A complex of enzymes and PROTON PUMPS located on the inner membrane of the MITOCHONDRIA and in bacterial membranes. The protein complex provides energy in the form of an electrochemical gradient, which may be used by either MITOCHONDRIAL PROTON-TRANSLOCATING ATPASES or BACTERIAL PROTON-TRANSLOCATING ATPASES.
The 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 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.
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)
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.
Molecules or ions formed by the incomplete one-electron reduction of oxygen. These reactive oxygen intermediates include SINGLET OXYGEN; SUPEROXIDES; PEROXIDES; HYDROXYL RADICAL; and HYPOCHLOROUS ACID. They contribute to the microbicidal activity of PHAGOCYTES, regulation of signal transduction and gene expression, and the oxidative damage to NUCLEIC ACIDS; PROTEINS; and LIPIDS.
A disturbance in the prooxidant-antioxidant balance in favor of the former, leading to potential damage. Indicators of oxidative stress include damaged DNA bases, protein oxidation products, and lipid peroxidation products (Sies, Oxidative Stress, 1991, pxv-xvi).
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.
A multisubunit enzyme complex containing CYTOCHROME A GROUP; CYTOCHROME A3; two copper atoms; and 13 different protein subunits. It is the terminal oxidase complex of the RESPIRATORY CHAIN and collects electrons that are transferred from the reduced CYTOCHROME C GROUP and donates them to molecular OXYGEN, which is then reduced to water. The redox reaction is simultaneously coupled to the transport of PROTONS across the inner mitochondrial membrane.
An antibiotic substance produced by Streptomyces species. It inhibits mitochondrial respiration and may deplete cellular levels of ATP. Antimycin A1 has been used as a fungicide, insecticide, and miticide. (From Merck Index, 12th ed)
A botanical insecticide that is an inhibitor of mitochondrial electron transport.
Electron transfer through the cytochrome system liberating free energy which is transformed into high-energy phosphate bonds.
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 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 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.
The metabolic process of all living cells (animal and plant) in which oxygen is used to provide a source of energy for the cell.
The synthesis by organisms of organic chemical compounds, especially carbohydrates, from carbon dioxide using energy obtained from light rather than from the oxidation of chemical compounds. Photosynthesis comprises two separate processes: the light reactions and the dark reactions. In higher plants; GREEN ALGAE; and CYANOBACTERIA; NADPH and ATP formed by the light reactions drive the dark reactions which result in the fixation of carbon dioxide. (from Oxford Dictionary of Biochemistry and Molecular Biology, 2001)
Stable elementary particles having the smallest known negative charge, present in all elements; also called negatrons. Positively charged electrons are called positrons. The numbers, energies and arrangement of electrons around atomic nuclei determine the chemical identities of elements. Beams of electrons are called CATHODE RAYS.
A flavoprotein containing oxidoreductase that catalyzes the dehydrogenation of SUCCINATE to fumarate. In most eukaryotic organisms this enzyme is a component of mitochondrial electron transport complex II.
The 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)
Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen.
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 movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.
The mitochondria of the myocardium.
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.
Diseases caused by abnormal function of the MITOCHONDRIA. They may be caused by mutations, acquired or inherited, in mitochondrial DNA or in nuclear genes that code for mitochondrial components. They may also be the result of acquired mitochondria dysfunction due to adverse effects of drugs, infections, or other environmental causes.
Proteins encoded by the mitochondrial genome or proteins encoded by the nuclear genome that are imported to and resident in the MITOCHONDRIA.
The 8-hydroxy derivatives inhibit various enzymes and their halogenated derivatives, though neurotoxic, are used as topical anti-infective agents, among other uses.
The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)
A 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)
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.
Proteins that form the structure of the NUCLEAR PORE. They are involved in active, facilitated and passive transport of molecules in and out of the CELL NUCLEUS.
Mitochondria of skeletal and smooth muscle. It does not include myocardial mitochondria for which MITOCHONDRIA, HEART is available.
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.
Double-stranded DNA of MITOCHONDRIA. In eukaryotes, the mitochondrial GENOME is circular and codes for ribosomal RNAs, transfer RNAs, and about 10 proteins.
The movement of materials across cell membranes and epithelial layers against an electrochemical gradient, requiring the expenditure of metabolic energy.
The voltage difference, normally maintained at approximately -180mV, across the INNER MITOCHONDRIAL MEMBRANE, by a net movement of positive charge across the membrane. It is a major component of the PROTON MOTIVE FORCE in MITOCHONDRIA used to drive the synthesis of ATP.
An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.
A pre-emergent herbicide.
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.
The rate dynamics in chemical or physical systems.

Gene structure and quinol oxidase activity of a cytochrome bd-type oxidase from Bacillus stearothermophilus. (1/368)

Gram-positive thermophilic Bacillus species contain cytochrome caa3-type cytochrome c oxidase as their main terminal oxidase in the respiratory chain. We previously identified and purified an alternative oxidase, cytochrome bd-type quinol oxidase, from a mutant of Bacillus stearothermophilus defective in the caa3-type oxidase activity (J. Sakamoto et al., FEMS Microbiol. Lett. 143 (1996) 151-158). Compared with proteobacterial counterparts, B. stearothermophilus cytochrome bd showed lower molecular weights of the two subunits, shorter wavelength of alpha-band absorption maximum due to heme D, and lower quinol oxidase activity. Preincubation with menaquinone-2 enhanced the enzyme activity up to 40 times, suggesting that, besides the catalytic site, there is another quinone-binding site which largely affects the enzyme activity. In order to clarify the molecular basis of the differences of cytochromes bd between B. stearothermophilus and proteobacteria, the genes encoding for the B. stearothermophilus bd was cloned based on its partial peptide sequences. The gene for subunit I (cbdA) encodes 448 amino acid residues with a molecular weight of 50195 Da, which is 14 and 17% shorter than those of Escherichia coli and Azotobacter vinelandii, respectively, and CbdA lacks the C-terminal half of the long hydrophilic loop between the putative transmembrane segments V and VI (Q loop), which has been suggested to include the substrate quinone-binding site for the E. coli enzyme. The gene for subunit II (cbdB) encodes 342 residues with a molecular weight of 38992 Da. Homology search indicated that the B. stearothermophilus cbdAB has the highest sequence similarity to ythAB in B. subtilis genome rather than to cydAB, the first set of cytochrome bd genes identified in the genome. Sequence comparison of cytochromes bd and their homologs from various organisms demonstrates that the proteins can be classified into two subfamilies, a proteobacterial type including E. coli bd and a more widely distributed type including the B. stearothermophilus enzyme, suggesting that the latter type is evolutionarily older.  (+info)

Fourier-transform infrared studies on conformation changes in bd-type ubiquinol oxidase from Escherichia coli upon photoreduction of the redox metal centers. (2/368)

Cytochrome bd is a two-subunit ubiquinol oxidase in the aerobic respiratory chain of Escherichia coli that does not belong to the heme-copper terminal oxidase superfamily. To explore unique protein structural changes associated with the reduction of the redox metal centers, we carried out Fourier-transform infrared and visible spectroscopic studies on cytochrome bd. For infrared measurements of a partially dehydrated thin sample solution, the air-oxidized enzyme was fully reduced by the intermolecular electron transfer of photo-excited riboflavin in the absence and presence of KCN, and redox difference spectra were calculated. Upon reduction, the bound cyanide was released from the heme b595-heme d binuclear center but remained in a protein pocket as a deprotonated form. Reduction of heme b558, heme b595, and heme d resulted in large changes in amide-I and protonated carboxylic CO-stretching vibrations and also a small change in the cysteine SH-stretching vibration. The location of the redox metal centers and the effects of cyanide suggest that these protein structural changes occur at the heme-binding pockets near the protein surface. Systematic site-directed mutagenesis and time-resolved FTIR studies on cytochrome bd will facilitate an understanding of the unique molecular mechanisms for dioxygen reduction and delivery of chemical protons to the active center at the atomic level.  (+info)

Fluoride-binding to the Escherichia coli bd-type ubiquinol oxidase studied by visible absorption and EPR spectroscopies. (3/368)

Cytochrome bd-type ubiquinol oxidase in the aerobic respiratory chain of Escherichia coli contains two hemes b (b558 and b595) and one heme d as redox metal centers. To clarify the structure of the reaction center, we analyzed the fully oxidized enzyme by visible and EPR spectroscopies using fluoride ion as a monitoring probe. The visible spectral changes upon fluoride-binding were typical of ferric iron-chlorine species, indicating heme d as a primary binding site. The negative peak at 645 nm in the difference spectrum indicates that heme b595 also provides the low-affinity fluoride-binding site. Fluoride-binding caused a complete disappearance from the EPR spectra of the low-spin signals ascribable to heme d and spectral changes in both rhombic and axial high-spin signals. After fluoride-binding, each component of the rhombic high-spin signal showed superhyperfine splitting arising from the interaction of the unpaired spin of the heme d iron with the nuclear magnetic moment of 19F. The axial high-spin species was converted to a new rhombic high-spin species assignable to heme b595-fluoride. The g = 2 component of this new species also gave 19F-superhyperfine splitting. These results indicate that both heme d and heme b595 can coordinate with a fluoride ion with different affinities in the fully oxidized state.  (+info)

Oxidative protein folding is driven by the electron transport system. (4/368)

Disulfide bond formation is catalyzed in vivo by DsbA and DsbB. Here we reconstitute this oxidative folding system using purified components. We have found the sources of oxidative power for protein folding and show how disulfide bond formation is linked to cellular metabolism. We find that disulfide bond formation and the electron transport chain are directly coupled. DsbB uses quinones as electron acceptors, allowing various choices for electron transport to support disulfide bond formation. Electrons flow via cytochrome bo oxidase to oxygen under aerobic conditions or via cytochrome bd oxidase under partially anaerobic conditions. Under truly anaerobic conditions, menaquinone shuttles electrons to alternate final electron acceptors such as fumarate. This flexibility reflects the vital nature of the disulfide catalytic system.  (+info)

Azide- and cyanide-binding to the Escherichia coli bd-type ubiquinol oxidase studied by visible absorption, EPR and FTIR spectroscopies. (5/368)

Cytochrome bd-type ubiquinol oxidase contains two hemes b (b(558) and b(595)) and one heme d as the redox metal centers. To clarify the structure of the reaction center, we analyzed Escherichia coli cytochrome bd by visible absorption, EPR and FTIR spectroscopies using azide and cyanide as monitoring probes for the exogenous ligand binding site. Azide-binding caused the appearance of a new EPR low-spin signal characteristic of ferric iron-chlorin-azide species and a new visible absorption band at 647 nm. However, the bound azide ((14)N(3)) anti-symmetric stretching infrared band (2, 010.5 cm(-1)) showed anomalies upon (15)N-substitutions, indicating interactions with surrounding protein residues or heme b(595) in close proximity. The spectral changes upon cyanide-binding in the visible region were typical of those observed for ferric iron-chlorin species with diol substituents in macrocycles. However, we found no indication of a low-spin EPR signal corresponding to the ferric iron-chlorin-cyanide complexes. Instead, derivative-shaped signals at g = 3.19 and g = 7.15, which could arise from the heme d(Fe(3+))-CN-heme b(595)(Fe(3+)) moiety, were observed. Further, after the addition of cyanide, a part of ferric heme d showed the rhombic high-spin signal that coexisted with the g(z) = 2.85 signal ascribed to the minor heme b(595)-CN species. This indicates strong steric hindrance of cyanide-binding to ferric heme d with the bound cyanide at ferric heme b(595).  (+info)

A cytochrome bb'-type quinol oxidase in Bacillus subtilis strain 168. (6/368)

The aerobic respiratory system of Bacillus subtilis 168 is known to contain three terminal oxidases: cytochrome caa(3), which is a cytochrome c oxidase, and cytochrome aa(3) and bd, which are quinol oxidases. The presence of a possible fourth oxidase in the bacterium was investigated using a constructed mutant, LUH27, that lacks the aa(3) and caa(3) terminal oxidases and is also deficient in succinate:menaquinone oxidoreductase. The cytochrome bd content of LUH27 can be varied by using different growth conditions. LUH27 membranes virtually devoid of cytochrome bd respired with NADH or exogenous quinol as actively as preparations containing 0.4 nmol of cytochrome bd/mg of protein but were more sensitive to cyanide and aurachin D. The reduced minus oxidized difference spectra of the bd-deficient membranes as well as absorption changes induced by CO and cyanide indicated the presence of a "cytochrome o"-like component; however, the membranes did not contain heme O. The results provide strong evidence for the presence of a terminal oxidase of the bb' type in B. subtilis. The enzyme does not pump protons and combines with CO much faster than typical heme-copper oxidases; in these respects, it resembles a cytochrome bd rather than members of the heme-copper oxidase superfamily. The genome sequence of B. subtilis 168 contains gene clusters for four respiratory oxidases. Two of these clusters, cta and qox, are deleted in LUH27. The remaining two, cydAB and ythAB, encode the identified cytochrome bd and a putative second cytochrome bd, respectively. Deletion of ythAB in strain LUH27 or the presence of the yth genes on plasmid did not affect the expression of the bb' oxidase. It is concluded that the novel bb'-type oxidase probably is cytochrome bd encoded by the cyd locus but with heme D being substituted by high spin heme B at the oxygen reactive site, i.e. cytochrome b(558)b(595)b'.  (+info)

Femtosecond resolution of ligand-heme interactions in the high-affinity quinol oxidase bd: A di-heme active site? (7/368)

Interaction of the two high-spin hemes in the oxygen reduction site of the bd-type quinol oxidase from Escherichia coli has been studied by femtosecond multicolor transient absorption spectroscopy. The previously unidentified Soret band of ferrous heme b(595) was determined to be centered around 440 nm by selective excitation of the fully reduced unliganded or CO-bound cytochrome bd in the alpha-band of heme b(595). The redox state of the b-type hemes strongly affects both the line shape and the kinetics of the absorption changes induced by photodissociation of CO from heme d. In the reduced enzyme, CO photodissociation from heme d perturbs the spectrum of ferrous cytochrome b(595) within a few ps, pointing to a direct interaction between hemes b(595) and d. Whereas in the reduced enzyme no heme d-CO geminate recombination is observed, in the mixed-valence CO-liganded complex with heme b(595) initially oxidized, a significant part of photodissociated CO does not leave the protein and recombines with heme d within a few hundred ps. This caging effect may indicate that ferrous heme b(595) provides a transient binding site for carbon monoxide within one of the routes by which the dissociated ligand leaves the protein. Taken together, the data indicate physical proximity of the hemes d and b(595) and corroborate the possibility of a functional cooperation between the two hemes in the dioxygen-reducing center of cytochrome bd.  (+info)

Regulation of cytochrome bd expression in the obligate aerobe Azotobacter vinelandii by CydR (Fnr). Sensitivity to oxygen, reactive oxygen species, and nitric oxide. (8/368)

Azotobacter vinelandii is an obligately aerobic bacterium in which aerotolerant nitrogen fixation requires cytochrome bd. Regulation of cytochrome bd expression is achieved by CydR (an Fnr homologue), which represses transcription of the oxidase genes cydAB. cydAB mRNA was mapped by primer extension; the transcriptional start site was determined, and putative -10 and -35 regions were deduced. Two "CydR boxes," one at the +1 site and one upstream of the -35 region, were identified. Transcriptionally inactive, purified CydR was converted, by adding NifS, cysteine, and Fe(2+), into an active form possessing acid-labile sulfide and spectra suggesting a [4Fe-4S](2+) cluster. Reconstituted CydR specifically bound both CydR boxes cooperatively, with higher affinity for the nearer consensus +1 site. Low concentrations of O(2) or NO ([O(2)]/[[CydR] or [NO]/[CydR] = 0.1-0. 6) elicited loss of the 420 nm absorbance attributed to the [4Fe-4S](2+) cluster, formation of a 315 nm species, and loss of ability to retard DNA migration. Retardation by reconstituted CydR was enhanced by superoxide dismutase and/or catalase, suggesting a role for reactive oxygen species in CydR inactivation. The role of CydR in regulating cydAB expression in the supposedly anoxic cytoplasm of A. vinelandii and similarities to cydAB regulation by Fnr in Escherichia coli are discussed.  (+info)

The Electron Transport Chain (ETC) is a series of complexes in the inner mitochondrial membrane that are involved in the process of cellular respiration, through which the majority of energy is generated for the cell. The ETC complex proteins are a group of transmembrane protein complexes that facilitate the transfer of electrons from electron donors to electron acceptors via redox reactions. This transfer of electrons drives the generation of a proton gradient across the inner mitochondrial membrane, which is then used by ATP synthase to generate ATP, the primary energy currency of the cell.

The ETC complex proteins consist of four main complexes: Complex I (NADH-Q oxidoreductase), Complex II (succinate-Q oxidoreductase), Complex III (cytochrome bc1 complex or CoQ:cytochrome c oxidoreductase), and Complex IV (cytochrome c oxidase). Each complex contains a number of subunits, many of which are encoded by both the nuclear and mitochondrial genomes.

In summary, Electron Transport Chain Complex Proteins are a group of transmembrane protein complexes located in the inner mitochondrial membrane that facilitate the transfer of electrons from electron donors to electron acceptors, driving the generation of a proton gradient and ultimately ATP synthesis during cellular respiration.

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.

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.

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.

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.

Reactive Oxygen Species (ROS) are highly reactive molecules containing oxygen, including peroxides, superoxide, hydroxyl radical, and singlet oxygen. They are naturally produced as byproducts of normal cellular metabolism in the mitochondria, and can also be generated by external sources such as ionizing radiation, tobacco smoke, and air pollutants. At low or moderate concentrations, ROS play important roles in cell signaling and homeostasis, but at high concentrations, they can cause significant damage to cell structures, including lipids, proteins, and DNA, leading to oxidative stress and potential cell death.

Oxidative stress is defined as an imbalance between the production of reactive oxygen species (free radicals) and the body's ability to detoxify them or repair the damage they cause. This imbalance can lead to cellular damage, oxidation of proteins, lipids, and DNA, disruption of cellular functions, and activation of inflammatory responses. Prolonged or excessive oxidative stress has been linked to various health conditions, including cancer, cardiovascular diseases, neurodegenerative disorders, and aging-related diseases.

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.

Electron Transport Complex IV is also known as Cytochrome c oxidase. It is the last complex in the electron transport chain, located in the inner mitochondrial membrane of eukaryotic cells and the plasma membrane of prokaryotic cells. This complex contains 13 subunits, two heme groups (a and a3), and three copper centers (A, B, and C).

In the electron transport chain, Complex IV receives electrons from cytochrome c and transfers them to molecular oxygen, reducing it to water. This process is accompanied by the pumping of protons across the membrane, contributing to the generation of a proton gradient that drives ATP synthesis via ATP synthase (Complex V). The overall reaction catalyzed by Complex IV can be summarized as follows:

4e- + 4H+ + O2 → 2H2O

Defects in Cytochrome c oxidase can lead to various diseases, including mitochondrial encephalomyopathies and neurodegenerative disorders.

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.

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.

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.

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.

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.

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.

Cell respiration is the process by which cells convert biochemical energy from nutrients into adenosine triphosphate (ATP), and then release waste products. The three main stages of cell respiration are glycolysis, the citric acid cycle (also known as the Krebs cycle), and the electron transport chain.

During glycolysis, which takes place in the cytoplasm, glucose is broken down into two molecules of pyruvate, producing a small amount of ATP and reducing power in the form of NADH.

The citric acid cycle occurs in the mitochondria and involves the breakdown of acetyl-CoA (formed from pyruvate) to produce more ATP, NADH, and FADH2.

Finally, the electron transport chain, also located in the mitochondria, uses the energy from NADH and FADH2 to pump protons across the inner mitochondrial membrane, creating a proton gradient. The flow of protons back across the membrane drives the synthesis of ATP, which is used as a source of energy by the cell.

Cell respiration is a crucial process that allows cells to generate the energy they need to perform various functions and maintain homeostasis.

Photosynthesis is not strictly a medical term, but it is a fundamental biological process with significant implications for medicine, particularly in understanding energy production in cells and the role of oxygen in sustaining life. Here's a general biological definition:

Photosynthesis is a process by which plants, algae, and some bacteria convert light energy, usually from the sun, into chemical energy in the form of organic compounds, such as glucose (or sugar), using water and carbon dioxide. This process primarily takes place in the chloroplasts of plant cells, specifically in structures called thylakoids. The overall reaction can be summarized as:

6 CO2 + 6 H2O + light energy → C6H12O6 + 6 O2

In this equation, carbon dioxide (CO2) and water (H2O) are the reactants, while glucose (C6H12O6) and oxygen (O2) are the products. Photosynthesis has two main stages: the light-dependent reactions and the light-independent reactions (Calvin cycle). The light-dependent reactions occur in the thylakoid membrane and involve the conversion of light energy into ATP and NADPH, which are used to power the Calvin cycle. The Calvin cycle takes place in the stroma of chloroplasts and involves the synthesis of glucose from CO2 and water using the ATP and NADPH generated during the light-dependent reactions.

Understanding photosynthesis is crucial for understanding various biological processes, including cellular respiration, plant metabolism, and the global carbon cycle. Additionally, research into artificial photosynthesis has potential applications in renewable energy production and environmental remediation.

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.

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.

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.

Electron microscopy (EM) is a type of microscopy that uses a beam of electrons to create an image of the sample being examined, resulting in much higher magnification and resolution than light microscopy. There are several types of electron microscopy, including transmission electron microscopy (TEM), scanning electron microscopy (SEM), and reflection electron microscopy (REM).

In TEM, a beam of electrons is transmitted through a thin slice of the sample, and the electrons that pass through the sample are focused to form an image. This technique can provide detailed information about the internal structure of cells, viruses, and other biological specimens, as well as the composition and structure of materials at the atomic level.

In SEM, a beam of electrons is scanned across the surface of the sample, and the electrons that are scattered back from the surface are detected to create an image. This technique can provide information about the topography and composition of surfaces, as well as the structure of materials at the microscopic level.

REM is a variation of SEM in which the beam of electrons is reflected off the surface of the sample, rather than scattered back from it. This technique can provide information about the surface chemistry and composition of materials.

Electron microscopy has a wide range of applications in biology, medicine, and materials science, including the study of cellular structure and function, disease diagnosis, and the development of new materials and technologies.

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.

Biological transport refers to the movement of molecules, ions, or solutes across biological membranes or through cells in living organisms. This process is essential for maintaining homeostasis, regulating cellular functions, and enabling communication between cells. There are two main types of biological transport: passive transport and active transport.

Passive transport does not require the input of energy and includes:

1. Diffusion: The random movement of molecules from an area of high concentration to an area of low concentration until equilibrium is reached.
2. Osmosis: The diffusion of solvent molecules (usually water) across a semi-permeable membrane from an area of lower solute concentration to an area of higher solute concentration.
3. Facilitated diffusion: The assisted passage of polar or charged substances through protein channels or carriers in the cell membrane, which increases the rate of diffusion without consuming energy.

Active transport requires the input of energy (in the form of ATP) and includes:

1. Primary active transport: The direct use of ATP to move molecules against their concentration gradient, often driven by specific transport proteins called pumps.
2. Secondary active transport: The coupling of the movement of one substance down its electrochemical gradient with the uphill transport of another substance, mediated by a shared transport protein. This process is also known as co-transport or counter-transport.

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).

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.

Mitochondrial diseases are a group of disorders caused by dysfunctions in the mitochondria, which are the energy-producing structures in cells. These diseases can affect people of any age and can manifest in various ways, depending on which organs or systems are affected. Common symptoms include muscle weakness, neurological problems, cardiac disease, diabetes, and vision/hearing loss. Mitochondrial diseases can be inherited from either the mother's or father's side, or they can occur spontaneously due to genetic mutations. They can range from mild to severe and can even be life-threatening in some cases.

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.

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.

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.

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.

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.

Nuclear pore complex proteins, also known as nucleoporins, are a group of specialized proteins that make up the nuclear pore complex (NPC), a large protein structure found in the nuclear envelope of eukaryotic cells. The NPC regulates the transport of molecules between the nucleus and the cytoplasm.

Nucleoporins are organized into distinct subcomplexes, which together form the NPC. They contain phenylalanine-glycine (FG) repeats, which are stretches of amino acids rich in phenylalanine and glycine residues. These FG repeats interact with transport factors, which are responsible for carrying molecules through the NPC.

Nucleoporins play a critical role in the regulation of nuclear transport, and mutations in these proteins have been linked to various human diseases, including neurological disorders and cancer.

Mitochondria in muscle, also known as the "powerhouses" of the cell, are organelles that play a crucial role in generating energy for muscle cells through a process called cellular respiration. They convert the chemical energy found in glucose and oxygen into ATP (adenosine triphosphate), which is the main source of energy used by cells.

Muscle cells contain a high number of mitochondria due to their high energy demands for muscle contraction and relaxation. The number and size of mitochondria in muscle fibers can vary depending on the type of muscle fiber, with slow-twitch, aerobic fibers having more numerous and larger mitochondria than fast-twitch, anaerobic fibers.

Mitochondrial dysfunction has been linked to various muscle disorders, including mitochondrial myopathies, which are characterized by muscle weakness, exercise intolerance, and other symptoms related to impaired energy production in the muscle cells.

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.

Mitochondrial DNA (mtDNA) is the genetic material present in the mitochondria, which are specialized structures within cells that generate energy. Unlike nuclear DNA, which is present in the cell nucleus and inherited from both parents, mtDNA is inherited solely from the mother.

MtDNA is a circular molecule that contains 37 genes, including 13 genes that encode for proteins involved in oxidative phosphorylation, a process that generates energy in the form of ATP. The remaining genes encode for rRNAs and tRNAs, which are necessary for protein synthesis within the mitochondria.

Mutations in mtDNA can lead to a variety of genetic disorders, including mitochondrial diseases, which can affect any organ system in the body. These mutations can also be used in forensic science to identify individuals and establish biological relationships.

Biological transport, active is the process by which cells use energy to move materials across their membranes from an area of lower concentration to an area of higher concentration. This type of transport is facilitated by specialized proteins called transporters or pumps that are located in the cell membrane. These proteins undergo conformational changes to physically carry the molecules through the lipid bilayer of the membrane, often against their concentration gradient.

Active transport requires energy because it works against the natural tendency of molecules to move from an area of higher concentration to an area of lower concentration, a process known as diffusion. Cells obtain this energy in the form of ATP (adenosine triphosphate), which is produced through cellular respiration.

Examples of active transport include the uptake of glucose and amino acids into cells, as well as the secretion of hormones and neurotransmitters. The sodium-potassium pump, which helps maintain resting membrane potential in nerve and muscle cells, is a classic example of an active transporter.

Mitochondrial membrane potential is the electric potential difference (voltage) across the inner mitochondrial membrane. It is negative inside the mitochondria and positive outside. This electrical gradient is established by the active transport of hydrogen ions (protons) out of the mitochondrial matrix and into the intermembrane space by complexes in the electron transport chain during oxidative phosphorylation. The energy stored in this electrochemical gradient is used to generate ATP, which is the main source of energy for cellular metabolism.

Adenosine Triphosphate (ATP) is a high-energy molecule that stores and transports energy within cells. It is the main source of energy for most cellular processes, including muscle contraction, nerve impulse transmission, and protein synthesis. ATP is composed of a base (adenine), a sugar (ribose), and three phosphate groups. The bonds between these phosphate groups contain a significant amount of energy, which can be released when the bond between the second and third phosphate group is broken, resulting in the formation of adenosine diphosphate (ADP) and inorganic phosphate. This process is known as hydrolysis and can be catalyzed by various enzymes to drive a wide range of cellular functions. ATP can also be regenerated from ADP through various metabolic pathways, such as oxidative phosphorylation or substrate-level phosphorylation, allowing for the continuous supply of energy to cells.

Diuron is a pesticide and herbicide that is used to control weeds in various settings, such as agriculture, landscaping, and forestry. Its chemical name is 3-(3,4-dichlorophenyl)-1,1-dimethylurea. Diuron works by inhibiting photosynthesis in plants, which prevents them from growing and eventually kills them.

While diuron is effective at controlling weeds, it can also have harmful effects on non-target organisms, including aquatic life and pollinators. Additionally, there are concerns about the potential for diuron to contaminate water sources and pose risks to human health. As a result, its use is regulated in many countries, and there are restrictions on how it can be applied and disposed of.

It's worth noting that Diuron is not a medical term or a drug used for treating any medical condition in humans or animals.

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.

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.

Mitochondrial SNO-proteins inhibit Complex I of the electron transport chain; modulate mitochondrial reactive oxygen species ( ... NO signaling is mediated by a coordinating complex between NO and transition metals or target cellular proteins, often via S- ... At millimolar concentrations, they may also modulate the redox state of the NMDA receptor complex. de Oliveira CP, de Lima VM, ... Hess DT, Matsumoto A, Kim SO, Marshall HE, Stamler JS (February 2005). "Protein S-nitrosylation: purview and parameters". Nat. ...
Cytochrome c oxidase, also known as complex IV, is the final protein complex in the electron transport chain. The mammalian ... so in the electron transport chain they serve solely to transport electrons through proteins. Electrons move quite long ... These linked sets of proteins are called the electron transport chain. In eukaryotes, five main protein complexes are involved ... The chain of redox reactions driving the flow of electrons through the electron transport chain, from electron donors such as ...
... is a membrane-bound protein complex present in the electron transport chain ... M.; Pereira, I. S. A. C. (2003). "A novel membrane-bound respiratory complex from Desulfovibrio desulfuricans ATCC 27774". ... Portal: Biology v t e (Cellular respiration, Integral membrane proteins, Oxidoreductases, All stub articles, Oxidoreductase ...
Thirdly, kalkitoxin blocks the electron transport chain (ETC) complex 1, one of the protein complexes involved in mitochondrial ... It also blocks the voltage-gated sodium channel and the electron transport chain (ETC) complex 1. It remains unknown how ... Kalkitoxin exerts this cytotoxic effect through inhibition of the mitochondrial electron transport chain complex 1. This causes ... and induces cellular hypoxia by inhibiting the electron transport chain (ETC) complex 1. Kalkitoxin is an ichthyotoxin, derived ...
This ubiqinone-binding protein is a subunit of mitochondrial Complex III in the electron transport chain. A mutation in the ... The protein encoded by UQCRQ has protein-protein interactions with UQCRC1, OPTN, ERCC8, GRINL1A, Dctn1, K8.1, XRCC3, PML, RAB7A ... It is a small core-associated protein and a subunit of ubiquinol-cytochrome c reductase complex III, which is part of the ... Ubiquinol-cytochrome c reductase, complex III subunit VII, 9.5kDa is a protein that in humans is encoded by the UQCRQ gene. ...
... dehalogenase complex in Dehalococcoides mccartyi strain CBDB1 suggests a protein-dependent respiratory electron transport chain ... Dehalococcoides strains do not seem to encode quinones but respire with a novel protein-bound electron transport chain. ... via changes in gene expression that likely disrupt normal electron transport chain function. When selecting Dehalococcoides ... Certain strains cannot use PCE or TCE as electron acceptors (e.g. CBDB1) and some cannot use vinyl chloride as an electron ...
... and protein subunits found in the protein complexes of the electron transport chain. Matrix (biology) Mitochondrial DNA ... the electron transport chain protein complexes, and ATP synthase. ADP acts as an activator. The mitochondria contains its own ... complex III (coenzyme Q: cytochrome c oxidoreductase), and complex IV (cytochrome c oxidase). The electron transport chain is ... which contains the electron transport chain that is found on the cristae of the inner membrane and consists of four protein ...
The protein is involved in the assembly of complex I in the mitochondrial electron transport chain. Mutations in the NDUFAF6 ... The encoded protein plays an important role in the assembly of complex I (NADH-ubiquinone oxidoreductase) of the mitochondrial ... NADH:ubiquinone oxidoreductase complex assembly factor 6 is a protein that in humans is encoded by the NDUFAF6 gene. ... The protein contains a predicted phytoene synthase domain. The NDUFAF6 gene encodes a protein that localizes to mitochondria. ...
... mistletoe is the only multicellular organism to not have a functioning respiratory complex I in its electron transport chain, a ... Viscumin strongly inhibits protein synthesis by inactivating the 60 S ribosomal subunit. The structure of this protein is very ... Viscumin is a cytotoxic protein (ribosome inactivating protein, or RIP) that binds to galactose residues of cell surface ... "How Does European Mistletoe Survive Without Complex I?". Trends in Plant Science. 23 (10): 847-850. doi:10.1016/j.tplants. ...
... is a large transmembrane protein complex that is part of the respiratory electron transport chain of mitochondria. The small ... The encoded protein interacts with MR-1S and COX7A2. This protein is required for MR-1S, PET117, and Complex IV to interact. ... The protein encoded by PET100 is involved in Complex IV biogenesis as a COX chaperone; it is required for interaction between ... This protein's N-terminus is essential for mitochondrial localization. It assembles into a 300 kDA complex which is dependent ...
Oxidative phosphorylation comprises the electron transport chain, which is a series of four protein complexes that transfer ... a process that takes place in a protein complex called photosystem I (PSI). The transport of electrons is coupled to the ... transport proteins, large signaling molecules, antibodies, and structural proteins. The basic unit (or monomer) of a protein is ... electron transport chain, and oxidative phosphorylation. Glycolysis is a metabolic process that occurs in the cytoplasm whereby ...
The cytochrome b6f protein complex catalyzes the electron transfer between plastoquinone and plastocyanin, but also transports ... It transfers the electrons further down the electron transport chain to plastocyanin, a mobile, water-soluble electron carrier ... Plastoquinone (PQ) is an isoprenoid quinone molecule involved in the electron transport chain in the light-dependent reactions ... Tikhonov, Alexander N. (2014-08-01). "The cytochrome b6f complex at the crossroad of photosynthetic electron transport pathways ...
See electron transport chain. Cytochrome c oxidases from bacteria and mitochondria Proton or sodium translocating F-type and V- ... DsbA-DsbB complex) T cell receptor transmembrane dimerization domain ] Cytochrome c nitrite reductase complex Steryl-sulfate ... In humans, 27% of all proteins have been estimated to be alpha-helical membrane proteins. Beta-barrel proteins are so far found ... Many transmembrane proteins function as gateways to permit the transport of specific substances across the membrane. They ...
... cholesterol side-chain cleavage enzyme MeSH D08.811.600.250 - electron transport chain complex proteins MeSH D08.811.600.250. ... electron transport complex i MeSH D08.811.600.250.500.750 - electron transport complex ii MeSH D08.811.600.250.500.750.500 - ... electron transport complex iii MeSH D08.811.600.317 - fatty acid synthetase complex MeSH D08.811.600.391 - glycine ... electron transport complex ii MeSH D08.811.682.830.249.500 - succinate dehydrogenase MeSH D08.811.682.830.500 - electron ...
... is the first enzyme complex in the electron transport chain of mitochondria. The iron-sulfur protein (IP) fraction is made up ... "Intron based radiation hybrid mapping of 15 complex I genes of the human electron transport chain". Cytogenetics and Cell ... Triepels RH, Van Den Heuvel LP, Trijbels JM, Smeitink JA (2001). "Respiratory chain complex I deficiency". American Journal of ... Mitochondrial complex I deficiency shows extreme genetic heterogeneity and can be caused by mutation in nuclear-encoded genes ...
An electron transport chain (ETC) is a series of protein complexes and other molecules that transfer electrons from electron ... electrons from inorganic electron donors (nitrite, ferrous iron, electron transport chain) enter the electron transport chain ... The associated electron transport chain is NADH → Complex I → Q → Complex III → cytochrome c → Complex IV → O2 where Complexes ... The overall electron transport chain can be summarized as follows: NADH+H+ → Complex I → Q ↑ Complex II ↑ Succinate → Complex ...
... the protein is a key contributor in the formation of Complex III that is part of the electron transport chain. Complex III is ... The deficiency of Complex III is more pronounced in the liver and kidneys, which leads to the symptoms seen in those with ... The BCS1L gene is responsible for the production of the BCS1L protein found in the mitochondria, which is connected to the ...
... disrupting function of Complex I in the electron transport chain. It is unknown how this mutation leads to the loss of vision ... product is a subunit of the respiratory chain Complex I that is believed to belong to the minimal assembly of core proteins ... which is located in the mitochondrial inner membrane and is the largest of the five complexes of the electron transport chain. ... MT-ND4L is a gene of the mitochondrial genome coding for the NADH-ubiquinone oxidoreductase chain 4L (ND4L) protein. The ND4L ...
... corresponding with reduced activity of complex I in the electron transport chain were reported in PD patients, while deletions ... of aminoacyl-tRNA synthetase complex and far upstream element-binding protein 1 through addition of Lys48-linked poly-Ub chains ... The precise function of parkin is unknown; however, the protein is a component of a multiprotein E3 ubiquitin ligase complex ... Miro (or RHOT1/RHOT2) is an OMM protein critical for axonal transport, and may be ubiquitinated and targeted towards ...
Pathways that are affected by pyocyanin include the electron transport chain, vesicular transport, and cell growth. An enhanced ... susceptibility to pyocyanin is seen in cells with certain mutant proteins or complexes. Mutations in genes affecting V-ATPase ... Mitochondrial electron carriers ubiquinone and nicotinic acid are also susceptible to pyocyanin. The cell cycle can be ... Secondly, phosphorylation of CFTR by Protein kinase A II should occur in order for the channel to be operational. PKA II is ...
... the fourth complex in the mitochondrial electron transport chain. Though the subunits of the protein found in affected cells ... though the mutations in cytochrome c oxidase and other electron transport chain proteins were not discovered until 1977. Joseph ... Without ATP synthase, the electron transport chain will not produce any ATP. The most common MT-ATP6 mutation found with Leigh ... a gene that codes for a protein in the last complex of the oxidative phosphorylation chain, ATP synthase, an enzyme that ...
... can be imported via the malate-aspartate shuttle system of antiporter proteins or fed into the electron transport chain using a ... α-ketoglutarate dehydrogenase complex (OGDC), branched-chain α-ketoacid dehydrogenase complex (BCKDC), and in the glycine ... that are a source of electrons for the electron transport chain, and a molecule of GTP (which is readily converted to an ATP). ... While the reactions are controlled by an electron transport chain, free electrons are not amongst the reactants or products in ...
... protein synthesis include the inactivation of ribosomes or the inhibition of complexes in the mitochondrial electron transport ... chain. These toxins have a very high affinity and level of specificity for the receptors that they bind to. Mitotoxins bind to ... Mitotoxins are responsible for mediating cell death by interfering with protein or DNA synthesis. Some mechanisms by which ...
The NDUFA9 protein is a subunit of NADH:ubiquinone oxidoreductase (Complex I of the electron transport chain), which is located ... "Intron based radiation hybrid mapping of 15 complex I genes of the human electron transport chain". Cytogenetics and Cell ... in the mitochondrial inner membrane and is the largest of the five complexes of the electron transport chain. Mutations in NADH ... The human NDUFA9 gene codes for a subunit of Complex I of the respiratory chain, which transfers electrons from NADH to ...
It functions as part of the electron transport chain and is the main subunit of transmembrane cytochrome bc1 and b6f complexes ... Electron-transfer proteins, Protein domains, Protein families, Transmembrane proteins). ... also known as the b6f complex. These complexes are involved in electron transport, the pumping of protons to create a proton- ... cytochrome b is a component of respiratory chain complex III (EC 1.10.2.2) - also known as the bc1 complex or ubiquinol- ...
It is also associated with a 15% reduction in linked complex I/III activity of the electron transport chain, which is thought ... The enzyme cytochrome c oxidase, also known as Complex IV, is a large transmembrane protein complex found in mitochondria and ... It is the last enzyme in the respiratory electron transport chain located in the inner mitochondrial or bacterial membrane. It ... 2008). "Cardiolipin and electron transport chain abnormalities in mouse brain tumor mitochondria: lipidomic evidence supporting ...
... it is found in the iron-sulfur complexes of the electron transport chains in photosynthesis. It is needed for N2 fixation by ... facilitated by transport proteins. Active transport is the uptake by cells of ions or molecules against a concentration ... Hydrogen ions are imperative for a proton gradient to help drive the electron transport chain in photosynthesis and for ... It helps in the electron transport of plant. As with other biological processes, the main useful form of iron is that of iron( ...
... the fourth complex of the electron transport chain found in the inner membrane of the mitochondria of eukaryotic cells. It ... attaches to the iron within this protein. The binding of cyanide to this enzyme prevents transport of electrons from cytochrome ... As a result, the electron transport chain is disrupted, meaning that the cell can no longer aerobically produce ATP for energy ... In organic synthesis, cyanide is a C-1 synthon; i.e., it can be used to lengthen a carbon chain by one, while retaining the ...
It is involved in the final step in the linear photosynthetic electron transport chain and has also been implicated in cyclic ... v t e (Protein pages needing a picture, Protein domains, Single-pass transmembrane proteins, All stub articles, Membrane ... electron flow around photosystem I where its role would be to return electrons from ferredoxin to the cytochrome B-F complex. ... Oxidoreductase NAD-binding domain is an evolutionary conserved protein domain present in a variety of proteins that include, ...
The cytochrome b6f complex is part of the thylakoid electron transport chain and couples electron transfer to the pumping of ... The electron transport protein plastocyanin is present in the lumen and shuttles electrons from the cytochrome b6f protein ... The carriers in the electron transport chain use some of the electron's energy to actively transport protons from the stroma to ... these proteins make use of light energy to drive electron transport chains that generate a chemiosmotic potential across the ...
Mitochondrial SNO-proteins inhibit Complex I of the electron transport chain; modulate mitochondrial reactive oxygen species ( ... NO signaling is mediated by a coordinating complex between NO and transition metals or target cellular proteins, often via S- ... At millimolar concentrations, they may also modulate the redox state of the NMDA receptor complex. de Oliveira CP, de Lima VM, ... Hess DT, Matsumoto A, Kim SO, Marshall HE, Stamler JS (February 2005). "Protein S-nitrosylation: purview and parameters". Nat. ...
Encephalopathy may accompany acute renal failure and presents with a complex of symptoms progressing from m … ... Electron Transport Chain Complex Proteins / metabolism* * Energy Metabolism / physiology* * Humans * Kidney / metabolism ... The present findings suggest that the inhibition of mitochondrial respiratory chain complexes and creatine kinase caused by the ... Thus, we measured mitochondrial respiratory chain complexes and creatine kinase activities in rat brain and kidney after ...
Moreover, viral proteins can bind to mitochondrial complexes, disrupting mitochondrial function and causing the immune cells to ... TOM70 is involved in protein transport for electron transport chain complex assembly in mitochondria [174]. TOM70 interacts ... Mitochondrial electron transport chain complex III sustains hepatitis E virus replication and represents an antiviral target. ... When the mitochondrial membrane and electron transport chain complex are disrupted, more ROS are generated due to the loss of ...
By targeting electron transport chain complex 1 and independently of AMP-activated protein kinase... (More). Acute respiratory ... By targeting electron transport chain complex 1 and independently of AMP-activated protein kinase (AMPK) or NF-κB, metformin ... By targeting electron transport chain complex 1 and independently of AMP-activated protein kinase (AMPK) or NF-κB, metformin ... Pyrin Domain-Containing 3 Protein/metabolism, Nucleoside-Phosphate Kinase/metabolism, Pneumonia/metabolism, Respiratory ...
... the final protein carrier in the mitochondrial electron-transport chain.. Plays a role in apoptosis. Suppression of the anti- ... Cytochrome c then transfers this electron to the cytochrome oxidase complex, ... Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the ... Proteins and Peptides. Proteomics tools. Agonists, activators, antagonists and inhibitors. Cell lines and Lysates. Multiplex ...
... and protection over key electron transport chain proteins including complexes I and IV [131, 132]. These studies showed that ... protein oxidation can lead to PSSG, protein aggregation, decreased crystallin, protein solubility abnormalities, and an overall ... prevents protein aggregation, and maintains lens protein functionality. Because of increasing protein oxidation and ... Upregulation of hypoxic stress-induced proteins, such as hypoxia-inducible factor-1α and heat shock proteins, have been shown ...
GO and electron transport chain complex proteins. Similarly, Sirt3 is a mitochondrial deacetylase that has been extensively ... Hydroxyacyl-CoA Dehydrogenase (HADHA) and Long Chain Acyl-CoA Dehydrogenase (LCAD) catalyze the oxidation of long chain fatty ... We aim to investigate: 1) The mechanisms as to how acetylation regulates the activities of FAO and GO proteins in young and old ... These studies will provide us novel insights into the regulatory role of both FAO and GO protein acetylation on mitochondrial ...
These redox reactions, called electron transport chains, form a series of protein complexes within the cells mitochondria that ... during which electrons are transferred from electron donors to electron acceptors (such as oxygen in redox reactions), using ... Magnesium is intimately involved in potassium transport. Magnesium depletion and potassium depletion cause similar damaging ...
... is responsible for shuttling electrons between two of these protein complexes in the photosynthetic electron transport chain. ... driven by large protein complexes at internal membranes of vegetal cells. The protein plastocyanin (Pc) ... For an efficient electron flow, Pc must transiently bind its partner complex (Photosystem I) keeping a balance between ... A novel function of Capicua family proteins The Capicua (Cic) protein is an evolutionarily conserved nuclear factor with ...
It carries electrons to the electron transport chain, where the electrons are passed along a series of protein complexes, ... NADH then donates its electrons to the electron transport chain, which is a series of protein complexes in the inner ... NADH also donates electrons to the electron transport chain, but at a higher energy level. NAD+ is the oxidized form of NADH ... These electron carriers are then used in the electron transport chain to produce ATP. Since each pyruvate molecule produces 3 ...
In this Part 2, you will see four different protein complexes that make up the mitochondrial electron transport chain. And ... four protein complexes that are involved in ATP synthesis. They are indicated as complex 1, complex 2, complex 3, and complex 4 ... Its these four complexes that get and give electrons by means of mobile electron carriers. So lets see how that works. ... each complex by itself can work to generate the proton and voltage gradient. But now, complexes 1, 3, and 4 are known to be ...
Overall, these results highlight the complex nature of organic matter transformation in NRZs and the microbial metabolic ... served as the sole source of electron donors and microorganisms. The microcosms were constructed and incubated under anaerobic ... served as the sole source of electron donors and microorganisms. The microcosms were constructed and incubated under anaerobic ... and accessory/maturation proteins; electron transport chain (ETC)/oxidative phosphorylation: 81, ETC complex I-NADH:ubiquinone ...
... the last of the enzymes in the mitochondrial electron transport chain and represents a large integral membrane protein complex ... New technologies for purifying membrane-bound protein complexes in combination with cryo-electron microscopy (EM) have recently ... Cross-linking, in general, involves the covalent linkage of two amino acid residues of proteins or protein complexes in close ... The activity of most proteins and protein complexes relies on the formation of defined three-dimensional structures. The ...
Electron Transport Chain Complex Proteins - Preferred Concept UI. M0447484. Scope note. A complex of enzymes and PROTON PUMPS ... Electron Transport Chain Complex Proteins Descriptor Spanish: Proteínas del Complejo de Cadena de Transporte de Electrón ... Electron Transport Chain Complex Proteins [D08.811.600.250] Electron Transport Chain Complex Proteins ... Electron Transport Chain Complex Proteins [D12.776.543.277] Electron Transport Chain Complex Proteins ...
Electron Transport Complex II [D12.776.331.199.750]. *Membrane Proteins [D12.776.543]. *Electron Transport Chain Complex ... "Electron Transport Complex II" by people in this website by year, and whether "Electron Transport Complex II" was a major or ... "Electron Transport Complex II" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH ( ... Below are the most recent publications written about "Electron Transport Complex II" by people in Profiles. ...
AMPK function; expression of mitochondrial electron transport chain (ETC) complex proteins I-V, Dll4, and Jag1; mitochondrial ... G-protein-coupled receptor 120 (GPR120), as a member of the rhodopsin family of G-protein-coupled receptors, has been shown to ... Expression of mitochondrial transcription factor, PGC-1α, ETC complex proteins I-V, and mitochondrial number were decreased in ... AMPK agonists A769662 and metformin increased the mitochondrial complex proteins and number, in vitro angiogenesis, and Jag1 ...
The electron transport chain (or respiratory chain) is a series of mitochondrial protein complexes (Complexes I-IV) that ... Complex IV (cytochrome c oxidase) is the terminal complex of the respiratory chain, responsible for transporting electrons from ... By coupling this electron transport with active proton pumping across the inner mitochondrial membrane, an electrochemical ... Immunoprecipitation for Native Proteins. This protocol is intended for immunoprecipitation of native proteins for analysis by ...
Complex I) which is the first enzyme in the electron transport chain of mitochondria. This protein localizes to the inner ... involved_in mitochondrial electron transport, NADH to ubiquinone NAS Non-traceable Author Statement. more info ... involved_in mitochondrial respiratory chain complex I assembly IBA Inferred from Biological aspect of Ancestor. more info ... part_of mitochondrial respiratory chain complex I IBA Inferred from Biological aspect of Ancestor. more info ...
Electrons from NADH and FADH2 are passed to protein complexes in the electron transport chain. As they are passed from one ... accessory electron carriers, is called the electron transport chain. The electron transport chain is present in multiple copies ... In each transfer of an electron through the electron transport chain, the electron loses energy, but with some transfers, the ... In the fourth protein complex, the electrons are accepted by oxygen, the terminal acceptor. The oxygen with its extra electrons ...
... the final electron acceptor. As the electrons pass through the protein complexes of the electron transport chain, their energy ... Electron-transport chains , Credit: humanbiology.pressbooks.tru.ca. Electron Transport Chain (ETC): The electron transport ... During electron transport in the electron transport chain, NADH and FADH2 donate their electrons, which pass through complexes ... Overall Function: Complex IV serves as the final electron transfer point in the electron transport chain, accepting electrons ...
S2D and reduced electron transport chain ETC proteins, notably complex II, reflecting transcriptional downregulation of SDH ... post transcriptional mechanisms stromectol The receptor will thus form a real signaling platform made up of several proteins ...
The chain consists of a series of electron carriers Most of which are proteins that exist in large complexes Electrons are ... Electron carriers such as NADH deliver their electrons to an electron transport chain embedded in the inner membrane of the ... to the next in the electron transport chain Lets take a closer look at the path electrons take through the chain As electrons ... move along each step of the chain they give up a bit of energy The oxygen you breath pulls electrons from the transport chain ...
... the electron transport chain and chemiosmosis. The electron transport chain is a series of protein complexes that transfer ... transferring electrons from NADH and FADH2 to oxygen through a series of protein complexes called the electron transport chain ... In the electron transport chain, electrons are transferred from NADH and FADH2 to oxygen, forming water. The electron transfer ... The NADH and FADH2 molecules carry electrons to the electron transport chain, where they generate more ATP through oxidative ...
... glucose using oxygen and then turn it into energy using protein complexes called the mitochondrial electron transport chain. ... Proteins make up the mitochondrial transport chain, and some fatty acids also play a crucial role. Other compounds, like ... stimulates the protein chain which plays a crucial role in the Krebs cycle, and boosts the mitochondrias ability to produce ... Carnitine transports the acids needed for the ATP-making process. Red meat is full of it. ...
... glucose using oxygen and then turn it into energy using protein complexes called the mitochondrial electron transport chain. ... Proteins make up the mitochondrial transport chain, and some fatty acids also play a crucial role. Other compounds, like ... stimulates the protein chain which plays a crucial role in the Krebs cycle, and boosts the mitochondrias ability to produce ... Carnitine transports the acids needed for the ATP making process. Red meat is full of it. ...
... as well as genes encoding proteins in complexes I, II, III, and IV of the electron transport chain. These changes were ... genes of the electron transport chain), nuclear genes encoding mitochondrial proteins (e.g., mitochondrial carrier proteins), ... complex II (SDHB), complex III (CYC1), complex IV (SURF1), and a mitochondrial carrier protein (SLC25A12). Data are shown as ... complex II (SDHB), complex III (CYC1), complex IV (SURF1), and a mitochondrial carrier protein (SLC25A12). Data are shown as ...
Water is split to release the electron that travels the electron transport chain in a protein complex right at the beginning of ... around the electron transport chains that funnel the photons to that first protein complex (the major protein is D1). ... Below, you will find some images of diatoms as seen through an electron microscope (left) and immersed in oil seen through a ... the chain. Chlorophyll and other pigments are a network, umbrella, ...
Proteins with iron-containing heme complex used to transfer electrons in the electron transport chain. ... What is the electron transport chain?. Electron transport chain is a process that takes place in the inner membrane of the ... What is the electron transport chain?. The electron transport chain is a series of chemical reactions that occurs during ... What are the end products of the electron transport chain?. The end products of the electron transport chain are ATP and water. ...
Electrons from NADH and FADH2 are passed to protein complexes in the electron transport chain. As they are passed from one ... accessory electron carriers, is called the electron transport chain. The electron transport chain is present in multiple copies ... Electron Transport Chain. Most ATP from glucose is generated in the electron transport chain. It is the only part of cellular ... The electron transport chain is made up of 4 proteins along the membrane and a proton pump. A cofactor shuttles electrons ...
... a cluster of proteins vital to the function of the electron transport chain. This results in a dampening of the production of ... "Evidence that metformin exerts its anti-diabetic effects through inhibition of complex 1 of the mitochondrial respiratory chain ... This occurs over a period of hours and inhibits the operation of the electron transport chain, which reduces ATP production. ... 47] Y. Yi, W. Zhang, J. Yi, and Z.-X. Xiao, "Role of p53 Family Proteins in Metformin Anti-Cancer Activities," J. Cancer, vol. ...
  • Rather, it derives from a process that begins with passing electrons through a series of chemical reactions to a final electron acceptor, oxygen. (opentextbooks.org.hk)
  • Electron transport is a series of chemical reactions that resembles a bucket brigade in that electrons are passed rapidly from one component to the next, to the endpoint of the chain where oxygen is the final electron acceptor and water is produced. (opentextbooks.org.hk)
  • In the fourth protein complex, the electrons are accepted by oxygen, the terminal acceptor. (opentextbooks.org.hk)
  • In aerobic respiration, oxygen serves as the final electron acceptor, enabling the efficient production of ATP. (microbiologynote.com)
  • The oxygen serves as the last electron acceptor molecule during the oxidative phosphorylation process. (lambdageeks.com)
  • An electron transport chain works because each acceptor, the next in the chain, is more electronegative than the donor. (ishinobu.com)
  • For an electron transport chain to function - allowing electrons to pass through - an exogenous electron acceptor must be present at the end of the chain. (ishinobu.com)
  • Dr Matt Johnson, reader in Biochemistry at the University of Sheffield and one of the supervisors of the study added: "Cytochrome b6f is the beating heart of photosynthesis which plays a … Afterward, the electron acceptor of PSI may redirect electrons to ferredoxin-thioredoxin reductase (FTR) to form reduced thioredoxin, to ferredoxin-NADPH reductase (FNR) to generate NADPH, or to molecular oxygen to form hydrogen peroxide (H2O2). (rehabsociety.org.hk)
  • A glycolysis and fermentation only B glycolysis and the citric acid cycle only C glycolysis, pyruvate oxidation, and the citric acid cycle D oxidative phosphorylation only E glycolysis, pyruvate oxidation, the citric acid cycle, and oxidative phosphorylation, using an electron acceptor other than oxygen An organism is discovered that thrives both in the presence and absence of oxygen in the air. (vumc.org)
  • It is widely accepted that in conditions leading to over-reduction, pseudo-cyclic electron transfer enables electrons to flow from water to PSI, with molecular oxygen as alternative electron acceptor 5 . (nature.com)
  • A complex of enzymes and PROTON PUMPS located on the inner membrane of the MITOCHONDRIA and in bacterial membranes. (bvsalud.org)
  • This protein localizes to the inner membrane of the mitochondrion as a single-pass membrane protein. (nih.gov)
  • These reactions take place in specialized protein complexes located in the inner membrane of the mitochondria of eukaryotic organisms and on the inner part of the cell membrane of prokaryotic organisms. (opentextbooks.org.hk)
  • Hydrogen ions diffuse through the inner membrane through an integral membrane protein called ATP synthase ( Figure 4.15 b). (opentextbooks.org.hk)
  • These electron transfers generate a flow of protons across the inner membrane into the intermembrane space, creating an electrochemical gradient. (24insight.com)
  • The electron transport chain is a series of proteins and organic molecules found in the inner membrane of the mitochondria. (vumc.org)
  • The inner membrane houses the mitochondrial respiratory chain . (histocutup.co.uk)
  • Four protein complexes in the inner membrane make up the electron transport chain (ETC, also known as the electron transport system), which converts the redox energy stored as NADH and FADH 2 into chemical energy in the form of ATP. (biomedcentral.com)
  • Full length native protein (purified) corresponding to Cow Cytochrome C. Bovine heart Cytochrome C. (abcam.com)
  • Cyanide inhibits cytochrome c oxidase, a component of the electron transport chain. (opentextbooks.org.hk)
  • Complex III or coenzyme Q : cytochrome c - oxidoreductase, sometimes also called the cytochrome bc 1 complex is a complex of the electron transfer pathway . (mitophysiology.org)
  • The cytochrome b6f complex occupies a central position in the sequence of photosynthetic electron transport carriers, oxidizing plastoquinol (PQH 2) and providing the electron transfer connection between the two reaction center complexes, PS II and PS I, to which H + transfer is coupled, thus contributing to the trans-membrane. (rehabsociety.org.hk)
  • The structure of the cytochrome b6f complex was determined by isomorphous replacement, and the cytochrome b6f complex transfers 2H+ to the lumen (Kurisu et al. (rehabsociety.org.hk)
  • Sheffield University doctor and biochemist Matt Johnson, one of the study supervisors, adds that "the Cytochrome b6f it is the heart of photosynthesis, which plays a crucial role in the regulation of photosynthetic efficiency, and that in previous studies have shown that by manipulating the levels of this complex we can grow larger and better plants. (rehabsociety.org.hk)
  • The electron transport chain is also called the Cytochrome oxidase system or as the Respiratory chain. (vumc.org)
  • It is a cytochrome protein that contains IRON and MOLYBDENUM. (lookformedical.com)
  • The 30-kDa membrane-bound c-type cytochrome protein of mitochondria that functions as an electron donor to CYTOCHROME C GROUP in the mitochondrial and bacterial RESPIRATORY CHAIN. (lookformedical.com)
  • A bacterial protein from Pseudomonas, Bordetella, or Alcaligenes which operates as an electron transfer unit associated with the cytochrome chain. (lookformedical.com)
  • Cytochrome bc1, a dimeric multi-subunit electron-transport protein embedded in the inner mitochondrial membrane, is a major drug target for the treatment and prevention of malaria and toxoplasmosis. (liverpool.ac.uk)
  • However, owing to the limited amount of cytochrome bc1 that may be available from parasites, all efforts have been focused on homologous cytochrome bc1 complexes from mammalian species, which has resulted in the failure of some drug candidates owing to toxicity in the host. (liverpool.ac.uk)
  • Here, it is demonstrated that cytochrome bc1 is highly amenable to single-particle cryo-EM (which uses significantly less protein) by solving the apo and two inhibitor-bound structures to ∼4.1 Å resolution, revealing clear inhibitor density at the binding site. (liverpool.ac.uk)
  • Fd acts simultaneously as a bottleneck and as a hub which distributes high-energy electrons to a multitude of enzymes, which include nitrite reductase, sulphite reductase, fatty acid desaturase, glutamine-2-oxoglutarate amino transferase (GOGAT), redox complexes such as cytochrome b 6 /f for cyclic electron transport (CET) and thioredoxins 2 . (nature.com)
  • Electrons from NADH and FADH2 are passed to protein complexes in the electron transport chain. (opentextbooks.org.hk)
  • The resulting acetyl-CoA molecules enter the Krebs cycle, generating additional carbon dioxide, ATP, and electron carriers (such as NADH and FADH2). (microbiologynote.com)
  • It involves transferring electrons from NADH and FADH2 to oxygen through a series of protein complexes called the electron transport chain. (stemcelldaily.com)
  • Magnesium is a modulator of oxidative phosphorylation, during which electrons are transferred from electron donors to electron acceptors (such as oxygen in redox reactions), using magnesium as a cofactor. (hippocrates.com.au)
  • We conducted a 20-day microcosm experiment in which NRZ sediments, which were enriched in buried woody plant material, served as the sole source of electron donors and microorganisms. (frontiersin.org)
  • An electron transport chain comprises electron transfer between a series of electron donors and acceptors. (ishinobu.com)
  • The electron transport chain ETC is a series of protein complexes that transfer electrons from electron donors to electron acceptors via redox reactions both reduction and oxidation occurring simultaneously and couples this electron transfer with the transfer of protons. (vumc.org)
  • The electron transport chain ( Figure 4.15 a) is the last component of aerobic respiration and is the only part of metabolism that uses atmospheric oxygen. (opentextbooks.org.hk)
  • The oxygen with its extra electrons then combines with two hydrogen ions, further enhancing the electrochemical gradient, to form water. (opentextbooks.org.hk)
  • If there were no oxygen present in the mitochondrion, the electrons could not be removed from the system, and the entire electron transport chain would back up and stop. (opentextbooks.org.hk)
  • Oxygen is essential for the electron transport chain, which occurs in the mitochondria of eukaryotic cells. (microbiologynote.com)
  • The mitochondria break down glucose using oxygen and then turn it into energy using protein complexes called the mitochondrial electron transport chain. (recharge.health)
  • Within the mitochondria, CoQ10 is a vital component of the electron transport chain, a series of protein complexes that produce ATP by transferring electrons from food molecules to oxygen. (opanutrition.com)
  • D all respiring cells, both prokaryotic and eukaryotic, using either oxygen or other electron acceptors. (vumc.org)
  • The absence of mitochondria and other organelles in red blood cells leaves room for the millions of hemoglobin molecules needed in order to transport oxygen throughout the body. (nir1000.com)
  • Over-reduction of PET chain can damage protein complexes and result in production of the excess amounts of reactive oxygen species (ROS) 6 . (nature.com)
  • As a result, more oxygen is transported to the muscle cells to produce energy and other metabolic waste by-products are removed from the working muscles more rapidly. (bigskymultisportcoaching.com)
  • CO readily crosses capillary membranes in the lungs and binds the heme moiety on the erythrocyte hemoglobin complex with an affinity 200-300 times greater than that of oxygen. (medscape.com)
  • This binding drastically reduces the number of binding spots available for oxygen transport. (medscape.com)
  • During the electron transport chain, each NADH molecule produces 3 molecules of ATP, so the total number of ATP molecules produced is 45 x 3 = 135. (proprofs.com)
  • Major histocompatibility complex class I (MHC I) molecules present antigenic peptides to cytotoxic T cells to eliminate infected or cancerous cells. (researchgate.net)
  • a) The electron transport chain is a set of molecules that supports a series of oxidation-reduction reactions. (opentextbooks.org.hk)
  • These processes require energy to synthesize complex molecules necessary for cellular growth, maintenance, and functioning. (microbiologynote.com)
  • Enzymes and other proteins use ATP to power reactions, maintain ion gradients across membranes, contract muscle fibers, and transport molecules across cellular membranes. (microbiologynote.com)
  • Nutrients and other molecules are imported into the cell, metabolized (broken down) and possibly synthesized into new molecules, modified if needed, transported around the cell, and possibly distributed to the entire organism. (libretexts.org)
  • For example, the large proteins that make up muscles are built from smaller molecules imported from dietary amino acids. (libretexts.org)
  • Just as energy is required to both build and demolish a building, energy is required for the synthesis and breakdown of molecules as well as the transport of molecules into and out of cells. (libretexts.org)
  • mtDNA encodes for 13 of the respiratory chain enzymes, along with 24 RNA molecules used in intramitrochondrial protein synthesis. (medscape.com)
  • The electron transport chain is a series of molecules that accept or donate electrons easily. (vumc.org)
  • Coenzymes are non-protein molecules while cofactors are composed of amino acids. (vumc.org)
  • Proteins synthesized from mtDNA also encode for the production of the RNA molecules transfer RNA and ribosomal RNA. (nir1000.com)
  • Within the inner mitochondrial membrane are a series of protein complexes and electron carrier molecules, which form the electron transport chain (ETC). The ETC represents the third stage of aerobic cellular respiration and the stage where the vast majority of ATP molecules are generated. (nir1000.com)
  • By targeting electron transport chain complex 1 and independently of AMP-activated protein kinase (AMPK) or NF-κB, metformin blocked LPS-induced and ATP-dependent mitochondrial (mt) DNA synthesis and generation of oxidized mtDNA, an NLRP3 ligand. (lu.se)
  • Cells require a constant supply of energy to perform vital functions, including nutrient uptake, protein synthesis, DNA replication, and active transport across cell membranes. (microbiologynote.com)
  • Similarly, PGC1α increases the transcription of enzymes necessary for substrate oxidation, electron transport, and ATP synthesis. (diabetesjournals.org)
  • Mitochondrial translation, essential for synthesis of the electron transport chain complexes in the mitochondria, is governed by nuclear encoded genes. (prolekarniky.cz)
  • Amino acids can be employed in energy generation but as their main function is to form the building blocks of proteins catabolising them in energy production disrupts protein synthesis and therefore tends to be used only as a last resort. (histocutup.co.uk)
  • New technologies for purifying membrane-bound protein complexes in combination with cryo-electron microscopy (EM) have recently allowed the exploration of such complexes under near-native conditions. (researchgate.net)
  • Oxidative stress can denature lipids and proteins [ 10 , 12 - 14 ], as well as induce DNA and RNA fragmentation [ 15 - 17 ], leading to cell dysfunction, injury, and death. (hindawi.com)
  • Some protein complexes use electron transport chains to transfer H + ions (protons) across a membrane. (ishinobu.com)
  • The NADH and NADPH derived from various metabolic reactions in the mitochondrial matrix interact with the proteins of the mitochondrial respiratory chain and result in hydrogen ions (protons) being pumped out of the matrix into the space between the inner and outer mitochondrial membranes. (histocutup.co.uk)
  • These include cytochromes, which are haem-containing proteins that use iron to carry electrons and coenzyme Q, which can transport both electrons and protons. (histocutup.co.uk)
  • As electrons are shuttled through the complexes I, III and IV by electron carriers, protons (H + ) are moved from the mitochondrial matrix into the intermembrane space. (biomedcentral.com)
  • The preferred route for protons in the intermembrane space to re-enter the matrix, in an attempt to flow down the gradient and re-establish equilibrium, is to enter through the ATP synthase enzyme complex. (biomedcentral.com)
  • Each step is a complex multistep enzymatic reaction process that involves different substrates, intermediates, products, enzymes, and coenzymes. (stemcelldaily.com)
  • In vascular plants, photosynthetic electron transport (PET) chain produces reductive power that is utilised by diverse acceptors involved in both chloroplast and cellular metabolism 1 . (nature.com)
  • Loss of Pink1 modulates synaptic mitochondrial bioenergetics in the rat striatum prior to motor symptoms: concomitant complex I respiratory defects and increased complex II-mediated respiration. (ouhsc.edu)
  • In cellular respiration process basically the nutrient or food molecule like carbohydrate, proteins participates in respiration process to produce energy. (lambdageeks.com)
  • These muscles each offer unique advantages across a host of methodologies including measuring isometric force production, susceptibility to muscle injury, mitochondrial respiration, protein content, and histology. (biomedcentral.com)
  • Mitochondrial DNA (mtDNA) encodes for proteins that are involved in electron transport and oxidative phosphorylation, which occur in cellular respiration. (nir1000.com)
  • Cardiac function, utilizing the Vevo 2100 Imaging System, electron transport chain complex activities, and mitochondrial respiration assessed cardiac and mitochondrial function. (cdc.gov)
  • In knockout animals, complex I, III, and IV activities (approximately 2- to 6-fold) and fatty acid respiration (approximately 5-fold) were significantly increased. (cdc.gov)
  • The protein plastocyanin (Pc) is responsible for shuttling electrons between two of these protein complexes in the photosynthetic electron transport chain. (icrea.cat)
  • During oxidative phosphorylation, electrons are transferred through a series of protein complexes, known as the electron transport chain, located within the inner mitochondrial membrane. (24insight.com)
  • The mitochondrial respiratory chain (also known as the electron transport chain) is composed of four complexes. (histocutup.co.uk)
  • These feature various proteins and coenzymes. (histocutup.co.uk)
  • In mammalian cells, most of the redox potential used for generating ATP arrives at the mitochondrion in the form of the nicotinamide adenine dinucleotide (NADH) and flavin adenine dinucleotide (FADH 2 ), reduced coenzymes generated by the acceptance of electrons derived from the breakdown of organic substances in the tricarboxylic acid (TCA) cycle. (biomedcentral.com)
  • It is a component of flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN), coenzymes that participate in the electron transport chain-a series of reactions occurring in the mitochondria that generate ATP, the energy currency of the cell. (ushealthcrisis.com)
  • Gnaiger E (2023) Complex II ambiguities ― FADH 2 in the electron transfer system. (bioblast.at)
  • Single molecule force spectroscopy setup to evaluate interactions between partners photosynthetic complex I (PSI) and plastocyanin (Pc) under illumination and redox control (oxidized, reduced). (icrea.cat)
  • Reduction is a gain of electrons, or a decrease in oxidation state by a molecule, atom, or ion. (ishinobu.com)
  • A chemical reaction in which an electron is transferred from one molecule to another. (lookformedical.com)
  • the electron-accepting molecule is the oxidizing agent or oxidant. (lookformedical.com)
  • Riboflavin (B2) participates in the electron transport chain, a critical process within the mitochondria responsible for generating the bulk of ATP-the molecule that powers cellular activities. (ushealthcrisis.com)
  • These electron carriers are then used in the electron transport chain to produce ATP. (proprofs.com)
  • There are four complexes composed of proteins, labeled I through IV in Figure 4.15 c, and the aggregation of these four complexes, together with associated mobile, accessory electron carriers, is called the electron transport chain . (opentextbooks.org.hk)
  • The electron carriers then enter the electron transport chain, located in the inner mitochondrial membrane, where oxidative phosphorylation takes place. (microbiologynote.com)
  • This allows the recycling of the electron carriers (NADH) back into their oxidized forms (NAD+), enabling glycolysis to continue. (microbiologynote.com)
  • B the thermodynamically favorable flow of electrons from NADH to the mitochondrial electron transport carriers. (vumc.org)
  • These redox reactions, called electron transport chains, form a series of protein complexes within the cell's mitochondria that release energy or ATP. (hippocrates.com.au)
  • Electron transport chains are formed by protein complexes embedded in a membrane that act concertedly during a sequence of redox reactions. (ishinobu.com)
  • Electrons are passed from one member of the transport chain to another in a series of redox reactions. (vumc.org)
  • In photosynthesis, final electron transfer from ferredoxin to NADP + is accomplished by the flavo enzyme ferredoxin:NADP + oxidoreductase (FNR). (nature.com)
  • Vercellino I, Sazanov LA (2022) The assembly, regulation and function of the mitochondrial respiratory chain. (mitophysiology.org)
  • Ganguly U, Bir A, Chakrabarti S (2022) Cytotoxicity of mitochondrial Complex I inhibitor rotenone: a complex interplay of cell death pathways. (mitophysiology.org)
  • Banerjee R, Purhonen J, Kallijärvi J (2022) The mitochondrial coenzyme Q junction and Complex III: biochemistry and pathophysiology. (mitophysiology.org)
  • Maklashina E, Iverson TM, Cecchini G (2022) How an assembly factor enhances covalent FAD attachment to the flavoprotein subunit of complex II. (bioblast.at)
  • We have employed electron paramagnetic resonance (EPR) spectroscopy to study free radical formation and electron partitioning in TROL-depleted chloroplasts. (nature.com)
  • Compared with individual exposures, co-exposure aerosols produced greater acellular and cellular oxidants detected by electron paramagnetic resonance (EPR) spectroscopy, and in vivo immune-spin trapping (IST), as well as synergistically increased lavage neutrophils, lavage proteins and inflammation related gene/protein expression. (cdc.gov)
  • In the electron transport chain, the free energy from the series of reactions just described is used to pump hydrogen ions across the membrane. (opentextbooks.org.hk)
  • The result of the reactions is the production of ATP from the energy of the electrons removed from hydrogen atoms. (opentextbooks.org.hk)
  • Hydrogen (H), with an oxidation state of +1, is the strongest reductant, as it freely gives its sole electron for chemical reactions. (ishinobu.com)
  • Electron transfer is the elemental transaction in chemical reactions. (ishinobu.com)
  • Niacin (B3) facilitates reactions that extract energy from fats, carbohydrates, and proteins. (ushealthcrisis.com)
  • Photosynthesis is a fundamental process that uses light to synthesize molecular fuel, driven by large protein complexes at internal membranes of vegetal cells. (icrea.cat)
  • Thus, we measured mitochondrial respiratory chain complexes and creatine kinase activities in rat brain and kidney after administration of contrast media. (nih.gov)
  • The present findings suggest that the inhibition of mitochondrial respiratory chain complexes and creatine kinase caused by the acute renal failure induced by contrast media administration may be involved in the neurological complications reported in patients and might play a role in the pathogenesis of the encephalopathy caused by acute renal failure. (nih.gov)
  • Activities of respiratory chain complexes and citrate synthase influenced by pharmacologically different antidepressants and mood stabilizers. (nel.edu)
  • cDNA of eight nuclear encoded subunits of NADH:ubiquinone oxidoreductase: human complex I cDNA characterization completed. (nih.gov)
  • Kumar R, Landry AP, Guha A, Vitvitsky V, Lee HJ, Seike K, Reddy P, Lyssiotis CA, Banerjee R (2021) A redox cycle with complex II prioritizes sulfide quinone oxidoreductase dependent H 2 S oxidation. (bioblast.at)
  • Ethidium Bromide treated cells are depleted of mitochondrial DNA (mtDNA) and mtDNA encoded proteins. (cellsignal.com)
  • Pyridoxine (B6) influences the metabolism of amino acids, the building blocks of proteins, thereby indirectly impacting energy production. (ushealthcrisis.com)
  • Activity and protein expression of Na+/K+ ATPase are reduced in microvillous syncytiotrophoblast plasma membranes isolated from pregnancies complicated by intrauterine growth restriction. (ucdenver.edu)
  • Activity and protein expression of the Na+/H+ exchanger is reduced in syncytiotrophoblast microvillous plasma membranes isolated from preterm intrauterine growth restriction pregnancies. (ucdenver.edu)
  • Each of these membranes is a phospholipid bilayer with embedded proteins. (nir1000.com)
  • FNR is recruited to thylakoid membranes via integral membrane thylakoid rhodanase-like protein TROL. (nature.com)
  • The buried organic matter (e.g., weathered plant biomass) in these deposits has likely served as a long-lived electron donor fueling sulfate reduction and, directly or indirectly, Fe(III) and U(VI) reduction, thus contributing to the formation of iron sulfide minerals and deposits of poorly soluble U(IV) (e.g. (frontiersin.org)
  • We propose that the dynamic binding and release of FNR from TROL can control the flow of photosynthetic electrons prior to activation of the pseudo-cyclic electron transfer pathway. (nature.com)
  • This is known as the linear electron transfer (LET) pathway 1 . (nature.com)
  • Some bacterial pathogens have been shown to substantially modify their surface components in response to the host immune system and modify their energy metabolism and transport pathways to allow efficient growth within the host. (cdc.gov)
  • As shown in Figure 1 , in the absence of oxidative stress, Kelch-like ECH-associated protein 1 (Keap1) keeps Nrf2 sequestered in the cytosol, where it mediates proteasomal degradation of Nrf2 [ 25 - 27 ]. (hindawi.com)
  • In reduction reaction the amount of positive charge of the atom is reduced when adding negatively charged electron. (proprofs.com)
  • This is because electrons have a negative charge, and when they are added to an atom, they neutralize some of the positive charge, resulting in a reduction of the overall positive charge of the atom. (proprofs.com)
  • Reduction potential is the tendency of a chemical species to acquire electrons, and thereby be reduced. (ishinobu.com)
  • To summarize, redox is a change during a reaction that involves loss or gain of electrons, with reduction a gain and oxidation a loss. (ishinobu.com)
  • very positive reduction potentials because of their unique coordination That is just like the FeS cluster in complex III. (rehabsociety.org.hk)
  • NAD+ is able to receive and transport electrons and is therefore important in many oxidation-reduction processes. (histocutup.co.uk)
  • The electron transport chain is present in multiple copies in the inner mitochondrial membrane of eukaryotes and in the plasma membrane of prokaryotes. (opentextbooks.org.hk)
  • In prokaryotes the respiratory electron transport chain is located. (vumc.org)
  • Where is the electron transport chain found within prokaryotes? (vumc.org)
  • Metabolism is sometimes defined more expansively, for an organism rather than at the cellular level, thus including digestion and the transport of substances between cells. (ishinobu.com)
  • This pyruvate is then transported into the mitochondria, the cellular powerhouses, to undergo further oxidation. (ushealthcrisis.com)
  • Hydroxyacyl-CoA Dehydrogenase (HADHA) and Long Chain Acyl-CoA Dehydrogenase (LCAD) catalyze the oxidation of long chain fatty acids, whereas pyruvate dehydrogenase (PDH) catalyzes glucose oxidation in the heart. (wvu.edu)
  • Mitochondria are cellular organelles that harvest energy in the form of ATP through a process termed oxidative phosphorylation (OXPHOS), which occurs via the protein complexes of the electron transport chain (ETC). In recent years it has become unequivocally clear that mitochondrial complexes of. (sagepub.com)
  • Where does respiratory electron transport chain occurs? (vumc.org)
  • Overall, these results highlight the complex nature of organic matter transformation in NRZs and the microbial metabolic pathways that interact to mediate redox status and elemental cycling. (frontiersin.org)
  • This gene encodes an accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which is the first enzyme in the electron transport chain of mitochondria. (nih.gov)
  • Mutations in this gene contribute to mitochondrial complex 1 deficiency. (nih.gov)
  • A second group of methods, which includes DNA microarrays and proteomics, have advantages that overcome the limitations implicit in signature-tagged mutagenesis and in vivo expression technology, namely, the ability to directly measure expression (gene or protein) levels on a true genome-wide scale, but their application to analysis of bacterial pathogens during real infections is still in its infancy. (cdc.gov)
  • Skeletal muscle MnSOD, mitochondrial complex II, and SIRT3 enzyme activities are decreased in maternal obesity during human pregnancy and gestational diabetes mellitus. (ouhsc.edu)
  • 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). (lookformedical.com)
  • Complex II of the chain is the succinate dehydrogenase enzyme complex. (histocutup.co.uk)
  • This enzyme is also part of the citric acid cycle and uses the electron carrier flavin adenine dinucleotide (FAD/FADH). (histocutup.co.uk)
  • F 1 F 0 -ATP synthase is a large enzyme complex made up of over 22 subunits. (biomedcentral.com)
  • In each transfer of an electron through the electron transport chain, the electron loses energy, but with some transfers, the energy is stored as potential energy by using it to pump hydrogen ions across the inner mitochondria membrane into the intermembrane space, creating an electrochemical gradient. (opentextbooks.org.hk)
  • As they are passed from one complex to another (there are a total of four), the electrons lose energy, and some of that energy is used to pump hydrogen ions from the mitochondrial matrix into the intermembrane space. (opentextbooks.org.hk)
  • This complex protein acts as a tiny generator, turned by the force of the hydrogen ions diffusing through it, down their electrochemical gradient from the intermembrane space, where there are many mutually repelling hydrogen ions to the matrix, where there are few. (opentextbooks.org.hk)
  • Unlike other low molecular weight messengers that bind to and activate target cellular receptors, NO signaling is mediated by a coordinating complex between NO and transition metals or target cellular proteins, often via S-nitrosylation of cysteine residues. (wikipedia.org)
  • protein Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. (theinfolist.com)
  • The primary function of the mitochondria is the aerobic production of ATP, a process that is reliant on a series of protein complexes that comprise the electron transport chain. (prolekarniky.cz)
  • Reduced placental amino acid transport in response to maternal nutrient restriction in the baboon. (ucdenver.edu)
  • Effect of high altitude on human placental amino acid transport. (ucdenver.edu)
  • Proteins make up the mitochondrial transport chain, and some fatty acids also play a crucial role. (recharge.health)
  • Fatty acids, which are often found in chains as CoA-esters, are first transported across the outer mitochondrial membrane by palmitoyl transferase I, resulting in translocation to the intermembrane space and transformation into an acyl-carnitine form. (biomedcentral.com)
  • The frequency of PSI-Pc interaction is higher when at least one of the partners is in a state ready for electron transfer, and it is lower once the electron is transferred. (icrea.cat)
  • In the last steps of this process transfer of energy-conserving electrons beyond photosystem I (PSI) is performed by a small iron-sulphur protein ferredoxin (Fd). (nature.com)
  • A flavoprotein oxidase complex that contains iron-sulfur centers. (ouhsc.edu)
  • An IRON-containing protein that uses siroheme and 4Fe-4S iron-sulfur centers as prosthetic groups. (lookformedical.com)

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