteristics. In other words, it refers to the branching pattern of evolution that shows how various organisms have descended from a common ancestor over time. Phylogenetic analysis involves constructing a tree-like diagram called a phylogenetic tree, which depicts the inferred evolutionary relationships among organisms or genes based on molecular sequence data or other types of characters. This information is crucial for understanding the diversity and distribution of life on Earth, as well as for studying the emergence and spread of diseases.

Succinic acid, also known as butanedioic acid, is an organic compound with the chemical formula HOOC(CH2)2COOH. It is a white crystalline powder that is soluble in water and has a slightly acerbic taste. In medicine, succinic acid is not used as a treatment for any specific condition. However, it is a naturally occurring substance found in the body and plays a role in the citric acid cycle, which is a key process in energy production within cells. It can also be found in some foods and is used in the manufacturing of various products such as pharmaceuticals, resins, and perfumes.

Mevalonic acid is not a term that is typically used in medical definitions, but rather it is a biochemical concept. Mevalonic acid is a key intermediate in the biosynthetic pathway for cholesterol and other isoprenoids. It is formed from 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) by the enzyme HMG-CoA reductase, which is the target of cholesterol-lowering drugs known as statins.

In a medical context, mevalonic acid may be mentioned in relation to certain rare genetic disorders, such as mevalonate kinase deficiency (MKD) or hyperimmunoglobulinemia D and periodic fever syndrome (HIDS), which are caused by mutations in the gene encoding mevalonate kinase, an enzyme involved in the metabolism of mevalonic acid. These conditions can cause recurrent fevers, rashes, joint pain, and other symptoms.

Cytochrome b is a type of cytochrome, which is a class of proteins that contain heme as a cofactor and are involved in electron transfer. Cytochromes are classified based on the type of heme they contain and their absorption spectra.

The cytochrome b group includes several subfamilies of cytochromes, including cytochrome b5, cytochrome b2, and cytochrome bc1 (also known as complex III). These cytochromes are involved in various biological processes, such as fatty acid desaturation, steroid metabolism, and the electron transport chain.

The electron transport chain is a series of protein complexes in the inner mitochondrial membrane that generates most of the ATP (adenosine triphosphate) required for cellular energy production. Cytochrome bc1 is a key component of the electron transport chain, where it functions as a dimer and catalyzes the transfer of electrons from ubiquinol to cytochrome c while simultaneously pumping protons across the membrane. This creates an electrochemical gradient that drives ATP synthesis.

Deficiencies or mutations in cytochrome b genes can lead to various diseases, such as mitochondrial disorders and cancer.

Parabens are a group of synthetic preservatives that have been widely used in the cosmetics and personal care product industry since the 1920s. They are effective at inhibiting the growth of bacteria, yeasts, and molds, which helps to prolong the shelf life of these products. Parabens are commonly found in shampoos, conditioners, lotions, creams, deodorants, and other personal care items.

The most commonly used parabens include methylparaben, ethylparaben, propylparaben, and butylparaben. These compounds are often used in combination to provide broad-spectrum protection against microbial growth. Parabens work by penetrating the cell wall of microorganisms and disrupting their metabolism, which prevents them from multiplying.

Parabens have been approved for use as preservatives in cosmetics and personal care products by regulatory agencies around the world, including the U.S. Food and Drug Administration (FDA) and the European Commission's Scientific Committee on Consumer Safety (SCCS). However, there has been some controversy surrounding their safety, with concerns raised about their potential to mimic the hormone estrogen in the body and disrupt normal endocrine function.

While some studies have suggested that parabens may be associated with health problems such as breast cancer and reproductive toxicity, the evidence is not conclusive, and more research is needed to fully understand their potential risks. In response to these concerns, many manufacturers have begun to remove parabens from their products or offer paraben-free alternatives. It's important to note that while avoiding parabens may be a personal preference for some individuals, there is currently no scientific consensus on the need to avoid them entirely.

Rhodobacteraceae is a family of purple nonsulfur bacteria within the class Alphaproteobacteria. These bacteria are gram-negative, facultatively anaerobic or aerobic, and can perform photosynthesis under appropriate conditions. They are widely distributed in various environments such as freshwater, marine, and terrestrial habitats. Some members of this family are capable of nitrogen fixation, denitrification, and sulfur oxidation. They play important roles in biogeochemical cycles and have potential applications in wastewater treatment and bioenergy production.

Coenzymes are small organic molecules that assist enzymes in catalyzing chemical reactions within cells. They typically act as carriers of specific atoms or groups of atoms during enzymatic reactions, facilitating the conversion of substrates into products. Coenzymes often bind temporarily to enzymes at the active site, forming an enzyme-coenzyme complex.

Coenzymes are usually derived from vitamins or minerals and are essential for maintaining proper metabolic functions in the body. Examples of coenzymes include nicotinamide adenine dinucleotide (NAD+), flavin adenine dinucleotide (FAD), and coenzyme A (CoA). When a coenzyme is used up in a reaction, it must be regenerated or replaced for the enzyme to continue functioning.

In summary, coenzymes are vital organic compounds that work closely with enzymes to facilitate biochemical reactions, ensuring the smooth operation of various metabolic processes within living organisms.

Electron Spin Resonance (ESR) Spectroscopy, also known as Electron Paramagnetic Resonance (EPR) Spectroscopy, is a technique used to investigate materials with unpaired electrons. It is based on the principle of absorption of energy by the unpaired electrons when they are exposed to an external magnetic field and microwave radiation.

In this technique, a sample is placed in a magnetic field and microwave radiation is applied. The unpaired electrons in the sample absorb energy and change their spin state when the energy of the microwaves matches the energy difference between the spin states. This absorption of energy is recorded as a function of the magnetic field strength, producing an ESR spectrum.

ESR spectroscopy can provide information about the number, type, and behavior of unpaired electrons in a sample, as well as the local environment around the electron. It is widely used in physics, chemistry, and biology to study materials such as free radicals, transition metal ions, and defects in solids.

rRNA (ribosomal RNA) is not a type of gene itself, but rather a crucial component that is transcribed from genes known as ribosomal DNA (rDNA). In cells, rRNA plays an essential role in protein synthesis by assembling with ribosomal proteins to form ribosomes. Ribosomes are complex structures where the translation of mRNA into proteins occurs. There are multiple types of rRNA molecules, including 5S, 5.8S, 18S, and 28S rRNAs in eukaryotic cells, each with specific functions during protein synthesis.

In summary, 'Genes, rRNA' would refer to the genetic regions (genes) that code for ribosomal RNA molecules, which are vital components of the protein synthesis machinery within cells.

Cytochromes are a type of hemeprotein found in the mitochondria and other cellular membranes of organisms. They contain a heme group, which is a prosthetic group composed of an iron atom surrounded by a porphyrin ring. This structure allows cytochromes to participate in redox reactions, acting as electron carriers in various biological processes.

There are several types of cytochromes, classified based on the type of heme they contain and their absorption spectra. Some of the most well-known cytochromes include:

* Cytochrome c: a small, mobile protein found in the inner mitochondrial membrane that plays a crucial role in the electron transport chain during cellular respiration.
* Cytochrome P450: a large family of enzymes involved in the metabolism of drugs, toxins, and other xenobiotics. They are found in various tissues, including the liver, lungs, and skin.
* Cytochrome b: a component of several electron transport chains, including those found in mitochondria, bacteria, and chloroplasts.

Cytochromes play essential roles in energy production, detoxification, and other metabolic processes, making them vital for the survival and function of living organisms.

Benzoquinones are a type of chemical compound that contain a benzene ring (a cyclic arrangement of six carbon atoms) with two ketone functional groups (-C=O) in the 1,4-positions. They exist in two stable forms, namely ortho-benzoquinone and para-benzoquinone, depending on the orientation of the ketone groups relative to each other.

Benzoquinones are important intermediates in various biological processes and are also used in industrial applications such as dyes, pigments, and pharmaceuticals. They can be produced synthetically or obtained naturally from certain plants and microorganisms.

In the medical field, benzoquinones have been studied for their potential therapeutic effects, particularly in the treatment of cancer and infectious diseases. However, they are also known to exhibit toxicity and may cause adverse reactions in some individuals. Therefore, further research is needed to fully understand their mechanisms of action and potential risks before they can be safely used as drugs or therapies.

Succinates, in a medical context, most commonly refer to the salts or esters of succinic acid. Succinic acid is a dicarboxylic acid that is involved in the Krebs cycle, which is a key metabolic pathway in cells that generates energy through the oxidation of acetyl-CoA derived from carbohydrates, fats, and proteins.

Succinates can also be used as a buffer in medical solutions and as a pharmaceutical intermediate in the synthesis of various drugs. In some cases, succinate may be used as a nutritional supplement or as a component of parenteral nutrition formulations to provide energy and help maintain acid-base balance in patients who are unable to eat normally.

It's worth noting that there is also a condition called "succinic semialdehyde dehydrogenase deficiency" which is a genetic disorder that affects the metabolism of the amino acid gamma-aminobutyric acid (GABA). This condition can lead to an accumulation of succinic semialdehyde and other metabolic byproducts, which can cause neurological symptoms such as developmental delay, hypotonia, and seizures.

Bacterial DNA refers to the genetic material found in bacteria. It is composed of a double-stranded helix containing four nucleotide bases - adenine (A), thymine (T), guanine (G), and cytosine (C) - that are linked together by phosphodiester bonds. The sequence of these bases in the DNA molecule carries the genetic information necessary for the growth, development, and reproduction of bacteria.

Bacterial DNA is circular in most bacterial species, although some have linear chromosomes. In addition to the main chromosome, many bacteria also contain small circular pieces of DNA called plasmids that can carry additional genes and provide resistance to antibiotics or other environmental stressors.

Unlike eukaryotic cells, which have their DNA enclosed within a nucleus, bacterial DNA is present in the cytoplasm of the cell, where it is in direct contact with the cell's metabolic machinery. This allows for rapid gene expression and regulation in response to changing environmental conditions.

'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.

While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.

E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.

Aerobiosis is the process of living, growing, and functioning in the presence of oxygen. It refers to the metabolic processes that require oxygen to break down nutrients and produce energy in cells. This is in contrast to anaerobiosis, which is the ability to live and grow in the absence of oxygen.

In medical terms, aerobiosis is often used to describe the growth of microorganisms, such as bacteria and fungi, that require oxygen to survive and multiply. These organisms are called aerobic organisms, and they play an important role in many biological processes, including decomposition and waste breakdown.

However, some microorganisms are unable to grow in the presence of oxygen and are instead restricted to environments where oxygen is absent or limited. These organisms are called anaerobic organisms, and their growth and metabolism are referred to as anaerobiosis.

Sphingomonadaceae is a family of gram-negative, aerobic bacteria that are commonly found in various environments such as soil, water, and clinical samples. They are characterized by the presence of sphingophospholipids in their outer membrane, which differentiates them from other gram-negative bacteria.

Members of this family are often rod-shaped or coccoid and may be motile or nonmotile. Some species have the ability to degrade various organic compounds, including polychlorinated biphenyls (PCBs) and other aromatic hydrocarbons.

Sphingomonadaceae includes several genera of medical importance, such as Sphingomonas, Sphingopyxis, and Novosphingobium. These bacteria have been associated with various infections in humans, including bacteremia, pneumonia, meningitis, and urinary tract infections, particularly in immunocompromised patients. However, they are generally considered to be opportunistic pathogens, and their clinical significance is not well understood.

Acetobacteraceae is a family of gram-negative, aerobic bacteria that are capable of converting ethanol into acetic acid, a process known as oxidative fermentation. These bacteria are commonly found in environments such as fruits, flowers, and the gut of insects. They are also used in the industrial production of vinegar and other products. Some members of this family can cause food spoilage or infections in humans with weakened immune systems.

Rhodobacter sphaeroides is not a medical term, but rather a scientific name for a type of bacteria. It belongs to the class of proteobacteria and is commonly found in soil, fresh water, and the ocean. This bacterium is capable of photosynthesis, and it can use light as an energy source, converting it into chemical energy. Rhodobacter sphaeroides is often studied in research settings due to its unique metabolic capabilities and potential applications in biotechnology.

In a medical context, Rhodobacter sphaeroides may be mentioned in relation to rare cases of infection, particularly in individuals with weakened immune systems. However, it is not considered a significant human pathogen, and there are no specific medical definitions associated with this bacterium.

A proton pump is a specialized protein structure that functions as an enzyme, known as a proton pump ATPase, which actively transports hydrogen ions (protons) across a membrane. This process creates a gradient of hydrogen ions, resulting in an electrochemical potential difference, also known as a proton motive force. The main function of proton pumps is to generate and maintain this gradient, which can be used for various purposes, such as driving the synthesis of ATP (adenosine triphosphate) or transporting other molecules against their concentration gradients.

In the context of gastric physiology, the term "proton pump" often refers to the H+/K+-ATPase present in the parietal cells of the stomach. This proton pump is responsible for secreting hydrochloric acid into the stomach lumen, contributing to the digestion and sterilization of ingested food. Inhibiting this specific proton pump with medications like proton pump inhibitors (PPIs) is a common treatment strategy for gastric acid-related disorders such as gastroesophageal reflux disease (GERD), peptic ulcers, and Zollinger-Ellison syndrome.

Bacterial typing techniques are methods used to identify and differentiate bacterial strains or isolates based on their unique characteristics. These techniques are essential in epidemiological studies, infection control, and research to understand the transmission dynamics, virulence, and antibiotic resistance patterns of bacterial pathogens.

There are various bacterial typing techniques available, including:

1. **Bacteriophage Typing:** This method involves using bacteriophages (viruses that infect bacteria) to identify specific bacterial strains based on their susceptibility or resistance to particular phages.
2. **Serotyping:** It is a technique that differentiates bacterial strains based on the antigenic properties of their cell surface components, such as capsules, flagella, and somatic (O) and flagellar (H) antigens.
3. **Biochemical Testing:** This method uses biochemical reactions to identify specific metabolic pathways or enzymes present in bacterial strains, which can be used for differentiation. Commonly used tests include the catalase test, oxidase test, and various sugar fermentation tests.
4. **Molecular Typing Techniques:** These methods use genetic markers to identify and differentiate bacterial strains at the DNA level. Examples of molecular typing techniques include:
* **Pulsed-Field Gel Electrophoresis (PFGE):** This method uses restriction enzymes to digest bacterial DNA, followed by electrophoresis in an agarose gel under pulsed electrical fields. The resulting banding patterns are analyzed and compared to identify related strains.
* **Multilocus Sequence Typing (MLST):** It involves sequencing specific housekeeping genes to generate unique sequence types that can be used for strain identification and phylogenetic analysis.
* **Whole Genome Sequencing (WGS):** This method sequences the entire genome of a bacterial strain, providing the most detailed information on genetic variation and relatedness between strains. WGS data can be analyzed using various bioinformatics tools to identify single nucleotide polymorphisms (SNPs), gene deletions or insertions, and other genetic changes that can be used for strain differentiation.

These molecular typing techniques provide higher resolution than traditional methods, allowing for more accurate identification and comparison of bacterial strains. They are particularly useful in epidemiological investigations to track the spread of pathogens and identify outbreaks.

Alkyl and aryl transferases are a group of enzymes that catalyze the transfer of alkyl or aryl groups from one molecule to another. These enzymes play a role in various biological processes, including the metabolism of drugs and other xenobiotics, as well as the biosynthesis of certain natural compounds.

Alkyl transferases typically catalyze the transfer of methyl or ethyl groups, while aryl transferases transfer larger aromatic rings. These enzymes often use cofactors such as S-adenosylmethionine (SAM) or acetyl-CoA to donate the alkyl or aryl group to a recipient molecule.

Examples of alkyl and aryl transferases include:

1. Methyltransferases: enzymes that transfer methyl groups from SAM to various acceptor molecules, such as DNA, RNA, proteins, and small molecules.
2. Histone methyltransferases: enzymes that methylate specific residues on histone proteins, which can affect chromatin structure and gene expression.
3. N-acyltransferases: enzymes that transfer acetyl or other acyl groups to amino groups in proteins or small molecules.
4. O-acyltransferases: enzymes that transfer acyl groups to hydroxyl groups in lipids, steroids, and other molecules.
5. Arylsulfatases: enzymes that remove sulfate groups from aromatic rings, releasing an alcohol and sulfate.
6. Glutathione S-transferases (GSTs): enzymes that transfer the tripeptide glutathione to electrophilic centers in xenobiotics and endogenous compounds, facilitating their detoxification and excretion.

Alphaproteobacteria is a class of proteobacteria, a group of gram-negative bacteria. This class includes a diverse range of bacterial species that can be found in various environments, such as soil, water, and the surfaces of plants and animals. Some notable members of Alphaproteobacteria include the nitrogen-fixing bacteria Rhizobium and Bradyrhizobium, which form symbiotic relationships with the roots of leguminous plants, as well as the pathogenic bacteria Rickettsia, which are responsible for causing diseases such as typhus and Rocky Mountain spotted fever.

The Alphaproteobacteria class is further divided into several orders, including Rhizobiales, Rhodobacterales, and Caulobacterales. These orders contain a variety of bacterial species that have different characteristics and ecological roles. For example, members of the order Rhizobiales are known for their ability to fix nitrogen, while members of the order Rhodobacterales include photosynthetic bacteria that can use light as an energy source.

Overall, Alphaproteobacteria is a diverse and important group of bacteria that play various roles in the environment and in the health of plants and animals.

Sphingomonas is a genus of gram-negative, aerobic bacteria that are widely distributed in the environment. They are known for their ability to degrade various organic compounds and are often found in water, soil, and air samples. The cells of Sphingomonas species are typically straight or slightly curved rods, and they do not form spores.

One distinctive feature of Sphingomonas species is the presence of a unique lipid called sphingolipid in their cell membranes. This lipid contains a long-chain base called sphingosine, which is not found in the cell membranes of other gram-negative bacteria. The genus Sphingomonas includes several species that have been associated with human infections, particularly in immunocompromised individuals. These infections can include bacteremia, pneumonia, and urinary tract infections. However, Sphingomonas species are generally considered to be of low virulence and are not typically regarded as major pathogens.

Uncoupling agents are chemicals that interfere with the normal process of oxidative phosphorylation in cells. In this process, the energy from food is converted into ATP (adenosine triphosphate), which is the main source of energy for cellular functions. Uncouplers disrupt this process by preventing the transfer of high-energy electrons to oxygen, which normally drives the production of ATP.

Instead, the energy from these electrons is released as heat, leading to an increase in body temperature. This effect is similar to what happens during shivering or exercise, when the body generates heat to maintain its core temperature. Uncoupling agents are therefore also known as "mitochondrial protonophores" because they allow protons to leak across the inner mitochondrial membrane, bypassing the ATP synthase enzyme that would normally use the energy from this proton gradient to produce ATP.

Uncoupling agents have been studied for their potential therapeutic uses, such as in weight loss and the treatment of metabolic disorders. However, they can also be toxic at high doses, and their long-term effects on health are not well understood.

Hydroxyquinolines are a group of synthetic antimicrobial agents that contain a hydroxyl group (-OH) attached to a quinoline ring. They have been used in the treatment of various bacterial, fungal, and parasitic infections. Some common examples of hydroxyquinolines include chloroquine, hydroxychloroquine, and quinacrine. These agents work by inhibiting the growth and multiplication of microorganisms, although their exact mechanisms of action may vary. Chloroquine and hydroxychloroquine, for example, are known to interfere with the replication of the malaria parasite within red blood cells, while quinacrine has been used to treat certain types of protozoal infections.

It is important to note that the use of hydroxyquinolines is associated with a number of potential side effects and risks, including gastrointestinal disturbances, visual disturbances, and cardiac toxicity. As such, they should only be used under the close supervision of a healthcare professional.

Flavins are a group of naturally occurring organic compounds that contain a characteristic isoalloxazine ring, which is a tricyclic aromatic structure. The most common and well-known flavin is flavin adenine dinucleotide (FAD), which plays a crucial role as a coenzyme in various biological oxidation-reduction reactions. FAD accepts electrons and hydrogens to form the reduced form, flavin adenine dinucleotide hydride (FADH2). Another important flavin is flavin mononucleotide (FMN), which is derived from FAD and functions similarly as a coenzyme. Flavins are yellow in color and can be found in various biological systems, including animals, plants, and microorganisms. They are involved in several metabolic pathways, such as the electron transport chain, where they contribute to energy production.

"Cattle" is a term used in the agricultural and veterinary fields to refer to domesticated animals of the genus *Bos*, primarily *Bos taurus* (European cattle) and *Bos indicus* (Zebu). These animals are often raised for meat, milk, leather, and labor. They are also known as bovines or cows (for females), bulls (intact males), and steers/bullocks (castrated males). However, in a strict medical definition, "cattle" does not apply to humans or other animals.

I'm sorry for any confusion, but "Korea" is not a medical term. It refers to a region in East Asia that is divided into two distinct sovereign states: North Korea (officially the Democratic People's Republic of Korea) and South Korea (officially the Republic of Korea).

If you're looking for medical terms, I'd be happy to help. Could you please provide more context?

I apologize, but there seems to be a misunderstanding. "Soil microbiology" is not a medical term; rather, it is a branch of microbiology that deals with the study of microorganisms in soil. It involves understanding the diversity, ecology, and biochemistry of bacteria, fungi, algae, protozoa, and other microscopic life forms found in soil. This field has applications in agriculture, environmental science, and waste management but is not directly related to medical definitions or human health.

Alcaligenaceae is a family of gram-negative, aerobic or facultatively anaerobic bacteria that are commonly found in soil, water, and the gastrointestinal tracts of animals. Members of this family are typically oxidase-positive and catalase-positive, and they can use a variety of organic compounds as carbon sources. Some species of Alcaligenaceae have been associated with human disease, including respiratory infections, urinary tract infections, and bacteremia. However, these infections are relatively rare, and the majority of Alcaligenaceae species are not considered to be significant pathogens.

DNA Sequence Analysis is the systematic determination of the order of nucleotides in a DNA molecule. It is a critical component of modern molecular biology, genetics, and genetic engineering. The process involves determining the exact order of the four nucleotide bases - adenine (A), guanine (G), cytosine (C), and thymine (T) - in a DNA molecule or fragment. This information is used in various applications such as identifying gene mutations, studying evolutionary relationships, developing molecular markers for breeding, and diagnosing genetic diseases.

The process of DNA Sequence Analysis typically involves several steps, including DNA extraction, PCR amplification (if necessary), purification, sequencing reaction, and electrophoresis. The resulting data is then analyzed using specialized software to determine the exact sequence of nucleotides.

In recent years, high-throughput DNA sequencing technologies have revolutionized the field of genomics, enabling the rapid and cost-effective sequencing of entire genomes. This has led to an explosion of genomic data and new insights into the genetic basis of many diseases and traits.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

Multienzyme complexes are specialized protein structures that consist of multiple enzymes closely associated or bound together, often with other cofactors and regulatory subunits. These complexes facilitate the sequential transfer of substrates along a series of enzymatic reactions, also known as a metabolic pathway. By keeping the enzymes in close proximity, multienzyme complexes enhance reaction efficiency, improve substrate specificity, and maintain proper stoichiometry between different enzymes involved in the pathway. Examples of multienzyme complexes include the pyruvate dehydrogenase complex, the citrate synthase complex, and the fatty acid synthetase complex.

I'd be happy to help! However, I believe there might be a slight misunderstanding in your question. Mitochondria are organelles found in the cells of all complex living organisms, including humans, while the liver is a large, solid organ located in the upper right portion of the abdomen. They don't have a medical definition together. I can certainly provide you with separate definitions for each:

1. Mitochondria: These are double-membrane-bound cellular organelles that generate most of the chemical energy needed to power the cell's biochemical reactions. Commonly known as the "powerhouse of the cell," mitochondria convert organic substrates, such as glucose, fatty acids, and amino acids, into adenosine triphosphate (ATP) through a process called oxidative phosphorylation. Mitochondria are dynamic structures that can change their shape, size, and number through fission (division) and fusion (merging) processes. They play essential roles in various cellular functions, including calcium signaling, apoptosis (programmed cell death), and the regulation of cellular metabolism.

2. Liver: The liver is a large, lobulated organ that lies mainly in the upper right portion of the abdominal cavity, just below the diaphragm. It plays a crucial role in various physiological functions, such as detoxification, protein synthesis, metabolism, and nutrient storage. The liver is responsible for removing toxins from the bloodstream, producing bile to aid in digestion, regulating glucose levels, synthesizing plasma proteins, and storing glycogen, vitamins, and minerals. It also contributes to the metabolism of carbohydrates, lipids, and amino acids, helping maintain energy homeostasis in the body.

I hope this clarifies any confusion! If you have any further questions or need more information, please don't hesitate to ask.

Xanthomonadaceae is a family of Gram-negative, aerobic or facultatively anaerobic bacteria within the class Gammaproteobacteria. The bacteria in this family are typically motile with a single polar flagellum and have a characteristic yellow-pigmented xanthomonad chromosome. They are known to cause various plant diseases, including bacterial spot, bacterial leaf blight, and citrus canker. Some species can also be found as opportunistic pathogens in humans and animals.

It's important to note that medical definitions of bacteria typically focus on their role as human or animal pathogens, while Xanthomonadaceae has a broader ecological significance beyond just medical contexts.

Naphthoquinones are a type of organic compound that consists of a naphthalene ring (two benzene rings fused together) with two ketone functional groups (=O) at the 1 and 2 positions. They exist in several forms, including natural and synthetic compounds. Some well-known naphthoquinones include vitamin K1 (phylloquinone) and K2 (menaquinone), which are important for blood clotting and bone metabolism. Other naphthoquinones have been studied for their potential medicinal properties, including anticancer, antibacterial, and anti-inflammatory activities. However, some naphthoquinones can also be toxic or harmful to living organisms, so they must be used with caution.

Dicumarol is an anticoagulant medication that belongs to a class of compounds known as coumarins. It works by inhibiting the action of vitamin K, which is necessary for the production of certain clotting factors in the liver. This results in a decrease in blood clotting ability and helps prevent the formation of harmful blood clots.

Dicumarol is primarily used to treat and prevent deep vein thrombosis (DVT), pulmonary embolism, and other conditions that may require anticoagulation therapy. It is also used in the management of atrial fibrillation, valvular heart disease, and certain types of heart attacks.

It's important to note that dicumarol has a narrow therapeutic index, meaning that the difference between an effective dose and a toxic dose is relatively small. Therefore, it requires careful monitoring of blood clotting times (INR) to ensure that the drug is working effectively without causing excessive bleeding.

Dicumarol is available in oral form and is typically taken once or twice daily. Common side effects include nausea, vomiting, diarrhea, skin rash, and abnormal liver function tests. Rare but serious side effects include severe bleeding, necrosis of the skin and other tissues, and allergic reactions.

Dicumarol is a prescription medication that should only be used under the guidance of a healthcare professional. It interacts with many other medications and foods, so it's important to inform your doctor about all the drugs you are taking and any dietary changes you may make while on this medication.

Terpenes are a large and diverse class of organic compounds produced by a variety of plants, including cannabis. They are responsible for the distinctive aromas and flavors found in different strains of cannabis. Terpenes have been found to have various therapeutic benefits, such as anti-inflammatory, analgesic, and antimicrobial properties. Some terpenes may also enhance the psychoactive effects of THC, the main psychoactive compound in cannabis. It's important to note that more research is needed to fully understand the potential medical benefits and risks associated with terpenes.

Oxepins are organic compounds that contain a seven-membered ring with one oxygen atom and six carbon atoms. The structure of an oxepin is similar to that of benzene, but with one methine group (=CH−) replaced by an oxygen atom. This gives the oxepin ring a unique combination of aromaticity and reactivity, which makes it a subject of interest in organic chemistry and medicinal chemistry research.

Oxepins are relatively rare in nature, and they are not typically found in living organisms. However, some synthetic drugs contain an oxepin ring structure, and these compounds have been studied for their potential therapeutic uses. For example, some oxepin-containing drugs have been shown to have anti-inflammatory, antiviral, and antitumor properties.

It's worth noting that the term "oxepins" can also refer to a broader class of compounds that contain a seven-membered ring with one oxygen atom and any number of carbon atoms. However, in medical and pharmaceutical contexts, the term is most commonly used to refer specifically to the class of compounds described above.

Oxygen consumption, also known as oxygen uptake, is the amount of oxygen that is consumed or utilized by the body during a specific period of time, usually measured in liters per minute (L/min). It is a common measurement used in exercise physiology and critical care medicine to assess an individual's aerobic metabolism and overall health status.

In clinical settings, oxygen consumption is often measured during cardiopulmonary exercise testing (CPET) to evaluate cardiovascular function, pulmonary function, and exercise capacity in patients with various medical conditions such as heart failure, chronic obstructive pulmonary disease (COPD), and other respiratory or cardiac disorders.

During exercise, oxygen is consumed by the muscles to generate energy through a process called oxidative phosphorylation. The amount of oxygen consumed during exercise can provide important information about an individual's fitness level, exercise capacity, and overall health status. Additionally, measuring oxygen consumption can help healthcare providers assess the effectiveness of treatments and rehabilitation programs in patients with various medical conditions.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Brucellaceae is a family of gram-negative, facultatively anaerobic bacteria that are known to cause brucellosis in humans and animals. The bacteria in this family are small, coccobacillary or rod-shaped, and non-spore forming. They can survive for extended periods in harsh environments, making them difficult to eradicate.

The genus Brucella is the most well-known member of this family and includes several species that cause different forms of brucellosis. These include B. abortus (cattle), B. melitensis (goats and sheep), B. suis (pigs), and B. canis (dogs).

Brucellosis is a zoonotic disease, meaning it can be transmitted from animals to humans through direct contact with infected animals or consumption of contaminated food products such as unpasteurized milk or undercooked meat. The symptoms of brucellosis in humans include fever, chills, sweats, headaches, muscle and joint pain, and fatigue.

Prevention measures for brucellosis include vaccination of animals, pasteurization of dairy products, and cooking meat thoroughly before consumption. It is also important to practice good hygiene when handling animals or their byproducts.

Plastoquinone is a lipid-soluble electron carrier in the photosynthetic electron transport chain located in the thylakoid membrane of chloroplasts. It plays a crucial role in both the light-dependent reactions of photosynthesis and cyclic photophosphorylation.

In more detail, plastoquinone exists in an oxidized (PQ) and reduced form (PQH2). In its oxidized state, it accepts electrons from cytochrome b6f complex during the transfer of electrons from photosystem II to photosystem I. Once plastoquinone accepts two electrons and two protons, it converts into its reduced form, plastoquinol (PQH2). Plastoquinol then donates the electrons to the cytochrome b6f complex, which in turn passes them on to the next carrier in the electron transport chain.

Plastoquinone is a member of the quinone family and is synthesized via the methylerythritol 4-phosphate (MEP) pathway, also known as the non-mevalonate pathway.

"Paracoccus denitrificans" is not a medical term, but rather a term used in the field of microbiology. It refers to a species of gram-negative, facultatively anaerobic bacteria that are commonly found in soil and water environments. These bacteria are known for their ability to carry out denitrification, which is the process of converting nitrate (NO3-) to nitrogen gas (N2) under anaerobic conditions. This ability makes them important players in the global nitrogen cycle.

While "Paracoccus denitrificans" itself is not a medical term, certain strains of this bacterium have been used in medical research and biotechnology applications. For example, some researchers have studied the use of "Paracoccus denitrificans" as a potential agent for removing nitrogenous compounds from wastewater or for producing hydrogen gas through fermentation. However, there is no direct medical relevance to this bacterium in terms of human health or disease.

"Neurospora crassa" is not a medical term, but it is a scientific name used in the field of biology. It refers to a type of filamentous fungus that belongs to the phylum Ascomycota. This organism is commonly found in the environment and has been widely used as a model system for studying various biological processes, including genetics, cell biology, and molecular biology.

"Neurospora crassa" has a characteristic red pigment that makes it easy to identify, and it reproduces sexually through the formation of specialized structures called ascocarps or "fruiting bodies." The fungus undergoes meiosis inside these structures, resulting in the production of ascospores, which are haploid spores that can germinate and form new individuals.

The genome of "Neurospora crassa" was one of the first fungal genomes to be sequenced, and it has served as an important tool for understanding fundamental biological processes in eukaryotic cells. However, because it is not a medical term, there is no official medical definition for "Neurospora crassa."

'Acetobacter' is a genus of gram-negative, aerobic, rod-shaped bacteria that are commonly found in various environments such as soil, water, and plant surfaces. They are known for their ability to oxidize alcohols to aldehydes and then to carboxylic acids, particularly the oxidation of ethanol to acetic acid. This property makes them important in the production of vinegar and other fermented foods. Some species of Acetobacter can also cause food spoilage and may be associated with certain human infections, although they are not considered primary human pathogens.

In the context of medicine, particularly in relation to cancer treatment, protons refer to positively charged subatomic particles found in the nucleus of an atom. Proton therapy, a type of radiation therapy, uses a beam of protons to target and destroy cancer cells with high precision, minimizing damage to surrounding healthy tissue. The concentrated dose of radiation is delivered directly to the tumor site, reducing side effects and improving quality of life during treatment.

Vitamin K2, also known as menaquinone, is a fat-soluble vitamin that plays a crucial role in the blood clotting process and bone metabolism. It is one of the two main forms of Vitamin K (the other being Vitamin K1 or phylloquinone), and it is found in animal-based foods and fermented foods.

Vitamin K2 is a collective name for a group of vitamin K compounds characterized by the presence of a long-chain fatty acid attached to the molecule. The most common forms of Vitamin K2 are MK-4 and MK-7, which differ in the length of their side chains.

Vitamin K2 is absorbed more efficiently than Vitamin K1 and has a longer half-life, which means it stays in the body for a longer period. It is stored in various tissues, including bones, where it plays an essential role in maintaining bone health by assisting in the regulation of calcium deposition and helping to prevent the calcification of blood vessels and other soft tissues.

Deficiency in Vitamin K2 is rare but can lead to bleeding disorders and weakened bones. Food sources of Vitamin K2 include animal-based foods such as liver, egg yolks, and fermented dairy products like cheese and natto (a Japanese food made from fermented soybeans). Some studies suggest that supplementing with Vitamin K2 may have benefits for bone health, heart health, and cognitive function. However, more research is needed to confirm these potential benefits.

"Halomonas" is a genus of bacteria that are found in saline environments, such as salt lakes, marine habitats, and salted food products. These bacteria are characterized by their ability to grow optimally in media with high salt concentrations (up to 20-30% sodium chloride). They are generally rod-shaped and motile, with a gram-negative cell wall structure. Some species of Halomonas have been studied for their potential applications in biotechnology, such as the production of compatible solutes, enzymes, and biofuels. However, it is important to note that "Halomonas" is not a medical term per se, but rather a taxonomic designation used in microbiology and related fields.

An electron is a subatomic particle, symbol e-, with a negative electric charge. Electrons are fundamental components of atoms and are responsible for the chemical bonding between atoms to form molecules. They are located in an atom's electron cloud, which is the outermost region of an atom and contains negatively charged electrons that surround the positively charged nucleus.

Electrons have a mass that is much smaller than that of protons or neutrons, making them virtually weightless on the atomic scale. They are also known to exhibit both particle-like and wave-like properties, which is a fundamental concept in quantum mechanics. Electrons play a crucial role in various physical phenomena, such as electricity, magnetism, and chemical reactions.

Neoprene is not a medical term, but it is a material that is used in some medical applications. Neoprene is a type of synthetic rubber that is known for its flexibility, durability, and resistance to heat, water, and chemicals. It is often used in the manufacture of medical devices such as braces, supports, and protective gear.

In medical terms, neoprene may be referred to as a component of a device or material used in medical applications. For example, a neoprene sleeve may be used as a compression garment for venous insufficiency or lymphedema management. Neoprene is also sometimes used in the manufacture of medical gloves and other protective equipment due to its resistance to chemicals and other substances.

However, it's important to note that some people may have allergic reactions to neoprene, causing skin irritation or other symptoms. Therefore, healthcare providers should consider patients' individual needs and potential allergies when selecting medical devices made of neoprene or other materials.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

Thenoyltrifluoroacetone (TTA) is not typically considered a medical compound, but rather a chemical compound with potential uses in various fields including chemistry, biology, and materials science. However, I can provide a general definition:

Thenoyltrifluoroacetone is an organofluorine compound with the formula C6H3F3O2S. It is a colorless liquid that is used as a fluorinated ligand in coordination chemistry and as a reagent in organic synthesis. Its unique chemical properties, such as its ability to act as a metal chelator and its volatility, have led to its use in various applications. Please consult relevant technical or scientific literature for more specific information regarding its uses and properties.

Oxalobacteraceae is a family of gram-negative, aerobic or facultatively anaerobic bacteria within the order Burkholderiales. The bacteria in this family are known for their ability to metabolize oxalate, a compound that is commonly found in many plant-based foods and can be harmful in large amounts. The type genus of this family is Oxalobacter, which includes species such as Oxalobacter formigenes, which is normally found in the human gut and helps to break down oxalates in the digestive system. Other genera in this family include Massilia, Janthinobacterium, and Herbaspirillum, among others.

Seawater is not a medical term, but it is a type of water that covers more than 70% of the Earth's surface. Medically, seawater can be relevant in certain contexts, such as in discussions of marine biology, environmental health, or water safety. Seawater has a high salt content, with an average salinity of around 3.5%, which is much higher than that of freshwater. This makes it unsuitable for drinking or irrigation without desalination.

Exposure to seawater can also have medical implications, such as in cases of immersion injuries, marine envenomations, or waterborne illnesses. However, there is no single medical definition of seawater.

Comamonadaceae is a family of gram-negative, aerobic or facultatively anaerobic bacteria that are commonly found in various environments such as soil, water, and the rhizosphere of plants. The name Comamonadaceae comes from the type genus Comamonas. Members of this family are known to be metabolically versatile and can degrade a wide range of organic compounds, including aromatic compounds and polysaccharides. Some species in this family are also known to be opportunistic pathogens in humans, causing infections such as pneumonia, bacteremia, and meningitis.

I'm sorry for any confusion, but "Hemiterpenes" is not a recognized term in medical or biochemistry terminology. The term "terpene" does refer to a large class of naturally occurring organic hydrocarbons, which are synthesized in various plants and animals. They are built from repeating units of isoprene (a five-carbon molecule), and can be further classified into monoterpenes (two isoprene units), sesquiterpenes (three isoprene units), diterpenes (four isoprene units), and so on.

However, the prefix "hemi-" means "half," which doesn't have a clear application in this context. It's possible there may be a misunderstanding or a typo in your question. If you meant to ask about a specific type of compound or a concept related to terpenes, please provide more context so I can give a more accurate answer.

Ferricyanides are a class of chemical compounds that contain the ferricyanide ion (Fe(CN)6−3). The ferricyanide ion is composed of a central iron atom in the +3 oxidation state, surrounded by six cyanide ligands. Ferricyanides are strong oxidizing agents and are used in various chemical reactions, including analytical chemistry and as reagents in organic synthesis.

It's important to note that while ferricyanides themselves are not highly toxic, they can release cyanide ions if they are decomposed or reduced under certain conditions. Therefore, they should be handled with care and used in well-ventilated areas.

Flavin Mononucleotide (FMN) is a coenzyme that plays a crucial role in biological oxidation-reduction reactions. It is derived from the vitamin riboflavin (also known as vitamin B2) and is composed of a flavin molecule bonded to a nucleotide. FMN functions as an electron carrier, accepting and donating electrons in various metabolic pathways, including the citric acid cycle and the electron transport chain, which are essential for energy production in cells. It also participates in the detoxification of harmful substances and contributes to the maintenance of cellular redox homeostasis. FMN can exist in two forms: the oxidized form (FMN) and the reduced form (FMNH2), depending on its involvement in redox reactions.

Ochrobactrum is a genus of gram-negative, aerobic, rod-shaped bacteria that are widely distributed in various environments such as soil, water, and clinical samples. The bacteria are often resistant to multiple antibiotics and can cause opportunistic infections in humans, particularly in immunocompromised individuals.

Ochrobactrum species have been isolated from a variety of clinical specimens, including blood, urine, respiratory tract secretions, wounds, and the genitourinary tract. They have been associated with various types of infections, such as bacteremia, pneumonia, meningitis, endocarditis, and catheter-related infections.

The clinical significance of Ochrobactrum infections is not well understood due to their low virulence and the difficulty in distinguishing them from other gram-negative bacteria. However, they can be challenging to treat due to their resistance to multiple antibiotics, including beta-lactams, aminoglycosides, and fluoroquinolones.

In summary, Ochrobactrum is a genus of environmental bacteria that can cause opportunistic infections in humans, particularly in immunocompromised individuals. The clinical significance of these infections is not well understood, but they can be challenging to treat due to their antibiotic resistance.

Mitochondrial proteins are any proteins that are encoded by the nuclear genome or mitochondrial genome and are located within the mitochondria, an organelle found in eukaryotic cells. These proteins play crucial roles in various cellular processes including energy production, metabolism of lipids, amino acids, and steroids, regulation of calcium homeostasis, and programmed cell death or apoptosis.

Mitochondrial proteins can be classified into two main categories based on their origin:

1. Nuclear-encoded mitochondrial proteins (NEMPs): These are proteins that are encoded by genes located in the nucleus, synthesized in the cytoplasm, and then imported into the mitochondria through specific import pathways. NEMPs make up about 99% of all mitochondrial proteins and are involved in various functions such as oxidative phosphorylation, tricarboxylic acid (TCA) cycle, fatty acid oxidation, and mitochondrial dynamics.

2. Mitochondrial DNA-encoded proteins (MEPs): These are proteins that are encoded by the mitochondrial genome, synthesized within the mitochondria, and play essential roles in the electron transport chain (ETC), a key component of oxidative phosphorylation. The human mitochondrial genome encodes only 13 proteins, all of which are subunits of complexes I, III, IV, and V of the ETC.

Defects in mitochondrial proteins can lead to various mitochondrial disorders, which often manifest as neurological, muscular, or metabolic symptoms due to impaired energy production. These disorders are usually caused by mutations in either nuclear or mitochondrial genes that encode mitochondrial proteins.

Spectrophotometry is a technical analytical method used in the field of medicine and science to measure the amount of light absorbed or transmitted by a substance at specific wavelengths. This technique involves the use of a spectrophotometer, an instrument that measures the intensity of light as it passes through a sample.

In medical applications, spectrophotometry is often used in laboratory settings to analyze various biological samples such as blood, urine, and tissues. For example, it can be used to measure the concentration of specific chemicals or compounds in a sample by measuring the amount of light that is absorbed or transmitted at specific wavelengths.

In addition, spectrophotometry can also be used to assess the properties of biological tissues, such as their optical density and thickness. This information can be useful in the diagnosis and treatment of various medical conditions, including skin disorders, eye diseases, and cancer.

Overall, spectrophotometry is a valuable tool for medical professionals and researchers seeking to understand the composition and properties of various biological samples and tissues.

Hyphomicrobiaceae is a family of bacteria that are characterized by their unique mode of reproduction known as "budding." This type of reproduction involves the formation of a new cell, or bud, on the surface of the parent cell. Once the bud has reached a certain size, it will separate from the parent cell and become a fully functioning independent organism.

Members of Hyphomicrobiaceae are typically gram-negative, aerobic bacteria that are found in a variety of environments, including soil, water, and plant material. They are often associated with nitrogen fixation, a process by which certain bacteria are able to convert atmospheric nitrogen into ammonia, a form that can be used by plants for growth.

One notable genus within Hyphomicrobiaceae is Hyphomicrobium, which is known for its ability to oxidize methanol and other single-carbon compounds as a source of energy. This makes it an important player in the global carbon cycle, as it helps to convert methane, a potent greenhouse gas, into less harmful forms.

Overall, Hyphomicrobiaceae is an interesting family of bacteria with diverse metabolic capabilities and ecological roles.

Atovaquone is an antiprotozoal medication used for the treatment and prevention of certain parasitic infections. It works by inhibiting the mitochondria of the parasites, disrupting their energy production and ultimately leading to their death. Atovaquone is available as a oral suspension or coated tablets and is often prescribed for conditions such as Pneumocystis pneumonia (PCP), Toxoplasma gondii encephalitis, and babesiosis. It is also used for the prevention of PCP in people with weakened immune systems due to HIV/AIDS or other causes.

The medical definition of Atovaquone can be stated as:

"Atovaquone is an antiprotozoal medication (synthetic hydroxynaphthoquinone) that exhibits activity against a variety of protozoa, including Plasmodium falciparum (the parasite responsible for malaria), Pneumocystis jirovecii (the causative agent of PCP), Toxoplasma gondii, and Babesia microti. It is used primarily for the treatment and prevention of PCP in individuals with compromised immune systems, as well as for the treatment of babesiosis and toxoplasmosis."

A protein subunit refers to a distinct and independently folding polypeptide chain that makes up a larger protein complex. Proteins are often composed of multiple subunits, which can be identical or different, that come together to form the functional unit of the protein. These subunits can interact with each other through non-covalent interactions such as hydrogen bonds, ionic bonds, and van der Waals forces, as well as covalent bonds like disulfide bridges. The arrangement and interaction of these subunits contribute to the overall structure and function of the protein.

I'm sorry for any confusion, but there is no established medical or scientific definition for "Vitamin U." The term was used in the past to refer to a substance found in cabbage juice that seemed to help ulcers, but it's not recognized as a vitamin by modern nutrition standards. It's often referred to as methylmethionine or S-methylmethionine, which is a compound derived from the amino acid methionine. Please consult with a healthcare professional for medical advice.

1-Methyl-4-phenylpyridinium (MPP+) is a neurotoxic compound that is widely used in scientific research to study Parkinson's disease and other neurological disorders. MPP+ is an ionic form of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP), which is a lipophilic compound that can cross the blood-brain barrier and be converted to MPP+ by monoamine oxidase B (MAO-B) in glial cells.

MPP+ is taken up by dopaminergic neurons through the dopamine transporter (DAT), where it inhibits complex I of the electron transport chain, leading to mitochondrial dysfunction and energy depletion. This results in the death of dopaminergic neurons, which are the primary cells affected in Parkinson's disease.

MPP+ has been used as a model compound to study the mechanisms of neurodegeneration in Parkinson's disease and other neurological disorders, and it has also been used in the development of potential therapeutic strategies for these conditions.

Vitamin K is a fat-soluble vitamin that plays a crucial role in blood clotting and bone metabolism. It is essential for the production of several proteins involved in blood clotting, including factor II (prothrombin), factor VII, factor IX, and factor X. Additionally, Vitamin K is necessary for the synthesis of osteocalcin, a protein that contributes to bone health by regulating the deposition of calcium in bones.

There are two main forms of Vitamin K: Vitamin K1 (phylloquinone), which is found primarily in green leafy vegetables and some vegetable oils, and Vitamin K2 (menaquinones), which is produced by bacteria in the intestines and is also found in some fermented foods.

Vitamin K deficiency can lead to bleeding disorders such as hemorrhage and excessive bruising. While Vitamin K deficiency is rare in adults, it can occur in newborns who have not yet developed sufficient levels of the vitamin. Therefore, newborns are often given a Vitamin K injection shortly after birth to prevent bleeding problems.

Hydrogen-ion concentration, also known as pH, is a measure of the acidity or basicity of a solution. It is defined as the negative logarithm (to the base 10) of the hydrogen ion activity in a solution. The standard unit of measurement is the pH unit. A pH of 7 is neutral, less than 7 is acidic, and greater than 7 is basic.

In medical terms, hydrogen-ion concentration is important for maintaining homeostasis within the body. For example, in the stomach, a high hydrogen-ion concentration (low pH) is necessary for the digestion of food. However, in other parts of the body such as blood, a high hydrogen-ion concentration can be harmful and lead to acidosis. Conversely, a low hydrogen-ion concentration (high pH) in the blood can lead to alkalosis. Both acidosis and alkalosis can have serious consequences on various organ systems if not corrected.

'Escherichia coli (E. coli) proteins' refer to the various types of proteins that are produced and expressed by the bacterium Escherichia coli. These proteins play a critical role in the growth, development, and survival of the organism. They are involved in various cellular processes such as metabolism, DNA replication, transcription, translation, repair, and regulation.

E. coli is a gram-negative, facultative anaerobe that is commonly found in the intestines of warm-blooded organisms. It is widely used as a model organism in scientific research due to its well-studied genetics, rapid growth, and ability to be easily manipulated in the laboratory. As a result, many E. coli proteins have been identified, characterized, and studied in great detail.

Some examples of E. coli proteins include enzymes involved in carbohydrate metabolism such as lactase, sucrase, and maltose; proteins involved in DNA replication such as the polymerases, single-stranded binding proteins, and helicases; proteins involved in transcription such as RNA polymerase and sigma factors; proteins involved in translation such as ribosomal proteins, tRNAs, and aminoacyl-tRNA synthetases; and regulatory proteins such as global regulators, two-component systems, and transcription factors.

Understanding the structure, function, and regulation of E. coli proteins is essential for understanding the basic biology of this important organism, as well as for developing new strategies for combating bacterial infections and improving industrial processes involving bacteria.

In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.

The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.

In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.

Oxidative phosphorylation is the metabolic process by which cells use enzymes to generate energy in the form of adenosine triphosphate (ATP) from the oxidation of nutrients, such as glucose or fatty acids. This process occurs in the inner mitochondrial membrane of eukaryotic cells and is facilitated by the electron transport chain, which consists of a series of protein complexes that transfer electrons from donor molecules to acceptor molecules. As the electrons are passed along the chain, they release energy that is used to pump protons across the membrane, creating a gradient. The ATP synthase enzyme then uses the flow of protons back across the membrane to generate ATP, which serves as the main energy currency for cellular processes.

I'm sorry for any confusion, but "Pentanes" is not a medical term. It is a chemical term that refers to a group of five-carbon alkane hydrocarbons, including n-pentane and iso-pentane. These substances can be used in medical settings as anesthetics or for medical research, but "Pentanes" itself does not have a specific medical definition.

Cytochrome reductases are a group of enzymes that play a crucial role in the electron transport chain, a process that occurs in the mitochondria of cells and is responsible for generating energy in the form of ATP (adenosine triphosphate). Specifically, cytochrome reductases are responsible for transferring electrons from one component of the electron transport chain to another, specifically to cytochromes.

There are several types of cytochrome reductases, including NADH dehydrogenase (also known as Complex I), succinate dehydrogenase (also known as Complex II), and ubiquinone-cytochrome c reductase (also known as Complex III). These enzymes help to facilitate the flow of electrons through the electron transport chain, which is essential for the production of ATP and the maintenance of cellular homeostasis.

Defects in cytochrome reductases can lead to a variety of mitochondrial diseases, which can affect multiple organ systems and may be associated with symptoms such as muscle weakness, developmental delays, and cardiac dysfunction.

... may refer to: NADH dehydrogenase, an enzyme NADH:ubiquinone reductase (non-electrogenic), an enzyme This ...
... may refer to: NADH dehydrogenase, an enzyme NADH:ubiquinone reductase (non-electrogenic), an enzyme ...
... may refer to: NADH dehydrogenase NADH:ubiquinone reductase (non-electrogenic) This set index ...
... may stand for NADH dehydrogenase NADH:ubiquinone reductase (non-electrogenic) This set index ...
... may refer to: NADH dehydrogenase NADH:ubiquinone reductase (non-electrogenic) This set index ...
... may refer to: NADH dehydrogenase, an enzyme NADH:ubiquinone reductase (non-electrogenic), an enzyme ...
NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1 is a protein that in humans is encoded by the NDUFA1 gene. The ... NDUFA1 is a subunit of the enzyme NADH dehydrogenase (ubiquinone), the largest of the respiratory complexes. The structure is L ... "NDUFA1 - NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB ... "Entrez Gene: NDUFA1 NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, 1, 7.5kDa". Donald Voet; Judith G. Voet; Charlotte W. ...
... (EC 1.6.5.8 is an enzyme with systematic name NADH:ubiquinone oxidoreductase (Na+- ... NADH + H+ + ubiquinone + n Na+in → NAD+ + ubiquinol + n Na+out The enzyme is iron-sulfur flavoprotein. Fritz G, Steuber J (2016 ... NADH:ubiquinone+reductase+(Na+-transporting) at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: ... The common function of these transmembrane enzymes in respiration is to oxidize NADH using ubiquinone (Q) as electron acceptor ...
... (EC 1.6.5.9, NDH-2, ubiquinone reductase, coenzyme Q reductase, ... NADH:ubiquinone+reductase+(non-electrogenic) at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: ... Kerscher SJ, Okun JG, Brandt U (July 1999). "A single external enzyme confers alternative NADH:ubiquinone oxidoreductase ... ubiquinone ⇌ {\displaystyle \rightleftharpoons } NAD+ + ubiquinol This enzyme is a flavoprotein (FAD). It belongs to the family ...
In molecular biology, the NADH dehydrogenase (ubiquinone) 1 alpha subcomplex subunit 7 family of proteins (also known as NADH- ... ubiquinone oxidoreductase subunit B14.5a or Complex I-B14.5a) form a part of NADH dehydrogenase (complex I). In mammals, it is ... ubiquinone oxidoreductase: human complex I cDNA characterization completed". Biochem. Biophys. Res. Commun. 253 (2): 415-22. ...
In natural ubiquinones, there are from six to ten subunits in the tail. This family of fat-soluble substances, which resemble ... This was confirmed later that year and Q-275/substance SA was renamed ubiquinone as it was a ubiquitous quinone that could be ... Coenzyme Q is a coenzyme family that is ubiquitous in animals and most bacteria (hence its other name, ubiquinone). In humans, ... Much of the research on the skin benefits of ubiquinone show that it works synergistically with other topical antioxidants to ...
... it catalyzes the first step in the biosynthesis of ubiquinone in E. coli. Ubiquinone is a lipid-soluble electron-transporting ... "KEGG PATHWAY: Ubiquinone and other terpenoid-quinone biosynthesis - Reference pathway". www.genome.jp. Retrieved 2021-04-09. " ... Meganathan R (2001). "Ubiquinone biosynthesis in microorganisms". FEMS Microbiol. Lett. 203 (2): 131-9. doi:10.1111/j.1574- ... The enzyme chorismate lyase (EC 4.1.3.40) catalyzes the first step in ubiquinone biosynthesis, the removal of pyruvate from ...
"NADH-ubiquinone oxidoreductase chain 5". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB). "MT-ND5 - NADH-ubiquinone ... MT-ND5 is a gene of the mitochondrial genome coding for the NADH-ubiquinone oxidoreductase chain 5 protein (ND5). The ND5 ... MT-ND5 is one of seven mitochondrial genes encoding subunits of the enzyme NADH dehydrogenase (ubiquinone), together with MT- ... protein is a subunit of NADH dehydrogenase (ubiquinone), which is located in the mitochondrial inner membrane and is the ...
"MT-ND3 - NADH-ubiquinone oxidoreductase chain 3 - Homo sapiens (Human)". UniProt.org: a hub for protein information. The ... The ND3 protein is a subunit of NADH dehydrogenase (ubiquinone), which is located in the mitochondrial inner membrane and is ... MT-ND3 is one of seven mitochondrial genes encoding subunits of the enzyme NADH dehydrogenase (ubiquinone), together with MT- ... "NADH-ubiquinone oxidoreductase chain 3". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB). "Complete mitochondrial ...
"NADH-ubiquinone oxidoreductase chain 6". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB). "MT-ND6 - NADH-ubiquinone ... MT-ND6 is a gene of the mitochondrial genome coding for the NADH-ubiquinone oxidoreductase chain 6 protein (ND6). The ND6 ... MT-ND6 is one of seven mitochondrial genes encoding subunits of the enzyme NADH dehydrogenase (ubiquinone), together with MT- ... These genetic changes appear to prevent Complex I from interacting normally with ubiquinone, which may affect the generation of ...
"NADH-ubiquinone oxidoreductase chain 1". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB). "MT-ND1 - NADH-ubiquinone ... MT-ND1 is a gene of the mitochondrial genome coding for the NADH-ubiquinone oxidoreductase chain 1 (ND1) protein. The ND1 ... MT-ND1-encoded NADH-ubiquinone oxidoreductase chain 1 is a subunit of the respiratory chain Complex I that is supposed to ... MT-ND1 is one of seven mitochondrial genes encoding subunits of the enzyme NADH dehydrogenase (ubiquinone), together with MT- ...
Aguilaniu, H.; Durieux, J.; Dillin, A. (2005). "Metabolism, ubiquinone synthesis, and longevity". Genes & Development. 19 (20 ...
Aguilaniu, Hugo; Durieux, Jenni; Dillin, Andrew (October 15, 2005). "Metabolism, ubiquinone synthesis, and longevity". Genes ...
"NADH-ubiquinone oxidoreductase chain 4". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB). "MT-ND4 - NADH-ubiquinone ... MT-ND4 is a gene of the mitochondrial genome coding for the NADH-ubiquinone oxidoreductase chain 4 (ND4) protein. The ND4 ... MT-ND4 is one of seven mitochondrial genes encoding subunits of the enzyme NADH dehydrogenase (ubiquinone), together with MT- ... ubiquinone reductase in the ND1/3460 and the ND4/11778 mutations of the Leber hereditary optic neuroretinopathy (LHON)". FEBS ...
This enzyme participates in ubiquinone biosynthesis. Clarke CF, Williams W, Teruya JH (1991). "Ubiquinone biosynthesis in ...
"NADH-ubiquinone oxidoreductase chain 4L". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB). "MT-ND4L - NADH-ubiquinone ... MT-ND4L is a gene of the mitochondrial genome coding for the NADH-ubiquinone oxidoreductase chain 4L (ND4L) protein. The ND4L ... MT-ND4L is one of seven mitochondrial genes encoding subunits of the enzyme NADH dehydrogenase (ubiquinone), together with MT- ... protein is a subunit of NADH dehydrogenase (ubiquinone), which is located in the mitochondrial inner membrane and is the ...
Aguilaniu, H. (2005). "Metabolism, ubiquinone synthesis, and longevity". Genes & Development. 19 (20): 2399-406. doi:10.1101/ ...
Diaphorase activity of DLD may have an antioxidant role through its ability to scavenge nitric oxide and to reduce ubiquinone ... Olsson JM, Xia L, Eriksson LC, Björnstedt M (April 1999). "Ubiquinone is reduced by lipoamide dehydrogenase and this reaction ... Xia L, Björnstedt M, Nordman T, Eriksson LC, Olsson JM (March 2001). "Reduction of ubiquinone by lipoamide dehydrogenase. An ... and ubiquinone. DLD is thought to have a pro-oxidant role by reducing oxygen to a superoxide or ferric to ferrous iron, which ...
This enzyme participates in ubiquinone biosynthesis. The systematic name of this enzyme class is polyprenyl-diphosphate:4- ... an enzyme involved in ubiquinone biosynthesis, in the endoplasmic reticulum-Golgi system of rat liver". J. Biol. Chem. 265 (2 ...
This enzyme catalyses the first step in ubiquinone biosynthesis in Escherichia coli and other Gram-negative bacteria. Benzoate ... This enzyme participates in ubiquinone biosynthesis. The enzyme 4-hydroxybenzoate geranyltransferase utilizes geranyl ...
Dominant respiratory quinones are ubiquinone-8 and rhodoquinone-8. G+C fractions are 59.3 - 69.0 mol%. The genus Azovibrio also ... Dominant respiratory quinone is ubiquinone-8. G+C fractions are 63.5 - 67.0 mol%. Zoogloeaceae contains the genera Zoogloea ( ... Dominant respiratory quinones are menaquinone-8, ubiquinone-8 and rhodoquinone-8. G+C fractions are 61.6 - 65.3 mol%. ...
"Structure of electron transfer flavoprotein-ubiquinone oxidoreductase and electron transfer to the mitochondrial ubiquinone ... Ubiquinone binding is achieved through a deep hydrophobic binding pocket which is a different mode than other UQ-binding ... Then, the bound ubiquinone is reduced to ubiquinol, at least transiently forming the singly reduced semiubiquinone. The second ... The overall reaction catalyzed by ETF-QO is as follows: ETF-QO(red) + ubiquinone ↔ ETF-QO(ox) + ubiquinol Enzymatic activity is ...
... whereas its two products are S-adenosylhomocysteine and ubiquinone-9. This enzyme participates in ubiquinone biosynthesis. This ... Leppik RA, Stroobant P, Shineberg B, Young IG, Gibson F (March 1976). "Membrane-associated reactions in ubiquinone biosynthesis ... ubiquinone-9 Thus, the two substrates of this enzyme are S-adenosyl methionine and 3-demethylubiquinone-9, ...
The combined content of cytosine and guanine (GC-content) in DNA is 41 to 43 mol%. The main isoprenoid quinone is ubiquinone-10 ...
The major ubiquinone present is Q-10. The cell wall of S. salmonicolor contains fucose, mannose, glucose and galactose, however ...
Ubiquinone reductase may refer to: NADH dehydrogenase, an enzyme NADH:ubiquinone reductase (non-electrogenic), an enzyme This ...
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NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial. Names. NADH dehydrogenase (ubiquinone) Fe-S protein 4, ... NDUFS4 NADH:ubiquinone oxidoreductase subunit S4 [Homo sapiens] NDUFS4 NADH:ubiquinone oxidoreductase subunit S4 [Homo sapiens] ... ubiquinone oxidoreductase). Complex I removes electrons from NADH and passes them to the electron acceptor ubiquinone. ... NADH:ubiquinone oxidoreductase subunit S4provided by HGNC. Primary source. HGNC:HGNC:7711 See related. Ensembl:ENSG00000164258 ...
Learn about the uses and potential benefits of Ubiquinone including dosage guidelines, side effects, interactions and safety/ ... Ubiquinone is also known as Coenzyme Q10 or CoQ10. CoQ10. It may help prevent heart problems after heart surgery. It may also ...
NDUF_B12; NADH-ubiquinone oxidoreductase B12 subunit family. * NM_002491.3 → NP_002482.1 NADH dehydrogenase [ubiquinone] 1 beta ... NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3. Names. NADH dehydrogenase (ubiquinone) 1 beta subcomplex, 3, 12kDa ... NDUFB3 NADH:ubiquinone oxidoreductase subunit B3 [Homo sapiens] NDUFB3 NADH:ubiquinone oxidoreductase subunit B3 [Homo sapiens] ... NDUF_B12; NADH-ubiquinone oxidoreductase B12 subunit family. Alternate T2T-CHM13v2.0. Genomic * NC_060926.1 Alternate T2T- ...
Protein target information for NADH-ubiquinone oxidoreductase chain 4 (Wickerhamomyces canadensis). Find diseases associated ...
Save today on CoQ10 Bioactive Ubiquinone 100mg 60 softgels from Europharma / Terry Naturally, VitaNet carries a large selection ... Why Ubiquinone? Supplemental CoQ10 has long been recognized for its benefits for the heart, brain, gum health, and healthy ... Coenzyme Q10 (ubiquinone) 100 mg ** **Daily Value (DV) Not Established † Percent Daily Values (DV) are based on a 2,000 calorie ... aging.* Terry Naturally® CoQ10 is a premium-quality, classic ubiquinone-the same form shown to have remarkable results in ...
Changes in NADH-Ubiquinone Reductase (Complex I) with Autolysis in the Rat Heart as Experimental Model Enzyme (August,2017) ... Ubiquinone (Coenzyme Q 10 ) and Mitochondria in Oxidative Stress of Parkinsons Disease Biological Signals and Receptors (May, ... Enzymatic and Structural Modifications of Mitochondrial NADH-Ubiquinone Reductase with Autolysis as Experimental Model Subject ... H. van Jaarsveld, G. M. Potgieter, A. Lochner; Enzymatic and Structural Modifications of Mitochondrial NADH-Ubiquinone ...
... with d-Limonene offers 50 mg of ubiquinone to support heart & brain health, aided by the absorption support of d-limonene. ... What is ubiquinone CoQ10?. Ubiquinone CoQ10 is an essential nutrient for healthy mitochondrial function, a process that ... What Is CoQ10 (Ubiquinone) with d-Limonene?. CoQ10 helps the body convert fats and sugars into cellular energy, yet the normal ... The ubiquinone form of CoQ10 is difficult for the body to absorb.11 Super-Absorbable CoQ10â„¢ with d-Limonene provides the ...
Also known as coenzyme Q10, it is a natural compound present in all cells of the body. Helps energize skin cells and prevents photoaging, as well as reducing the depth of wrinkles.. ...
CoQ10s is also known as ubiquinone. CoQ10 supplementation appears to have the potential […] ...
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CoQ10 Ubiquinone is found naturally in the body. However, CoQ10 levels might decrease with age, so it has become a popular ... CoQ10 Ubiquinone is found naturally in the body. However, CoQ10 levels might decrease with age, so it has become a popular ... Ubiquinone also contributes to energy production. CoQ10 safeguards cells against oxidative damage. It is also essential for ... ":"CoQ10 Ubiquinone","public_title":null,"options":["Default Title"],"price":2699,"weight":113,"compare_at_price":3999," ...
These statements have not been evaluated by the Food and Drug Administration. This Product is not intended to diagnose, treat, cure or prevent any disease. ...
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Ubiquinone-9: MW 794. Ubiquinone-10: MW862. Ubiquinones are readily destroyed by heating in alkali , but in the presence of ... Ubiquinones are present in all aerobic organisms, plants, animals (the name ubiquinone was proposed with reference to their ... coenzyme Q10 is also named ubiquinone (50). Ubiquinone became the official name of the compound in 1975 (IUPAC-IUB commission ... UBIQUINONES These molecules are also known as coenzyme Q or mitoquinones. They are involved in electron transport in ...
The key difference between ubiquinone and plastoquinone is that ubiquinone is present in the inner membrane of mitochondria ... 6. Summary - Ubiquinone vs Plastoquinone. What is Ubiquinone?. Ubiquinone is a type of prenylquinone that acts as an electron ... 2. What is Ubiquinone. 3. What is Plastoquinone. 4. Similarities - Ubiquinone and Plastoquinone. 5. Ubiquinone vs Plastoquinone ... Another term for ubiquinone is coenzyme Q. Ubiquinone is a vital factor in the cellular respiration of plants. It also helps in ...
White Leaf Nutrition 27.95 CoQ10 Ubiquinone is found naturally in the body. However, CoQ10 levels might decrease with age, so ... CoQ10 Ubiquinone is found naturally in the body. However, CoQ10 levels might decrease with age, so it has become a popular ... CoQ10 Ubiquinone is found naturally in the body. However, CoQ10 levels might decrease with age, so it has become a popular ... Ubiquinone also contributes to energy production. CoQ10 safeguards cells against oxidative damage. It is also essential for ...
CoQ10, also known as ubiquinone, is a coenzyme found in every cell in the body and is essential for the production of energy. ... CoQ10 Ubiquinone is a natural supplement that provides a powerful dose of this essential nutrient. ... CoQ10 Ubiquinone is a natural supplement that provides a powerful dose of this essential nutrient. CoQ10, also known as ... MaxiZests CoQ10 Ubiquinone capsules are easy to take, making it a convenient addition to your daily routine. ...
Super-Absorbable CoQ10 with d-Limonene provides the ubiquinone form of CoQ10 in a super-emulsified formulation. d-Limonene is a ... Ubiquinone. 50 mg. Other ingredients: polysorbate 80, gelatin, ethyl oleate, glycerin, purified water, carob color, d-alpha ... Ubiquinone CoQ10 is a crucial nutrient involved in the process for the production of energy at the cellular level. Regular ... Product details "Super-Absorbable Ubiquinone CoQ10 with d-Limonene, 60 softgels" Coenzyme Q10 is an essential component for ...
The SCOP classification for the Electron transfer flavoprotein-ubiquinone oxidoreductase-like family. Additional information, ... Electron transfer flavoprotein-ubiquinone oxidoreductase-like family. SCOP classification Root: SCOP hierarchy in SUPERFAMILY [ ...
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ICQA uses a ubiquinone formula as its official science reference. *Ubiquinol cost more to manufacture than ubiquinone and is ... In terms of absorption, there is no difference between ubiquinone and ubiquinone ... Ubiquinone or Ubiquinol - does it really matter? Ever since the discovery of coenzyme Q10 in 1957, scientists have been ... Ubiquinone has been used in the majority of studies. *Thousands of clinical trials have been conducted with CoQ10. Only few are ...
Investigating Ubiquinone Biosynthesis in Freshwater Sponges. The captivating world of porifera, commonly referred to as sponges ... In the microbial world, rqua functions by modifying ubiquinone (UB) into a distinct form, RQ (rhodoquinone), with a lower redox ...
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  • Our Super-Absorbable CoQ10 (Ubiquinone) with d -Limonene supports heart and brain health with the added absorbable power of limonene. (lifeextension.com)
  • What Is CoQ10 (Ubiquinone) with d-Limonene? (lifeextension.com)
  • Our Super-Absorbable CoQ10 (Ubiquinone) with d -Limonene supports the absorption of CoQ10 with a higher dose and the added benefits of d -Limonene. (lifeextension.com)
  • Super-Absorbable CoQ10 (Ubiquinone) with d -Limonene provides the benefits of CoQ10 in a highly absorbable formulation. (lifeextension.com)
  • CoQ10 Ubiquinone is found naturally in the body. (biovittawellness.com)
  • CoQ10 Ubiquinone is a natural supplement that provides a powerful dose of this essential nutrient. (maxizest.com)
  • MaxiZest's CoQ10 Ubiquinone capsules are easy to take, making it a convenient addition to your daily routine. (maxizest.com)
  • Whether you're looking to support heart health, boost energy levels, or protect against the effects of aging, CoQ10 Ubiquinone is a great choice. (maxizest.com)
  • Consumers as well as scientists got confused and started questioning the traditional form of CoQ10 - ubiquinone - although it had been sold commercially and used in studies all along. (healthandscience.eu)
  • Introducing our top-of-the-line CoQ10 Ubiquinone Supplement, designed to improve your overall health and well-being. (anacotte.com)
  • Experience the difference for yourself - try our CoQ10 Ubiquinone Supplement today! (anacotte.com)
  • Therefore, these are the ones that should take CoQ10 Ubiquinone capsules regularly. (hardrockhealth.com)
  • As a dietary supplement, take one capsule of CoQ10 Ubiquinone by Hard Rock Health per day. (hardrockhealth.com)
  • Revitalize your body and revive your health with CoQ10 Ubiquinone, an essential nutrient for cellular energy and overall vitality. (hardrockhealth.com)
  • Elevate your cellular health with CoQ10 Ubiquinone, an extra strength formula that supports energy production and protects against oxidative stress. (hardrockhealth.com)
  • Unlock the power of CoQ10 Ubiquinone, promoting healthy aging, optimal energy levels, and supporting a strong immune system. (hardrockhealth.com)
  • Experience the power of CoQ10 Ubiquinone and enjoy the benefits of optimal heart health, increased energy, and overall wellness. (hardrockhealth.com)
  • Supercharge your heart's performance with CoQ10 Ubiquinone, providing extra strength support for cardiovascular health and optimal function. (hardrockhealth.com)
  • Ubiquinone reductase may refer to: NADH dehydrogenase, an enzyme NADH:ubiquinone reductase (non-electrogenic), an enzyme This set index page lists enzyme articles associated with the same name. (wikipedia.org)
  • This gene encodes an nuclear-encoded accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (complex I, or NADH:ubiquinone oxidoreductase). (nih.gov)
  • Complex I removes electrons from NADH and passes them to the electron acceptor ubiquinone. (nih.gov)
  • Identification and primary structure of five human NADH-ubiquinone oxidoreductase subunits. (nih.gov)
  • cDNA of eight nuclear encoded subunits of NADH:ubiquinone oxidoreductase: human complex I cDNA characterization completed. (nih.gov)
  • Only those particles which contain 'turnover-preconditioned" NADH-ubiquinone reductase demonstrate the ubisemiquinone signal together with N-1, N-2, N-3 and N-4 iron-sulfur centers. (tau.ac.il)
  • The structures of two novel fungal antibiotics, isolated from a Pterula species, that interfere with the NADH: ubiquinone oxidoreductase and inhibit the respiration of eucaryotes, were determined by spectroscopic techniques. (go.jp)
  • The diverse inhibitors of bovine heart mitochondrial complex I (NADH-ubiquinone oxidoreductase) are believed to share a common large binding domain with partially overlapping sites, though it remains unclear how these binding sites relate to each other. (elsevierpure.com)
  • The complexes studied are Complex I (NADH:Ubiquinone oxidoreductase), Complex II (Succinate:ubiquinone oxidoreductase), Complex III (Ubiquinol:cytochrome c oxidoreductase), and Complex IV (Cytochrome c oxidase). (cdc.gov)
  • Ubiquinol and ubiquinone are two related but chemically different forms of Coenzyme Q10, both of which play important roles within the body. (mymed.com)
  • Ubiquinone and plastoquinone are two important prenylquinones that function as electron transporters in the electron transport chain of oxygenic photosynthesis and aerobic respiration , respectively. (differencebetween.com)
  • Ubiquinone is a type of prenylquinone that acts as an electron carrier in the process of oxidative phosphorylation that takes place in the mitochondria. (differencebetween.com)
  • Moreover, ubiquinone acts as an electron carrier in the electron transport chain of oxidative phosphorylation, while plastoquinone acts as an electron carrier in the electron transport chain of light dependant reactions of photosynthesis. (differencebetween.com)
  • Subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). SDH1 and SDH2 form the catalytic dimer. (ymdb.ca)
  • Coenzyme Q10, also referred to as CoQ10, ubiquinol, ubiquinone or ubidecarenone is fat-soluble vitamin-like nutrient . (mymed.com)
  • Coenzyme Q10 (ubiquinone) is an essential component of the mitochondrial respiratory chain, as well as being a powerful cellular antioxidant. (leedsth.nhs.uk)
  • Coenzyme Q10 (ubiquinone) is an enzyme that is naturally produced in the body. (msdmanuals.com)
  • Complex I (nicotinamide adenine dinucleotide-ubiquinone reductase) is a complex enzyme system located in the inner mitochondrial membrane. (karger.com)
  • So when you take ubiquinol it shifts to ubiquinone and vice versa. (healthandscience.eu)
  • If there are insufficient levels of ubiquinol in the body, it will reduce ubiquinone to form ubiquinol, and vice versa. (mymed.com)
  • Mitchell, P. Protonmotive redox mechanism of the cytochrome b - c 1 complex in the respiratory chain: protonmotive ubiquinone cycle. (nature.com)
  • The sole respiratory quinones were identified as ubiquinone-10. (bvsalud.org)
  • The structure of ubiquinone consists of a ring of ubiquinone (through the metabolism of the amino acid phenylalanine) along with a long chain of carbon called polyprenyl. (differencebetween.com)
  • Terry Naturally® CoQ10 is a premium-quality, classic ubiquinone-the same form shown to have remarkable results in clinical studies. (vitanetonline.com)
  • However, the ubiquinone form of CoQ10 is difficult for the body to absorb. (lifeextension.com)
  • Ironically, CoQ10 shifts between its ubiquinone and ubiquinol form in a continuous cycle inside the body. (healthandscience.eu)
  • In the microbial world, rqua functions by modifying ubiquinone (UB) into a distinct form, RQ (rhodoquinone), with a lower redox potential, thereby facilitating anaerobic respiration. (lu.se)
  • Coenzyme Q10 can be obtained in the form of ubiquinone through dietary means, although this is limited. (mymed.com)
  • ATP is a complex organic chemical that gives cells the energy they need to function and coenzyme Q10 in the form of ubiquinone is vital to this process. (mymed.com)
  • Ubiquinone CoQ10 is an essential nutrient for healthy mitochondrial function, a process that produces energy at the cellular level. (lifeextension.com)
  • Ubiquinone CoQ10 is a crucial nutrient involved in the process for the production of energy at the cellular level. (lifeextensioneurope.com)
  • Ubiquinone became the 'official' name of the compound in 1975 (IUPAC-IUB commission). (gerli.com)
  • CoQ10, also known as ubiquinone, is a coenzyme found in every cell in the body and is essential for the production of energy. (maxizest.com)
  • Ubiquinones are present in all aerobic organisms, plants, animals (the name ubiquinone was proposed with reference to their ubiquitous occurrence) and bacteria, but are absent from Gram-positive eubacteria and the archaebacteria. (gerli.com)
  • abstract = "An ubiquinone derivative, pseudoalteromone A (1), has been isolated from two marine-derived Pseudoalteromonas spp. (ewha.ac.kr)
  • The lesion that resulted from ischaemia was localised as altered enzymatic activities due to a different polypeptide composition, as well as loss of ubiquinone and non-haem iron from complex IB. (karger.com)
  • Another term for ubiquinone is coenzyme Q. Ubiquinone is a vital factor in the cellular respiration of plants. (differencebetween.com)
  • Researchers believe that by using ubiquinone, artificially engineered and bred plants can be made with more stress-resistant properties and have increased nutritional value properties. (differencebetween.com)
  • Ubiquinone is a vital factor for the cellular respiration of plants. (differencebetween.com)
  • Recent review: 'Biochemical, physiological and medical aspects of ubiquinone function' by Ernster L et al. (gerli.com)
  • Clever marketing campaigns attempted to pawn this off as the new and improved CoQ10 source that was absorbed more easily in the body and was superior to ubiquinone. (healthandscience.eu)
  • Another study (KiSel-10) which was published a nearly two years ago and showed a 54% lower mortality rate among elderly people who took supplements of CoQ10 (and selenium) was also conducted with ubiquinone. (healthandscience.eu)
  • The key difference between ubiquinone and plastoquinone is that ubiquinone is present in the inner membrane of mitochondria while plastoquinone is present in the thylakoids of chloroplast . (differencebetween.com)
  • Thus, this is the key difference between ubiquinone and plastoquinone. (differencebetween.com)
  • So, this summarizes the difference between ubiquinone and plastoquinone. (differencebetween.com)
  • Ubiquinol vs ubiquinone - what's the difference? (mymed.com)
  • Enzymatic activities, polypeptide composition, as well as other components such as non-haem iron, acid-labile sulphur and ubiquinone, were determined. (karger.com)
  • A composition comprises as the active agent a Non-glucocorticoid steroid, analogue thereof, a ubiquinone, or their salts, in an amount effective for reducing levels of, or hypersensitivity to, adenosine, increasing levels of lung surfactant or ubiquinone, or for preventing or treating respiratory, lung and cancer diseases. (ecu.edu)
  • CoQ10 or Coenzyme Q10 Extra Strength Ubiquinone has been shown to improve heart health and blood sugar regulation, assist in the prevention and treatment of cancer and reduce the frequency of migraines. (hardrockhealth.com)
  • Ubiquinone is present in the inner membrane of the mitochondria of the plant cell. (differencebetween.com)
  • Any process that activates or increases the frequency, rate or extent of ubiquinone biosynthetic process. (planteome.org)
  • Link to all annotated objects annotated to positive regulation of ubiquinone biosynthetic process. (planteome.org)
  • Link to all direct and indirect annotations to positive regulation of ubiquinone biosynthetic process. (planteome.org)