AnatomyOrganismsChemicals and DrugsAnalytical, Diagnostic and Therapeutic Techniques and EquipmentPhenomena and ProcessesDisciplines and OccupationsInformation Science
UbiquinoneCytochromesCytochrome c GroupCytochrome P-450 Enzyme SystemCytochrome b GroupElectron Transport Complex IIICytochromes cElectron Transport Complex IVElectron TransportOxidation-ReductionCytochromes c1Quinone ReductasesCytochromes b5Antimycin ACytochromes bElectron Transport Complex IOxidoreductasesElectron Transport Chain Complex ProteinsHemeCytochromes a1MitochondriaSpectrophotometryNADH, NADPH OxidoreductasesCytochromes fCytochrome P-450 CYP3ASuccinate Cytochrome c OxidoreductaseCytochrome d GroupQuinonesAcetobacterNADH DehydrogenaseParacoccus denitrificansIron-Sulfur ProteinsElectron Transport Complex IICytochrome P-450 CYP2E1Electron Spin Resonance SpectroscopyCytochrome ReductasesKineticsCytochrome a GroupHydroxyquinolinesMitochondria, HeartCytochrome b6f ComplexCytochromes c2Cytochrome P-450 CYP1A2Molecular Sequence DataSubmitochondrial ParticlesCytochrome P-450 CYP1A1ElectronsEscherichia coliSuccinic AcidCytochrome P-450 CYP2B1Microsomes, LiverRhodobacter sphaeroidesPotentiometryNADAmino Acid SequenceCyanidesCytochrome P-450 CYP2D6CoenzymesMethacrylatesNADPH-Ferrihemoprotein ReductaseCattleMultienzyme ComplexesBinding SitesSuccinatesEscherichia coli ProteinsOxygenNAD(P)H Dehydrogenase (Quinone)Succinate DehydrogenaseProton-Motive ForceSpectrum AnalysisYarrowiaProtonsBenzoquinonesFerricyanidesOxygen ConsumptionRhodobacter capsulatusPotassium CyanideAryl Hydrocarbon HydroxylasesMitochondria, LiverPolyenesHydrogen-Ion ConcentrationMixed Function OxygenasesAcidithiobacillus thiooxidansModels, MolecularMitochondrial ProteinsMutationProtein ConformationSaccharomyces cerevisiaeRotenoneGlucose DehydrogenasesCopperCytochromes aCytochrome-c PeroxidaseCytochromes c6CatalysisPhylogenyHydroxylationAerobiosisCytochromes c'Phenobarbital
NADHSubunitIntermembrane spaceCoenzymeInner mitochonMembraneOxidation of ubiquinolAccept one electronKnown as cytochromeSuccinateProteinsMitochondriaProteinSemiquinoneOxygenComplexesTransfersAcceptorCompoundsBoundFerrous stateReductionRieskeOxidativeCatalyzesRedoxPhysiologicalHemeFerricytochromeAerobic organismsCellsTerminalInhibitionReactionConsistsSequence
NADH6
  • The complexes studied are Complex I (NADH:Ubiquinone oxidoreductase), Complex II (Succinate:ubiquinone oxidoreductase), Complex III (Ubiquinol:cytochrome c oxidoreductase), and Complex IV (Cytochrome c oxidase). (cdc.gov)
  • The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. (affbiotech.cn)
  • They are involved in electron transport in mitochondrial preparations playing an essential role in the oxidation of succinate or NADH via the cytochrome system. (gerli.com)
  • Complex I (NADH:ubiquinone oxidoreductase) is crucial for respiration in many aerobic organisms. (gowebamerica.com)
  • 1], The proposed pathway for electron transport prior to ubiquinone reduction is as follows: NADH - FMN - N3 - N1b - N4 - N5 - N6a - N6b - N2 - Q, where Nx is a labelling convention for iron sulfur clusters. (gowebamerica.com)
  • In mitochondria, it oxidizes NADH from the tricarboxylic acid cycle and β-oxidation, reduces ubiquinone, and transports protons across the inner membrane, contributing to the proton-motive force. (gowebamerica.com)
Subunit2
  • The cytochrome bc 1 complex (also known as ubiquinol-cytochrome c oxidoreductase or complex III) is a multi-subunit dimeric integral membrane protein complex. (slimwithlynne.com)
  • Our data indicate that OCIAD1 is required for maintenance of normal steady state levels of Complex III and the proteolytic processing of the catalytic subunit cytochrome c 1 (CYC1). (biorxiv.org)
Intermembrane space5
  • Overall: 2 x QH2 oxidised to Q 1 x Q reduced to QH2 2 x Cyt c reduced 4 x H+ released into intermembrane space 2 x H+ picked up from matrix The reaction proceeds according to the following steps: Round 1: Cytochrome b binds a ubiquinol and a ubiquinone. (wikipedia.org)
  • The 2Fe/2S center and BL heme each pull an electron off the bound ubiquinol, releasing two protons into the intermembrane space. (wikipedia.org)
  • Ubiquinol-cytochrome c reductase pumps protons into the intermembrane space, creating an electrochemical gradient. (yeastgenome.org)
  • This is achieved by oxidizing ubiquinol (ubihydroquinone) which reacts from the membrane phase, reducing cytochrome c in the intermembrane space, and using the free energy change to transport H+ ions across the membrane from the matrix to the inter membrane space. (yeastgenome.org)
  • The protons released by ubiquinol oxidation are transferred to the intermembrane space. (slimwithlynne.com)
Coenzyme9
  • The coenzyme Q : cytochrome c - oxidoreductase, sometimes called the cytochrome bc1 complex, and at other times complex III, is the third complex in the electron transport chain (EC 1.10.2.2), playing a critical role in biochemical generation of ATP (oxidative phosphorylation). (wikipedia.org)
  • The reaction mechanism for complex III (cytochrome bc1, coenzyme Q: cytochrome C oxidoreductase) is known as the ubiquinone ("Q") cycle. (wikipedia.org)
  • The most common ubiquinone is coenzyme Q that has structural similarity to vitamin K. (drugstorepdfsearch.com)
  • Ubiquinone can carry two hydrogen atoms forming ubiquinol (reduced coenzyme Q) or one hydrogen atom forming semiquinone. (drugstorepdfsearch.com)
  • Reduced coenzyme Q passes the electrons to cytochrome b and releases 2H+ into the mitochondrial matrix The oxidation of ubiquinol involves the successive action of 2 enzymes: a) - Ubiquinol (coenzyme Q) dehydrogenase which transfers electrons to cytochrome c. (drugstorepdfsearch.com)
  • N.B. The mobile components of the electron transport chain include coenzyme Q and cytochrome c. (drugstorepdfsearch.com)
  • Coenzyme Q - ubiquinol cytochrome c reductase Crystal structure of mitochondrial cytochrome bc1 complex bound with ubiquinone. (en-academic.com)
  • Mitochondria contain quinine called "Ubiquinone" (also called "Coenzyme.Q" (or) simply "Q") which is a benzoquinone with a long isoprenoid side chain. (biochemden.com)
  • Thus, coenzyme Q10 is also named ubiquinone (50). (gerli.com)
Inner mitochon1
  • The Cytochromes of type a and b and some of type "C" are integral proteins of the inner mitochondrial membrane. (biochemden.com)
Membrane4
  • Cytochrome c is a water soluble, peripheral membrane protein. (drugstorepdfsearch.com)
  • Aminoacid degradation and urea cycle The cytochrome bc1complex (ubiquinone:cytochrome coxidoreductase) is the central integral membrane protein in the mitochondrial respiratory chain as well as the electron-transfer chains of many respiratory and photosynthetic prokaryotes. (slimwithlynne.com)
  • Citric acid cycle During the electron transfer through the cytochrome bc(1) complex (ubiquinol-cytochrome c oxidoreductase or complex III), protons are translocated across the membrane, and production of superoxide anion radicals (O(2)(*-)) is observed. (slimwithlynne.com)
  • The reaction can be reversed - referred to as aerobic succinate-supported NAD+ reduction by ubiquinol - in the presence of a high membrane potential, but the exact catalytic mechanism remains unknown. (gowebamerica.com)
Oxidation of ubiquinol1
  • The enzyme complex catalyzes the oxidation of ubiquinol to ubiquinone and ferrocytochrome c in the presence of ferricytochrome c. (doctorinternet.com)
Accept one electron1
  • Next, Complex III, also known as cytochrome reductase, transfers electrons from ubiquinone to cytochrome C. Because cytochrome C can only accept one electron at a time, two molecules of cytochrome C are actually needed to unload each ubiquinone molecule from Complex I and II. (pixorize.com)
Known as cytochrome1
  • Afterwards, Complex IV, also known as cytochrome oxidase, then transfers electrons from Cytochrome C to oxygen, producing water as a byproduct. (pixorize.com)
Succinate1
  • Molecular docking analysis for different enzymes involved in aging (collagenase, elastase and hyaluronidase), antioxidant enzymes (superoxide dismutase, glutathione-s-transferase, glutathione peroxidase and catalase) and mitochondrial enzymes (nicotinamide adenine dinucleotide (NAD)+hydrogen (H) dehydrogenase, succinate dehydrogenase, cytochrome c oxidase and adenosine triphosphate synthase) was carried out for epigallocatechin gallate alone (1), withaferin A alone (2), epigallocatechin gallate and withaferin A in combination (3) and a reference molecule. (ijpsonline.com)
Proteins3
  • The bc1 complex contains 11 subunits, 3 respiratory subunits (cytochrome B, cytochrome C1, Rieske protein), 2 core proteins and 6 low-molecular weight proteins. (wikipedia.org)
  • All cytochrome bc1 complexes contain three electron transfer proteins which contain four redox prosthetic groups. (slimwithlynne.com)
  • The cytochromes are proteins with characteristic strong absorption of visible light, due to their iron-containing heme prosthetic groups. (biochemden.com)
Mitochondria2
  • Mitochondria consists of three classes of cytochromes, designated "Cyt.a ,Cyt.b and Cyt.c" distinguished by differences in their light-absorption spectra. (biochemden.com)
  • Cytochrome c oxidase, photo receptors on your mitochondria, capture photons of red and near-infrared light. (truthseekerforum.com)
Protein6
  • Complex III is a multisubunit transmembrane protein encoded by both the mitochondrial (cytochrome b) and the nuclear genomes (all other subunits). (wikipedia.org)
  • The high potential chain, consisting of the iron sulfur protein, cyt c1 and cyt c2, transfers the first electron from quinol to an acceptor (cytochrome oxidase). (yeastgenome.org)
  • Complex III possesses a Fe-S protein like complex I. Mitochondrial cytochrome bc1 complex performs two functions: It is a respiratory multienzyme complex and it recognizes a mitochondrial targeting presequence. (slimwithlynne.com)
  • Hemoglobin During photosynthesis, the cytochrome b6f complex is one step along the chain that transfers electrons from Photosystem II to Phot… Stigmatellin, a Q(P) site inhibitor, inhibits electron transfer from iron-sulfur protein (ISP) to cytochrome c1 in the bc1 complex. (slimwithlynne.com)
  • Cytochrome a and a 3 possess and identical type of iron - porphyrin complex called "Heme.a",but their location to apo-protein are different. (biochemden.com)
  • Complex III (CoQ cytochrome c oxidoreductase) is an essential protein for mitochondrial oxidative phosphorylation. (bertin-bioreagent.com)
Semiquinone2
  • The first ubiquinol (now oxidised to ubiquinone) is released, whilst the semiquinone remains bound. (wikipedia.org)
  • Cytochrome c1 then transfers its electron to cytochrome c, whilst the nearby semiquinone produced from round 1 picks up a second electron from the BH heme, along with two protons from the matrix. (wikipedia.org)
Oxygen3
  • b) - Cytochrome oxidase which transfers electrons from cyt c to oxygen. (drugstorepdfsearch.com)
  • Cytochrome c oxidase (COX), the terminal enzyme of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced cytochrome c to oxygen. (affbiotech.cn)
  • Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. (affbiotech.cn)
Complexes4
  • Gluconeogenesis Design and use of photoactive ruthenium complexes to study electron transfer within cytochrome bc1 and from cytochrome bc1 to cytochrome c. (slimwithlynne.com)
  • There are two cytochrome complexes in the electron transport chain: cytochrome bc1 and cytochrome c oxidase. (slimwithlynne.com)
  • It accepts electrons from complexes I and II in the form of QH2, the reduced form of the electron carrier ubiquinone. (bertin-bioreagent.com)
  • Herein, we demonstrate that cytochrome c (Cyt c ) showed peroxidase activity on IGA as a component of complexes III and IV. (biologists.com)
Transfers3
  • Cytochrome c1 transfers its electron to cytochrome c (not to be confused with cytochrome c1), and the BH Heme transfers its electron to a nearby ubiquinone, resulting in the formation of a ubisemiquinone. (wikipedia.org)
  • Complex I then transfers both electrons to Ubiquinone, forming its high energy form, UQH2. (pixorize.com)
  • Like complex I, complex II transfers both of these electrons to ubiquinone, turning it into the high energy UQH2. (pixorize.com)
Acceptor1
  • This enzyme belongs to the family of oxidoreductases, specifically those acting on diphenols and related substances as donor with a cytochrome as acceptor. (wikipedia.org)
Compounds1
  • Ubiquinones are a group of compounds containing quinone ring but vary according to number of isoprene units at the side chain. (drugstorepdfsearch.com)
Bound1
  • Round 2: A second ubiquinol is bound by cytochrome b. (wikipedia.org)
Ferrous state1
  • ferrous state) during the physiological action of cytochromes, while the iron of haemoglobin remains in the reduced form during its physiological action. (drugstorepdfsearch.com)
Reduction1
  • Cayman's MitoCheck® Complex II/III Activity Assay measures the reduction of excess cytochrome c (550 nm absorbance) as catalyzed by complex III. (bertin-bioreagent.com)
Rieske1
  • It has four cofactors: cytochrome c1, cytochrome b-562, cytochrome b-566, and a 2-Iron ferredoxin of the Rieske type. (wikipedia.org)
Oxidative1
Catalyzes1
  • Ubiquinol-cytochrome-c reductase catalyzes the chemical reaction QH2 + 2 ferricytochrome c ⇌ {\displaystyle \rightleftharpoons } Q + 2 ferrocytochrome c + 2 H+ Thus, the two substrates of this enzyme are quinol (QH2) and ferri- (Fe3+) cytochrome c, whereas its 3 products are quinone (Q), ferro- (Fe2+) cytochrome c, and H+. (wikipedia.org)
Redox2
  • All cytochromes are haemoproteins but they differ in redox potential. (drugstorepdfsearch.com)
  • As funcións redox do ubiquinol na produción de enerxía celular e na protección antioxidante están baseadas na capacidade de intercambiar electróns nun ciclo redox entre as formas ubiquinol (reducida) e a ubiquinona (oxidada). (wikipedia.org)
Physiological1
  • Recent review: 'Biochemical, physiological and medical aspects of ubiquinone function' by Ernster L et al. (gerli.com)
Heme2
  • One electron is transferred to cytochrome c1 from the 2Fe/2S centre, whilst another is transferred from the BL heme to the BH Heme. (wikipedia.org)
  • The heme as prosthetic group to this cytochromes, but not covalently in Cyt.a and Cyt.b types. (biochemden.com)
Ferricytochrome1
  • The systematic name of this enzyme class is ubiquinol:ferricytochrome-c oxidoreductase. (wikipedia.org)
Aerobic organisms1
  • Ubiquinones are present in all aerobic organisms, plants, animals (the name ubiquinone was proposed with reference to their ubiquitous occurrence) and bacteria, but are absent from Gram-positive eubacteria and the archaebacteria. (gerli.com)
Cells1
  • Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. (ecmdb.ca)
Terminal1
  • Cyt.oxidase thus constitute the last carrier in the chain of electron transport and is referred to as the "terminal oxidase4" of the cytochrome chain. (biochemden.com)
Inhibition1
  • Ilicicolin inhibition and binding at center N of the dimeric cytochrome bc1 complex reveal electron transfer and regulatory interactions between monomers Raul Covian and Bernard L. Trumpower J. Biol. (slimwithlynne.com)
Reaction2
Consists2
  • The second electron is transferred to a The cytochrome bc1 consists of cytochrome b, FeS complex, and cytochrome c1. (slimwithlynne.com)
  • The second cytochrome complex c oxidase consists of cytochrome a and cytochrome a3. (slimwithlynne.com)
Sequence1
  • Previous molecular studies, mainly focusing on the sequence of mitochondrial cytochrome b gene, have made significant contributions to understanding the evolutionary history of Camelidae [2], and yet there has not been any significant comparative studies around the evolutionary relationship between Camelini and Lamini. (thetechnoant.info)