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Enzyme Nomenclature
Information on EC 1.10.2.2 - quinol-cytochrome-c reductase
for references in articles please use BRENDA:EC1.10.2.2
Word Map on EC 1.10.2.2
- 1.10.2.2
- antimycin
-
iron-sulfur
-
rieske
- superoxide
- dysfunction
- succinate
- heme
- myxothiazol
- rhodobacter
- sphaeroides
- rotenone
- epr
- stigmatellin
-
mtdna
- capsulatus
-
bioenergetics
- beef
-
supercomplexes
-
submitochondrial
-
midpoint
- semiquinone
-
oxphos
-
chromatophores
-
electron-transfer
- paracoccus
- denitrificans
-
nadh-ubiquinone
- cardiolipin
-
protonmotive
-
presequence
-
succinate-cytochrome
-
cybrids
-
succinate-ubiquinone
-
apocytochrome
- dccd
- gracile
-
flash-induced
-
low-potential
-
high-potential
-
heteroplasmic
- dicyclohexylcarbodiimide
- encephalomyopathy
-
mtdna-encoded
- maltoside
-
interfibrillar
-
extramembrane
-
respirometry
-
energy-transducing
-
salicylhydroxamic
- medicine
- bacteriochlorophyll
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
1.10.2.2
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RECOMMENDED NAME
GeneOntology No.
quinol-cytochrome-c reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
contains cytochromes b-562, b-566 and c1, and a 2-iron ferredoxin. depending on the organism and the physiological conditions, either two or four protons are extruded from the cytoplasmic to the non-cytoplasmic compartment (cf.EC1.6.99.3 NADH2 dehydrogenase)
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-
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quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
substrate binding site Qo structure, conformational changes upon inhibitor binding, overview
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quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
2 reaction mechanism variants, a fully active enzyme mechanism and a half-of-the sites mechanism of ubiquinol oxidation, switching between the two variants may regulate the enzyme, Glu272 and His181 are involved
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quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
binding structure and mode of cytochrome c1 within the enzyme complex and cytochrome c during the catalytic reaction, direct heme-to-heme electron transfer from the enzyme complex cytochrome c1 to cytochrome c, half-of-the sites mechanism
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quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
substrate binding mechanism at the Qo site of the cytochrome bc1 complex
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quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
the Qo-cycle, overview, reaction mechanism involving cytochrome c, Glu295, and His161, electron transfer mechanism and formation of the ES complex involving a binding square, substrate binding mechanism at the Qo site of the cytochrome bc1 complex
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quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
alternating half-of-the-sites mechanism of ubiquinol oxidation, enzyme links electron transfer from ubiquinol to cytochrome c by a protonmotive Q cycle mechanism in which ubiquinol is oxidized at one center in the enzyme, referred to as center P, und ubiquinone is re-reduced at a second center, referred to as center N
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
reaction and substrate binding mechanism, overview, conformational changes at the binding site of inhibitor 5-n-heptyl-6-hydroxy-4,7-dioxobenzothiazole confirm the proton transfer pathway and reveal plasticity at the active site
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quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
alternating half-of-sites mechanism of ubiquinol oxidation
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
current competing models for the two-electron oxidation of quinol QH2 at the cytochrome bc1 complex and related complexes impose distinct requirements for the reaction intermediate, the initial and rate-limiting step in quinol oxidation, both in the biological and biomimetic systems, involves electron and proton transfer, probably via a proton-coupled electron-transfer mechanism, a neutral semiquinone intermediate is formed in the biomimetic system, and oxidation of the QH*/QH2 couple for UQH2-0, but not TMQH2-0, exhibits an unusual and unexpected primary deuterium kinetic isotope effect on its Arrhenius activation energy, DELTA GTS, where DELTA GTS for the protiated form is larger than that for the deuterated form, detailed reaction mechanism, molecular modeling, electrochemical and computational study, overview
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quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
reaction mechanism, kinetic modeling
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quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
reaction mechanism, similar transition states mediate the Q-cycle and superoxide production by the cytochrome bc1 complex
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quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
reaction mechanism, structure-function analysis, overview
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quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
reaction mechanism, structure-function analysis, overview
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quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
reaction mechanism, structure-function analysis, overview
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
reaction mechanism, structure-function analysis, overview
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
reaction mechanism, structure-function analysis, overview
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
reaction mechanism, structure-function analysis, overview
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
reaction mechanism, structure-function analysis, overview
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quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
reaction mechanism of superoxide generation during ubiquinol oxidation by the cytochrome bc1 complex
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quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+
reaction mechanism of superoxide generation during ubiquinol oxidation by the cytochrome bc1 complex
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
-
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redox reaction
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-
-
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reduction
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-
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
quinol:ferricytochrome-c oxidoreductase
The enzyme, often referred to as the cytochrome bc1 complex or complex III, is the third complex in the electron transport chain. It is present in the mitochondria of all aerobic eukaryotes and in the inner membranes of most bacteria. The mammalian enzyme contains cytochromes b-562, b-566 and c1, and a 2-iron ferredoxin. Depending on the organism and physiological conditions, the enzyme extrudes either two or four protons from the cytoplasmic to the non-cytoplasmic compartment (cf. EC 1.6.99.3, NADH dehydrogenase).
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CAS REGISTRY NUMBER
COMMENTARY
9027-03-6
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
derived from Saccharomyces cerevisiae KL14-4A
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-
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395300, 396001, 439942, 439943, 439944, 439945, 439946, 439947, 439948, 439949, 439950, 439952, 439953, 439955, 439956, 439958, 439960, 439961, 439962, 439964, 439966, 439967, 439970, 439975, 439978, 439979, 439980, 439983, 439985, 439986, 439988, 439989, 439990, 439991, 439993, 439995, 440000, 440003, 440005, 440006, 440009, 440012, 440016, 440018, 440020, 440023, 440025, 440026, 440027, 440028, 440029, 440030, 440035, 657683, 658009, 672379, 674163, 685360, 685619, 686076, 724452, 725396
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-
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395300, 396001, 439942, 439945, 439946, 439951, 439955, 439962, 439967, 439969, 439972, 439977, 439987, 439988, 439990, 439992, 439994, 439997, 440000, 440004, 440015, 440017, 440024, 440030
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439946, 439976, 440003, 440010, 440012, 440015, 440019, 440021, 440030, 440036, 685619, 687705, 689387, 724452, 741983
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439963, 440009, 440010, 440012, 440015, 440019, 440030, 440033, 440036, 658194, 724433, 724452, 725396, 725875, 742085
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basonym Rhodopseudomonas spheroides; formerly Rhodopseudomonas sphaeroides
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blue-green mutant; formerly Rhodopseudomonas sphaeroides
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formerly Rhodopseudomonas sphaeroides; wild-type strain NCIB 8253
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439942, 439943, 439945, 439948, 439963, 439972, 439973, 439974, 439984, 439988, 439990, 439997, 440002, 440005, 440006, 440008, 440009, 440011, 440015, 440018, 440023, 440030, 440031, 658160, 658161, 659170, 659238, 659318, 659443, 674433, 674484, 674721, 685360, 685361, 698895, 700002, 724452
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bakers'yeast; commercial baker's yeast Red Star, strain D273-10B/A1
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parental control diploid strain KM91 obtained by crossing the haploid strain 777-3A with the haploid KL14-4A/60
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
malfunction
-
the electron transport from quinol to cytochrome c, catalyzed by the bc1 complex, is accompanied by the production of a small amount of superoxide anions presumably through electron leakage to molecular oxygen, which increases dramatically when the electron transport within the bc1 complex is blocked by specific bc1 inhibitors such as antimycin A or when the electron transport chain becomes over reduced
malfunction
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the electron transport from quinol to cytochrome c, catalyzed by the bc1 complex, is accompanied by the production of a small amount of superoxide anions presumably through electron leakage to molecular oxygen, which increases dramatically when the electron transport within the bc1 complex is blocked by specific bc1 inhibitors such as antimycin A or when the electron transport chain becomes over reduced
malfunction
-
the electron transport from quinol to cytochrome c, catalyzed by the bc1 complex, is accompanied by the production of a small amount of superoxide anions presumably through electron leakage to molecular oxygen, which increases dramatically when the electron transport within the bc1 complex is blocked by specific bc1 inhibitors such as antimycin A or when the electron transport chain becomes over reduced
malfunction
-
the electron transport from quinol to cytochrome c, catalyzed by the bc1 complex, is accompanied by the production of a small amount of superoxide anions presumably through electron leakage to molecular oxygen, which increases dramatically when the electron transport within the bc1 complex is blocked by specific bc1 inhibitors such as antimycin A or when the electron transport chain becomes over reduced
malfunction
-
when the only supernumerary subunit (subunit IV) is deleted from the Rhodobaacter sphaeroides wild-type complex, the resulting three-subunit core complex has only a fraction of the electron transfer activity of the wild-type complex but has about four times the superoxide anions generating activity. When the three-subunit core complex is reconstituted with subunit IV, the electron transfer activity increases, and the O2 -.-generating activity decreases to the same level as those in the wild-type, four-subunit complex
metabolism
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the complex III also exhibits enzyme mitochondrial processing peptidase activity, which is inactive in bovine cells, but can be activated through detergents treatment
metabolism
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the complex III also exhibits enzyme mitochondrial processing peptidase activity
metabolism
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the complex III also exhibits enzyme mitochondrial processing peptidase activity
metabolism
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the complex III also exhibits enzyme mitochondrial processing peptidase activity
metabolism
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the bc1 complex is a functional substituent of CymA in nitrate/nitrite respiration
physiological function
the respiratory cytochrome bc1 complex is a fundamental enzyme in biological energy conversion. It couples electron transfer from ubiquinol to cytochrome c with generation of protonmotive force which fuels ATP synthesis
physiological function
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the cytochrome bc1 complex is an essential energy transduction electron transfer complex in photosynthetic bacteria. This complex catalyzes the electron transfer from ubiquinol to cytochrome c (or c2) with concomitant generation of a proton gradient and membrane potential for ATP synthesis by the ATP synthase complex
physiological function
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respiratory complex III is an electron transport complex in mitochondria, related bc complexes, overview
physiological function
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respiratory complex III is an electron transport complex in mitochondria, related bc complexes, overview
physiological function
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respiratory complex III is an electron transport complex, related bc complexes, overview
physiological function
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respiratory complex III is an electron transport complex, related bc complexes, overview
physiological function
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respiratory complex III is an electron transport complex, related bc complexes, overview
physiological function
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respiratory complex III is an electron transport complex in mitochondria, related bc complexes, overview
physiological function
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respiratory complex III is an electron transport complex in mitochondria, related bc complexes, overview
physiological function
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the bc1 complex, is the enzyme in the respiratory chain of mitochondria responsible for the transfer reducing potential from ubiquinol to cytochrome c coupled to the movement of charge against the electrostatic potential across the mitochondrial inner membrane. The complex is also implicated in the generation of reactive oxygen species under certain conditions and is thus a contributor to cellular oxidative stress
physiological function
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reaction mechanism of superoxide generation by bc1, overview
physiological function
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the overexpression of ubiquinol-cytochrome c reductase core protein 1 can protect H9c2 cardiac cells against simulated ischemia/reperfusion
physiological function
ubiquinol–cytochrome c reductase binding protein induces angiogenesis in vitro and in vivo
physiological function
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the enzyme contributes to the loss-of-cardioprotection model induced by long-term diazoxide treatment and plays a role in delayed cardioprotection
additional information
structural diversity in the cytochrome c1 surface facing the iron-sulfur protein domain indicates low structural constraints on that surface for formation of a productive electron transfer complex. Modelling of the electron transfer complex with membrane-anchored cytochrome c552, the natural substrate
additional information
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the Q cycle mechanism defines two reaction sites: quinol oxidation and quinone reduction. It takes two quinol oxidation cycles to complete. At first, a QH2 moves into the QP site and undergoes oxidation with one electron going to cyt c via the iron-sulfur protein and cyt c1 (high-potential chain), and another ending in the QN via hemes bL and bH (low-potential chain) to form a ubisemiquinone, and releasing its two protons to the psi+ site of the membrane, mechanism of bc1 functions as well as its inactivation by respiratory inhibitors, docking study, overview. Structural organization of complex III is essential for the electron transport chain, interaction with substrates quinol and cytochrome c, lipids, inhibitors and metal ions
additional information
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the Q cycle mechanism defines two reaction sites: quinol oxidation and quinone reduction. It takes two quinol oxidation cycles to complete. At first, a quinol moves into the QP site and undergoes oxidation with one electron going to cytochrome c via the iron-sulfur protein and cyt c1 (high-potential chain), and another ending in the QN via hemes bL and bH (low-potential chain) to form a ubisemiquinone, and releasing its two protons to the psi+ site of the membrane, mechanism of bc1 functions as well as its inactivation by respiratory inhibitors, docking study, overview. Structural organization of complex III is essential for the electron transport chain, interaction with substrates quinol and cytochrome c, lipids, inhibitors and metal ions
additional information
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the Q cycle mechanism defines two reaction sites: quinol oxidation and quinone reduction. It takes two quinol oxidation cycles to complete. At first, a QH2 moves into the QP site and undergoes oxidation with one electron going to cyt c via the iron-sulfur protein and cyt c1 (high-potential chain), and another ending in the QN via hemes bL and bH (low-potential chain) to form a ubisemiquinone, and releasing its two protons to the psi+ site of the membrane, mechanism of bc1 functions as well as its inactivation by respiratory inhibitors, docking study, overview. Structural organization of complex III is essential for the electron transport chain, interaction with substrates quinol and cytochrome c, lipids, inhibitors and metal ions, interaction with substrates quinol and cytochrome c, lipids, inhibitors and metal ions
additional information
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the Q cycle mechanism defines two reaction sites: quinol oxidation and quinone reduction. It takes two quinol oxidation cycles to complete. At first, a QH2 moves into the QP site and undergoes oxidation with one electron going to cyt c via the iron-sulfur protein and cyt c1 (high-potential chain), and another ending in the QN via hemes bL and bH (low-potential chain) to form a ubisemiquinone, and releasing its two protons to the psi+ site of the membrane, mechanism of bc1 functions as well as its inactivation by respiratory inhibitors, docking study, overview. Structural organization of complex III is essential for the electron transport chain, interaction with substrates quinol and cytochrome c, lipids, inhibitors and metal ions
additional information
-
the Q cycle mechanism defines two reaction sites: quinol oxidation and quinone reduction. It takes two quinol oxidation cycles to complete. At first, a QH2 moves into the QP site and undergoes oxidation with one electron going to cyt c via the iron-sulfur protein and cyt c1 (high-potential chain), and another ending in the QN via hemes bL and bH (low-potential chain) to form a ubisemiquinone, and releasing its two protons to the psi+ site of the membrane, mechanism of bc1 functions as well as its inactivation by respiratory inhibitors, docking study, overview. Structural organization of complex III is essential for the electron transport chain, interaction with substrates quinol and cytochrome c, lipids, inhibitors and metal ions
additional information
-
the Q cycle mechanism defines two reaction sites: quinol oxidation and quinone reduction. It takes two quinol oxidation cycles to complete. At first, a quinol moves into the QP site and undergoes oxidation with one electron going to cytochrome c via the iron-sulfur protein and cyt c1 (high-potential chain), and another ending in the QN via hemes bL and bH (low-potential chain) to form a ubisemiquinone, and releasing its two protons to the psi+ site of the membrane, mechanism of bc1 functions as well as its inactivation by respiratory inhibitors, docking study, overview. Structural organization of complex III is essential for the electron transport chain, interaction with substrates quinol and cytochrome c, lipids, inhibitors and metal ions
additional information
-
the Q cycle mechanism defines two reaction sites: quinol oxidation and quinone reduction. It takes two quinol oxidation cycles to complete. At first, a quinol moves into the QP site and undergoes oxidation with one electron going to cytochrome c via the iron-sulfur protein and cyt c1 (high-potential chain), and another ending in the QN via hemes bL and bH (low-potential chain) to form a ubisemiquinone, and releasing its two protons to the psi+ site of the membrane, mechanism of bc1 functions as well as its inactivation by respiratory inhibitors, docking study, overview. Structural organization of complex III is essential for the electron transport chain, interaction with substrates quinol and cytochrome c, lipids, inhibitors and metal ions
additional information
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model of the bc1 complex for mammalian mitochondria incorporating the major redox centers near the Qo- and Qi-site of the enzyme, and including the pH-dependent redox reactions, overview. The model consists of six distinct states characterized by the mobile electron distribution in the enzyme
additional information
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mechanisms of quinone redox species flow in the intracytoplasmic membrane bilayer, overview. The enzyme complex from Phaeospirillum molischianum shows a more random organization and slower reaction center turnover compared to the enzyme complex from Rhodobacter sphaeroides
additional information
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mechanisms of quinone redox species flow in the intracytoplasmic membrane bilayer, overview. The enzyme shows a highly organized arrangement of light harvesting and reaction center complexes and fast reaction center electron transfer turnover. Cytochrome bc1 or ATPase complexes are localized in membrane domains distinct from the flat regions. Modeling of subunit IV into the cytochrome bc1 complex
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,3-dimethoxy-5-methyl-6-(10-bromodecyl)-1,4-benzoquinol + cytochrome c
2,3-dimethoxy-5-methyl-6-(10-bromodecyl)-1,4-benzoquinone + reduced cytochrome c
-
-
-
-
?
2,3-dimethoxy-5-methyl-6-decylbenzoquinol + cytochrome c
2,3-dimethoxy-5-methyl-6-decylbenzoquinone + reduced cytochrome c
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-
-
-
?
2-[(7E,11E,15E,19E,23E,27E,31E,35E)-4-hydroxy-4,8,12,16,20,24,28,32,36,40-decamethyl-7,11,15,19,23,27,31,35,39-hentetracontanonaen-1-yl]-5,6-dimethoxy-3-methyl-1,4-benzenediol + oxidized cytochrome c
2-[(7E,11E,15E,19E,23E,27E,31E,35E)-4-hydroxy-4,8,12,16,20,24,28,32,36,40-decamethylhentetraconta-7,11,15,19,23,27,31,35,39-nonaen-1-yl]-5,6-dimethoxy-3-methylcyclohexa-2,5-diene-1,4-dione + reduced cytochrome c
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ubiquinone-like compound with a hydroxyl-substituted side chain exhibits substrate efficiencies below that of native ubiquinone but significantly higher efficiency than alpha-tocopheryl quinone
-
-
?
cytochrome b561 + ?
?
-
cytochrome b561, reduced upon flash excitation, is re-oxidized slowly even in the absence of antimycin
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-
?
decylubiquinol + 2 ferricytochrome c
decylubiquinone + 2 ferrocytochrome c + 2 H+
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-
-
-
?
dihydroubiquinone + ferricytochrome c
ubiquinone + ferrocytochrome c + 2 H+
-
-
-
?
menaquinol + cytochrome c
menaquinone + reduced cytochrome c
-
-
-
-
?
menaquinol + ferricytochrome c
menaquinone + ferrocytochrome c + H+
-
-
-
-
?
naphthoquinol + ferricytochrome c
naphthoquinone + ferrocytochrome c
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naphthoquinone is the pool quinone of the organism
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?
plastoquinol 1 + cytochrome c
plastoquinone 1 + reduced cytochrome c
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-
-
-
?
plastoquinol 9 + cytochrome c
plastoquinone 9 + reduced cytochrome c
-
-
-
-
?
rhodoquinol-3 + ferricytochrome c
rhodoquinone + ferrocytochrome c
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a substrate-induced wQ-cycle bypass reaction leading to production of superoxide
i.e. 2-amino-5-farnesyl-3-methoxy-6-methyl-1,4-benzoquinone
-
?
tetramethyl-p-benzoquinol + cytochrome c
tetramethyl-p-benzoquinone + reduced cytochrome c
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duroquinol
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-
?
ubiquinol + 2 ferricytochrome c552
ubiquinone + 2 ferrocytochrome c552 + 2 H+
-
-
-
?
ubiquinol + 4-carboxy-2,6-dinitrophenyllysine27-cytochrome c
ubiquinone + ?
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cytochrome c from horse, modified at Lys27
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-
?
ubiquinol + ferricytochrome b-562
ubiquinone + ferrocytochrome b-562
-
-
-
-
?
2-azido-3-methyl-5-methoxy-6-geranyl-1,4-benzoquinone + cytochrome c1
?
-
-
-
-
?
2-azido-3-methyl-5-methoxy-6-geranyl-1,4-benzoquinone + cytochrome c1
?
-
-
-
-
?
2-azido-3-methyl-5-methoxy-6-geranyl-1,4-benzoquinone + cytochrome c1
?
-
-
-
-
?
3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinone + cytochrome c1
?
-
-
-
-
?
3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinone + cytochrome c1
?
-
-
-
-
?
3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinone + cytochrome c1
?
-
-
-
-
?
coenzyme Q1H2 + 2 cytochrome c/ox
coenzyme Q1 + 2 cytochrome c/red + 2 H+
-
-
-
-
?
coenzyme Q1H2 + 2 cytochrome c/ox
coenzyme Q1 + 2 cytochrome c/red + 2 H+
-
-
-
-
?
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
-
-
-
-
-
decyl-ubiquinol + ferricytochrome c
decyl-ubiquinone + ferrocytochrome c
-
-
-
-
?
decyl-ubiquinol + ferricytochrome c
decyl-ubiquinone + ferrocytochrome c
-
-
-
-
r
decyl-ubiquinol + ferricytochrome c
decyl-ubiquinone + ferrocytochrome c
-
anti-cooperative oxidation of ubiquinol, reversible partial reaction
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-
?
decylbenzohydroquinol + ferricytochrome c
decylbenzohydroquinone + ferrocytochrome c + H+
-
-
-
-
?
decylbenzohydroquinol + ferricytochrome c
decylbenzohydroquinone + ferrocytochrome c + H+
-
-
-
-
?
decylplastoquinol + cytochrome c
decylplastoquinone + reduced cytochrome c
-
-
-
-
?
decylplastoquinol + cytochrome c
decylplastoquinone + reduced cytochrome c
-
-
-
-
?
decylubiquinol + ferricytochrome c
decylubiquinone + ferrocytochrome c
-
-
-
-
?
decylubiquinol + ferricytochrome c
decylubiquinone + ferrocytochrome c
-
horse heart cytochrome c, half of the center N sites was insensitive to decylubiquinol
-
-
?
nonylubiquinol + cytochrome c
nonylubiquinone + reduced cytochrome c
-
-
-
-
?
plastohydroquinol + cytochrome c
plastohydroquinone + reduced cytochrome c
-
-
-
-
?
plastohydroquinol + cytochrome c
plastohydroquinone + reduced cytochrome c
-
-
-
-
?
QH2 + ferricytochrome c
Q + ferrocytochrome c
-
enzyme catalyzes the electron transfer from a quinol molecule to cytochrome c, and concomitantly translocates protons across membranes for ATP synthesis and various cellular processes
-
-
?
QH2 + ferricytochrome c
Q + ferrocytochrome c
-
binding interaction of ubiquinone with cytochrome b, overview
-
-
?
QH2 + ferricytochrome c
Q + ferrocytochrome c
-
proton-coupled electron transfer at the Qo-site of the bc1 complex controls the rate of ubihydroquinone oxidation
-
-
?
QH2 + ferricytochrome c
Q + ferrocytochrome c
-
rate-limiting is the transfer of the first electron from ubiquinol to the [2Fe-2S] cluster of the Rieske iron-sulfur-protein at the Qo-side, reaction energy profile
-
-
?
QH2 + ferricytochrome c
Q + ferrocytochrome c
-
electron transfer between yeast cytochrome bc1 complex and cytochrome c is coupled to proton transport across the inner mitochondrial membrane delivering a membrane potential, enzyme complex is important in cell respiration and photosynthesis
-
-
?
QH2 + ferricytochrome c
Q + ferrocytochrome c
-
enzyme complex is essentially involved in the mitochondrial respiratory electron transfer chain
-
-
?
QH2 + ferricytochrome c
Q + ferrocytochrome c
-
ubiquinol oxidation is part of the protonmotive Q cycle mechanism, overview, half-of-the sites mechanism with reciprocal control between high potential and low potential redox components involved in ubiquinol oxidation
-
-
?
QH2 + ferricytochrome c
Q + ferrocytochrome c
-
activity is highest near physiological ionic strength and decreases at higher concentrations
-
-
?
QH2 + ferricytochrome c
Q + ferrocytochrome c
-
anti-cooperative oxidation of ubiquinol, reversible partial reaction
-
-
?
QH2 + ferricytochrome c
Q + ferrocytochrome c
-
ubiquinol binds to the specific binding pocket of the cytochrome bc1 complex
-
-
?
quinol + 2 ferricytochrome c
quinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
quinol + ferricytochrome c
quinone + ferrocytochrome c + H+
-
-
-
-
?
ubideuteroquinol + cytochrome c
ubideuteroquinone + reduced cytochrome c
-
-
-
-
?
ubideuteroquinol + cytochrome c
ubideuteroquinone + reduced cytochrome c
-
-
-
-
?
ubihydroquinol + cytochrome c
ubihydroquinone + reduced cytochrome c
-
-
-
-
?
ubiquinol + 2 ferricyanide
ubiquinone + 2 ferrocyanide + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
interaction with ubiquinone at the QN site, overview
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced. Key step in the Q-cycle mechanism is the separation of the two electrons of the substrate quinol at the QP site
interaction with ubiquinone at the QN site, overview
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced. Key step in the Q-cycle mechanism is the separation of the two electrons of the substrate quinol at the QP site
interaction with ubiquinone at the QN site, overview
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced
interaction with ubiquinone at the QN site, overview
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced
interaction with ubiquinone at the QN site, overview
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced
interaction with ubiquinone at the QN site, overview
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced. Key step in the Q-cycle mechanism is the separation of the two electrons of the substrate quinol at the QP site
interaction with ubiquinone at the QN site, overview
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced. Key step in the Q-cycle mechanism is the separation of the two electrons of the substrate quinol at the QP site
interaction with ubiquinone at the QN site, overview
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
-
-
395300, 396001, 439942, 439943, 439944, 439945, 439946, 439947, 439948, 439949, 439950, 439952, 439953, 439955, 439956, 439958, 439960, 439961, 439962, 439964, 439966, 439967, 439970, 439975, 439978, 439979, 439980, 439983, 439985, 439986, 439988, 439989, 439990, 439991, 439993, 439995, 440000, 440003, 440005, 440006, 440009, 440012, 440016, 440018, 440020, 440023, 440025, 440026, 440027, 440028, 440029, 440030, 440035, 685360
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
-
-
395300, 396001, 439942, 439945, 439946, 439951, 439954, 439955, 439962, 439967, 439969, 439972, 439977, 439987, 439988, 439990, 439992, 439994, 439997, 440000, 440004, 440015, 440017, 440024, 440030
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
-
-
439946, 439976, 439998, 439999, 440003, 440010, 440012, 440015, 440019, 440021, 440022, 440030, 440036, 689387
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
-
under physiological conditions, the dimeric cytochrome bc1 complex is suggested to be continually primed by prompt oxidation of membrane ubiquinol via center N yielding a bound semiquinone in this center and a reduced, high-potential heme b in the other monomer of the enzyme. Then the oxidation of each ubiquinol molecule in center P is followed by ubiquinol formation in center N, proton translocation and generation of membrane voltage
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
-
-
395300, 439946, 439963, 439965, 439971, 439976, 439977, 439979, 439981, 439988, 439995, 440000, 440009, 440010, 440012, 440015, 440016, 440019, 440030, 440032, 440033, 440036
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
-
-
395300, 439942, 439943, 439945, 439948, 439949, 439950, 439963, 439966, 439972, 439973, 439974, 439984, 439988, 439990, 439992, 439997, 440002, 440005, 440006, 440008, 440009, 440011, 440014, 440015, 440017, 440018, 440021, 440023, 440026, 440030, 440031, 685360
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
-
algal cytochrome c
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
-
-
-
-
?
ubiquinol + cytochrome c
ubiquinone + reduced cytochrome c
-
-
-
-
?
ubiquinol + cytochrome c2
ubiquinone + reduced cytochrome c2
-
-
-
-
?
ubiquinol + cytochrome c2
ubiquinone + reduced cytochrome c2
-
-
-
-
?
ubiquinol + ferricytochrome b-561
ubiquinone + ferrocytochrome b-561
-
-
-
-
?
ubiquinol + ferricytochrome b-561
ubiquinone + ferrocytochrome b-561
-
-
-
-
?
ubiquinol + ferricytochrome c
ubiquinone + ferrocytochrome c
-
-
-
-
?
ubiquinol + ferricytochrome c
ubiquinone + ferrocytochrome c
-
the cytochrome bc1 complex resides in the inner membrane of mitochondria and transfers electrons from ubiquinol to cytochrome c, this electron transfer is coupled to the translocation of protons across the membrane by the protonmotive Q cycle mechanism, this mechanism topographically separates reduction of quinone and reoxidation of quinol at sites on opposite sites of the membrane, referred to as center N, Qn site, and center P, Qp site, respectively
-
-
?
ubiquinol + ferricytochrome c
ubiquinone + ferrocytochrome c + H+
-
-
-
-
?
ubiquinol + ferricytochrome c
ubiquinone + ferrocytochrome c + H+
-
-
-
-
?
ubiquinol + ferricytochrome c
ubiquinone + ferrocytochrome c + H+
-
-
-
-
?
ubiquinol + ferricytochrome c
ubiquinone + ferrocytochrome c + H+
-
-
-
-
?
ubiquinol + horse heart cytochrome c
?
-
-
-
-
?
ubiquinol 10 + cytochrome c
ubiquinone 10 + reduced cytochrome c
-
-
-
-
-
ubiquinol 10 + cytochrome c
ubiquinone 10 + reduced cytochrome c
-
-
-
-
-
ubiquinol 10 + cytochrome c
ubiquinone 10 + reduced cytochrome c
-
-
-
-
-
ubiquinol 2 + cytochrome c
ubiquinone 2 + reduced cytochrome c
-
-
-
-
?
ubiquinol 2 + cytochrome c
ubiquinone 2 + reduced cytochrome c
-
-
-
-
?
ubiquinol 2 + cytochrome c
ubiquinone 2 + reduced cytochrome c
-
-
-
-
?
ubiquinol 2 + cytochrome c
ubiquinone 2 + reduced cytochrome c
-
-
-
-
?
ubiquinol 4 + cytochrome c
ubiquinone 4 + reduced cytochrome c
-
-
-
-
?
ubiquinol 4 + cytochrome c
ubiquinone 4 + reduced cytochrome c
-
-
-
-
?
ubiquinol 9 + cytochrome c
ubiquinone 9 + reduced cytochrome c
-
-
-
-
?
ubiquinol 9 + cytochrome c
ubiquinone 9 + reduced cytochrome c
-
-
-
-
-
ubiquinol 9 + cytochrome c
ubiquinone 9 + reduced cytochrome c
-
-
-
-
-
ubiquinol-1 + cytochrome c
ubiquinone-1 + reduced cytochrome c
-
-
-
-
?
ubiquinol-1 + cytochrome c
ubiquinone-1 + reduced cytochrome c
-
-
-
-
?
ubiquinol-1 + cytochrome c
ubiquinone-1 + reduced cytochrome c
-
-
-
-
?
ubiquinol-1 + cytochrome c
ubiquinone-1 + reduced cytochrome c
-
-
-
-
?
ubiquinol-2 + ferricytochrome c
ubiquinone-2 + ferrocytochrome c
-
the cytochrome bc1 complex is the central segment of the respiratory chain in mitochondria
-
-
?
ubiquinol-2 + ferricytochrome c
ubiquinone-2 + ferrocytochrome c
-
substrate of chain length C5 to C10, ubiquinol binds transiently at the Qo site, only when both heme bL and the iron sulfur cluster are in the oxidized form, where it is oxidized
-
-
?
additional information
?
-
-
enzyme is part of the Knallgas reaction pathway
-
-
-
additional information
?
-
-
dihydroubiquinone-1 is not a suitable substrate, as it reacts nonenzymically with cytochrome c at a rapid rate
-
-
-
additional information
?
-
-
enzyme is a central component of cellular energy conservation machinery
-
-
-
additional information
?
-
-
the enzyme is a component of the multienzyme complex III
-
-
-
additional information
?
-
-
the cyt bc1 complex uses ubiquinol, but not plastoquinol, as a substrate, usage of a biomimetic oxidant, excited-state Ru(2,2'-dipyridyl)2(2-(2-pyridyl)benzimidazolate)+ in an aprotic medium to probe the oxidation of the ubiquinol analogue, 2,3-dimethoxy-5-methyl-1,4-benzoquinol, i.e. UQH2-0, and the plastoquinol analogue, trimethyl-1,4-benzoquinol, i.e. TMQH2-0, using time-resolved and steady-state spectroscopic techniques, comparison of isotope-dependent activation properties in the native and synthetic systems as well as analysis of the time-resolved direct-detection electron paramagnetic resonance signals in the synthetic system, overview
-
-
-
additional information
?
-
-
reaction mechanism of superoxide generation by bc1, overview. Maximum superoxide anions generation activity is observed when the complex is inhibited by antimycin A or inactivated by heat treatment or proteinase K digestion. The protein subunits, at least those surrounding the QP pocket, may play a role either in preventing the release of superoxide. from its production site to aqueous environments or in preventing O2 from getting access to the hydrophobic QP pocket and might not directly participate in superoxide production
-
-
-
additional information
?
-
-
activity of enzyme complex III of the mitochondrial electron transport chain is essential for early heart muscle cell differentiation
-
-
-
additional information
?
-
-
the enzyme is a component of the multienzyme complex III
-
-
-
additional information
?
-
-
protonation reactions coupled to quinone binding, binding of 2.3-2.6 quinones per enzyme monomer at the Qo side, conformational changes
-
-
-
additional information
?
-
-
enzyme complex III is part of the mitochondrial membrane electron transport chain
-
-
-
additional information
?
-
-
photosynthetic growth of purple non-sulfur bacteria such as Rhodobacter capsulatus depends on the cyclic electron transfer between the ubihydroquinone:cytochrome c oxidoreductases (cyt bc1 complex), and the photochemical reaction centers, mediated by either a membrane-bound or a freely diffusible electron carrier
-
-
-
additional information
?
-
-
reaction mechanism of superoxide generation by bc1, overview
-
-
-
additional information
?
-
-
electron transfer takes place between the 2 cytochrome b subunits
-
-
-
additional information
?
-
-
the physiological impact of a mixed Q pool in RQ-producing organisms, overview
-
-
-
additional information
?
-
-
model of half-of-the-sites activity in the dimeric cytochrome bc1 complex, overview
-
-
-
additional information
?
-
-
substrate synthesis and substrate specificity, overview
-
-
-
additional information
?
-
-
almost inert towards mammalian cytochrome c
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
naphthoquinol + ferricytochrome c
naphthoquinone + ferrocytochrome c
-
-
naphthoquinone is the pool quinone of the organism
-
?
ubiquinol + 2 ferricytochrome c552
ubiquinone + 2 ferrocytochrome c552 + 2 H+
P05418
-
-
-
?
ubiquinol + ferricytochrome c
ubiquinone + ferrocytochrome c + H+
-
-
-
-
?
ubiquinol-2 + ferricytochrome c
ubiquinone-2 + ferrocytochrome c
-
the cytochrome bc1 complex is the central segment of the respiratory chain in mitochondria
-
-
?
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
-
-
-
-
-
coenzyme ubiquinone 10 + cytochrome c
ubiquinol-50 + cytochrome c
-
-
-
-
-
QH2 + ferricytochrome c
Q + ferrocytochrome c
-
enzyme catalyzes the electron transfer from a quinol molecule to cytochrome c, and concomitantly translocates protons across membranes for ATP synthesis and various cellular processes
-
-
?
QH2 + ferricytochrome c
Q + ferrocytochrome c
-
proton-coupled electron transfer at the Qo-site of the bc1 complex controls the rate of ubihydroquinone oxidation
-
-
?
QH2 + ferricytochrome c
Q + ferrocytochrome c
-
electron transfer between yeast cytochrome bc1 complex and cytochrome c is coupled to proton transport across the inner mitochondrial membrane delivering a membrane potential, enzyme complex is important in cell respiration and photosynthesis
-
-
?
QH2 + ferricytochrome c
Q + ferrocytochrome c
-
enzyme complex is essentially involved in the mitochondrial respiratory electron transfer chain
-
-
?
QH2 + ferricytochrome c
Q + ferrocytochrome c
-
ubiquinol oxidation is part of the protonmotive Q cycle mechanism, overview, half-of-the sites mechanism with reciprocal control between high potential and low potential redox components involved in ubiquinol oxidation
-
-
?
quinol + 2 ferricytochrome c
quinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
quinol + ferricytochrome c
quinone + ferrocytochrome c + H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced. Key step in the Q-cycle mechanism is the separation of the two electrons of the substrate quinol at the QP site
interaction with ubiquinone at the QN site, overview
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced. Key step in the Q-cycle mechanism is the separation of the two electrons of the substrate quinol at the QP site
interaction with ubiquinone at the QN site, overview
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
P05418
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced
interaction with ubiquinone at the QN site, overview
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced
interaction with ubiquinone at the QN site, overview
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced
interaction with ubiquinone at the QN site, overview
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced. Key step in the Q-cycle mechanism is the separation of the two electrons of the substrate quinol at the QP site
interaction with ubiquinone at the QN site, overview
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced. Key step in the Q-cycle mechanism is the separation of the two electrons of the substrate quinol at the QP site
interaction with ubiquinone at the QN site, overview
-
?
ubiquinol + ferricytochrome c
ubiquinone + ferrocytochrome c
-
-
-
-
?
ubiquinol + ferricytochrome c
ubiquinone + ferrocytochrome c
-
the cytochrome bc1 complex resides in the inner membrane of mitochondria and transfers electrons from ubiquinol to cytochrome c, this electron transfer is coupled to the translocation of protons across the membrane by the protonmotive Q cycle mechanism, this mechanism topographically separates reduction of quinone and reoxidation of quinol at sites on opposite sites of the membrane, referred to as center N, Qn site, and center P, Qp site, respectively
-
-
?
additional information
?
-
-
enzyme is part of the Knallgas reaction pathway
-
-
-
additional information
?
-
-
enzyme is a central component of cellular energy conservation machinery
-
-
-
additional information
?
-
-
the enzyme is a component of the multienzyme complex III
-
-
-
additional information
?
-
-
reaction mechanism of superoxide generation by bc1, overview. Maximum superoxide anions generation activity is observed when the complex is inhibited by antimycin A or inactivated by heat treatment or proteinase K digestion. The protein subunits, at least those surrounding the QP pocket, may play a role either in preventing the release of superoxide. from its production site to aqueous environments or in preventing O2 from getting access to the hydrophobic QP pocket and might not directly participate in superoxide production
-
-
-
additional information
?
-
-
activity of enzyme complex III of the mitochondrial electron transport chain is essential for early heart muscle cell differentiation
-
-
-
additional information
?
-
-
the enzyme is a component of the multienzyme complex III
-
-
-
additional information
?
-
-
enzyme complex III is part of the mitochondrial membrane electron transport chain
-
-
-
additional information
?
-
-
photosynthetic growth of purple non-sulfur bacteria such as Rhodobacter capsulatus depends on the cyclic electron transfer between the ubihydroquinone:cytochrome c oxidoreductases (cyt bc1 complex), and the photochemical reaction centers, mediated by either a membrane-bound or a freely diffusible electron carrier
-
-
-
additional information
?
-
-
reaction mechanism of superoxide generation by bc1, overview
-
-
-
additional information
?
-
-
the physiological impact of a mixed Q pool in RQ-producing organisms, overview
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
all the bc1 complexes contain three redox prosthetic group bearing subunits (cytochrome b, cytochrome c1, and Rieske iron-sulfur protein) with varying numbers (ranging from 0 to 8) of non-redox prosthetic group bearing (supernumerary) subunits
-
cytochrome b
two cyt b subunits form the hydrophobic core of the complex, overview
-
cytochrome b
-
the cytochrome b subunit contains two b-type hemes, bL and bH
-
cytochrome c1
the domain houses the cofactor heme c1 which is bound by the characteristic CXXCH motif with residues Cys82, Cys85, His86 (Cys245cyt c1, Cys248cyt c1, His249cyt c1) and with Met210 (Met373cyt c1) as the sixth heme ligand, structure of the subunit, overview
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Iron
Iron-sulfur cluster
Sr2+
additional information
Fe2+
-
iron-sulfur protein, capturing and binding, performs a structural switch involved in the reaction mechanism, overview
Fe2+
-
iron-sulfur protein, capturing and binding, performs a structural switch involved in the reaction mechanism, overview
Fe2+
Rieske protein, the subunit iron-sulfur protein is made up of three domains. The membrane anchor is an N-terminal TMH (Asp17-Gln41) with pronounced tilt which brings the catalytic domain in contact with the second monomer providing the structural basis for the functional dimer. The catalytic domain is interconnected with the TMH by the hinge region, Met42-Leu51, which harbours the ADV motif, Ala46-Val48
Fe2+
-
iron-sulfur protein, capturing and binding, performs a structural switch involved in the reaction mechanism, overview
Fe2+
-
iron-sulfur protein, capturing and binding, performs a structural switch involved in the reaction mechanism, overview
Fe2+
-
Rieske iron-sulfur protein possessing a high potential [2Fe-2S] cluster
Fe2+
-
iron-sulfur protein, capturing and binding, performs a structural switch involved in the reaction mechanism, overview
Fe2+
-
iron-sulfur protein, capturing and binding, performs a structural switch involved in the reaction mechanism, overview
Fe2+
-
iron-sulfur protein, capturing and binding, performs a structural switch involved in the reaction mechanism, overview
Iron
-
enzyme contains 2 cytochromes with heme groups, enzyme contains a Rieske [2Fe-2S] cluster, structure analysis of the Rieske ISP and of soluble fragments thereof
Iron
-
enzyme complex contains a Rieske Fe-S protein which controls the rate of reduction of the cytochrome b
Iron
-
enzyme contains a Rieske [2Fe-2S] cluster required for activity
Iron
-
enzyme complex contains an iron-sulfur protein, and heme groups in the cytochrome molecules
Sr2+
-
crystals of Rsbc1 grown in the presence of strontium ions reveal several Sr2+ binding sites. One site that is not present in mitochondrial bc1 but appears to be conserved in photosynthetic bacteria is on cyt c1
additional information
-
no Zn2+ in the native enzyme structure. No Sr2+ binding sites in mitochondrial bc1
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,3,4-trimethoxy-5-decyl-6-methyl-phenol
-
competitive inhibitor, binds stably to the Qo site of the cytochrome bc1 complex, binding structure, inhibitory potency depends on the chain length of the ubiquinol substrate and is higher with Q0C5 than with Q0C10, inhibition is pH-dependent
2,3,4-trimethoxy-5-methyl-6-decyl-phenol
-
competitive inhibitor, binds stably to the Qo site of the cytochrome bc1 complex, binding structure, inhibition is pH-dependent
2-nonyl-4-hydroxyquinoline N-oxide
-
binding interaction with cytochrome b, and structural changes of the latter upon binding of inhibitor at the Qi side, overview
3-[(2,4-diethylphenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
-
-
3-[(2,6-diethylphenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
-
-
3-[(2-bromo-4-fluorophenyl)amino]-5-(6-bromopyridin-3-yl)-5-methyl-1,3-oxazolidine-2,4-dione
-
-
3-[(2-bromo-4-fluorophenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
-
-
3-[(4-bromophenyl)amino]-5-(6-bromopyridin-3-yl)-5-methyl-1,3-oxazolidine-2,4-dione
-
-
3-[(4-bromophenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
-
-
3-[(4-chlorophenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
-
-
3-[(4-methoxyphenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
-
-
3-[[5-methyl-2,4-dioxo-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidin-3-yl]amino]benzoic acid
-
-
4-[[5-(6-bromopyridin-3-yl)-5-methyl-2,4-dioxo-1,3-oxazolidin-3-yl]amino]benzonitrile
-
-
4-[[5-methyl-2,4-dioxo-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidin-3-yl]amino]benzoic acid
-
-
4-[[5-methyl-2,4-dioxo-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidin-3-yl]amino]benzonitrile
-
-
5-(6-bromopyridin-3-yl)-3-[(2,4-diethylphenyl)amino]-5-methyl-1,3-oxazolidine-2,4-dione
-
-
5-(6-bromopyridin-3-yl)-3-[(2,6-diethylphenyl)amino]-5-methyl-1,3-oxazolidine-2,4-dione
-
-
5-(6-bromopyridin-3-yl)-3-[(4-chlorophenyl)amino]-5-methyl-1,3-oxazolidine-2,4-dione
-
-
5-(6-bromopyridin-3-yl)-3-[(4-methoxyphenyl)amino]-5-methyl-1,3-oxazolidine-2,4-dione
-
-
5-(6-bromopyridin-3-yl)-5-methyl-3-[(2-methyl-4-nitrophenyl)amino]-1,3-oxazolidine-2,4-dione
-
-
5-(6-bromopyridin-3-yl)-5-methyl-3-[(4-methylphenyl)amino]-1,3-oxazolidine-2,4-dione
-
-
5-(6-bromopyridin-3-yl)-5-methyl-3-[[4-(trifluoromethyl)phenyl]amino]-1,3-oxazolidine-2,4-dione
-
-
5-methyl-3-[(4-methylphenyl)amino]-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
-
-
5-methyl-5-(4-phenoxyphenyl)-3-(phenylamino)-2,4-oxazolidinedione
-
i.e. famoxadone, noncompetitive inhibitor with respect to the substrate of cytochrome c, but is a competitive inhibitor with respect to the substrate of decylubiquinol
5-methyl-5-(6-phenoxypyridin-3-yl)-3-[[4-(trifluoromethyl)phenyl]amino]-1,3-oxazolidine-2,4-dione
-
-
6-((1-hydroxynaphthalen-4-ylamino)dioxysulfone)-2H-naphtho[1,8-bc]thiophen-2-one
-
-
-
antimycin A1
-
binding interaction with cytochrome b, and structural changes of the latter upon binding of inhibitor at the Qi side, overview
azoxystrobin
-
noncompetitive inhibitor with respect to the substrate of cytochrome c, but is a competitive inhibitor with respect to the substrate of decylubiquinol
n-alkyl-6-hydroxy-4,7-dioxobenzothiazole
-
length of side chain 7-15 carbon atoms
2,5-dibromo-6-methyl-3-isopropyl-1,4-benzoquinone
-
DBMIB, most potent inhibitor
2,5-dibromo-6-methyl-3-isopropyl-1,4-benzoquinone
-
DBMIB, most potent inhibitor
2,5-dibromo-6-methyl-3-isopropyl-1,4-benzoquinone
-
DBMIB, most potent inhibitor
5-n-heptyl-6-hydroxy-4,7-dioxobenzothiazole
-
competitive, structure of the enzyme with the hydroxyquinone anion Qo site inhibitor bound, binding mechanism
Antimycin
-
-
Antimycin
-
with one equivalent of antimycin more than 90% of activity is inhibited
Antimycin
-
inhibits ubiquinone reduction at the Qc site of the enzyme
Antimycin
-
due to half-of-sites mechanism of the enzyme, 1 inhibitor molecule per enzyme complex dimer is sufficient for inhibition, center N inhibitor
Antimycin
-
center N inhibitor, acts at the Qn site of the bc1 complex, binding mode differing from ilicicolin
Antimycin
-
with one equivalent of antimycin more than 90% of activity is inhibited
antimycin A
-
inhibits the enzyme complex and blocks the cell differentiation, inhibition mechanism
antimycin A
-
-
antimycin A
-
binds to center N sites, irreversible conformational change occurrs upon SQ formation in the active monomer
atovaquone
-
an anti-malarial agent that specifically targets the cytochrome bc1 complex and inhibits parasite respiration in vivo, mutants Y279S, Y279C, and L282V are resistant to the inhibition, modeling the variations in cytochrome b structure and atovaquone binding with the mutated bc1 complexes
famoxadone
-
reversible, tight-binding, non-competitive inhibitor, proximal Qo-site inhibitor, binding and inhibition mechanism, overview
ilicicolin H
-
center N inhibitor, the antibiotic substance acts at the Qn site of the bc1 complex, isolated from the fungus Cylindrocladium iliciola strain MFC-870, binding mode differing from antimycin, effects on kinetics
ilicicolin H
-
a Qn site inhibitor, a 5-(4-hydroxyphenyl)-alpha-pyridone with a decalin ring system, wild-type enzyme IC50: 12 nM
ilicicolin H
-
potent inhibitor. S20T, Q22E, Q22T and L198F mutations in the yeast bc1 complex conferr resistance to ilicicolin H
menaquinol
-
inhibitory ubiquinol analogue binds to the ubiquinol oxidation site in the bc1 complex, 1 molecule bound per enzyme dimer causes full inhibition, binding is anti-cooperative
methoxyacrylate stilbene
-
reversible, tight-binding, mixed-competitive inhibitor, proximal Qo-site inhibitor, binding and inhibition mechanism, overview
methoxyacrylate stilbene
-
inhibitory ubiquinol analogue binds to the ubiquinol oxidation site in the bc1 complex, 1 molecule bound per enzyme dimer causes full inhibition, binding is anti-cooperative
methoxyacrylate stilbene
-
inhibitory analogue of ubiquinol act anti-cooperatively on the enzyme, inhibitor blocks the enzymes center P with a stoichiometry of 0.5 per enzyme molecule
Myxothiazol
-
inhibits ubiquinone reduction at the Qz site of the enzyme
Myxothiazol
-
inhibitory analogue of ubiquinol act anti-cooperatively on the enzyme, inhibitor blocks the enzymes center P with a stoichiometry of 0.5 per enzyme molecule
Stigmatellin
species-specific binding of the inhibitor, binding structure and mechanism, overview
Stigmatellin
-
binding involves conformational change of Glu295, molecular dynamic simulation, mutants E295G, E295D, and E295Q are resistant to inhibition
Stigmatellin
-
inhibitory ubiquinol analogue binds to the ubiquinol oxidation site in the bc1 complex, 1 molecule bound per enzyme dimer causes full inhibition, binding is anti-cooperative
Stigmatellin
-
inhibitory analogue of ubiquinol act anti-cooperatively on the enzyme, inhibitor blocks the enzymes center P with a stoichiometry of 0.5 per enzyme molecule
undecyl-hydroxy-dioxobenzoxythiazole
-
UHDBT, efficient universal inhibitor
undecyl-hydroxy-dioxobenzoxythiazole
-
UHDBT, efficient universal inhibitor
undecyl-hydroxy-dioxobenzoxythiazole
-
UHDBT, efficient universal inhibitor
Zn2+
-
local structure of Zn2+ bound stoichiometrically to noncrystallized cyt bc1 complex. Ligands are His121, His267, Lys269, and Asp254
Zn2+
-
local structure of Zn2+ bound stoichiometrically to noncrystallized cyt bc1 complex. Ligands are His121, His268, Lys270, and Asp253
Zn2+
-
crystalline chicken bc1 complex specifically binds Zn2+ ions at two identical sites or one per monomer in the dimer. Zinc binding occurs close to the QP site and is likely to be the reason for the inhibitory effect on the activity of bc1 observable during zinc titration. The Zn2+ ion binds to a hydrophilic area between cytochromes b and c1 and is coordinated by GgH212 of cyt c1, GgH268, GgD253, and GgE255 of cyt b, and might interfere with the egress of protons from the QP site to the intermembrane aqueous medium. No Zn2+ is bound at the zinc binding motif of the putative MPP active site of core-1 and core-2 for chicken bc1 after prolonged soaking
Zn2+
-
local structure of Zn2+ bound stoichiometrically to noncrystallized cyt bc1 complex. Zinc binds five to six N or O atoms
additional information
-
structure determination of the inhibitor binding site Qi, located near the matrix side of the membrane bilayer
-
additional information
-
insensitive to N',N'-dicyclohexylcarbodiimide
-
additional information
-
inhibitor binding at the quinone reduction Qi side or the quinol oxidation Qo side
-
additional information
-
resistant to classical inhibitors like myxothiazol, stigmatellin and antimycin
-
additional information
-
the rate of cytochrome c1 is highly reduced in absence of ubiquinone
-
additional information
-
inhibition and inhibitor binding mechanisms
-
additional information
-
design, synthesis, and kinetic evaluation of 3-(phenylamino)oxazolidine-2,4-diones as potent cytochrome bc1 complex inhibitors, overview
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
O2
-
molecular oxygen increases the activity of Rhodobacter sphaeroides bc1 complex up to 82%, depending on the intactness of the complex. Since oxygen enhances the reduction rate of heme bL, but shows no effect on the reduction rate of heme bH, the effect of oxygen in the electron transfer sequence of the cytochrome bc1 complex is at the step of heme bL reduction during bifurcated oxidation of ubiquinol. Free superoxide anion is not involved in the oxygen enhanced reduction of heme bL
additional information
-
detergents stimulate superoxide anion production, overview
-
additional information
-
detergents stimulates superoxide anion production, overview
-
additional information
-
cardiolipin is essential for the function of bc1. Two phosphatidylethanolamines, one phosphatidylcholine, one phosphatidyinositol, and one cardiolipin are bound to the enzyme cmplex
-
additional information
-
cardiolipin is essential for the function of bc1
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0046
coenzyme Q1H2
-
estimated value of KM, descriptive of rotenone-dicumarol-insensitive CoQ1 reduction and CoQ1H2 oxidation on passage through normoxic lungs
additional information
additional information
-
kinetics of the enzyme complex activity dependent on pH and on the Rieske iron-sulfur protein midpoint potential, thermodynamic profile of the Q cycle
-
additional information
additional information
-
reaction kinetics of oxidation and electron transfer, complex formation kinetics, pH-dependence
-
additional information
additional information
-
pre-steady-state kinetics
-
additional information
additional information
-
pre-steady-state and steady-state kinetics, kinetic modeling, kinetics of interactions between monomers of the dimeric enzyme complex, pH 7.0 and pH 8.8
-
additional information
additional information
-
pre-steady-state kinetics of cytochrome b reduction
-
additional information
additional information
-
kinetics, the extent of cyt b reduction in the steady state, measurement of the reduction state of both cyt b hemes during steady state turnover, thermodynamic characterization of ubiquinol-3 and rhodoquinol-3, overview
-
additional information
additional information
-
pre-steady-state reduction of cyt b and cyt c1, steady-state kinetics and Arrhenius activation energies of wild-type and mutant enzymes, overview
-
additional information
additional information
-
pre-steady state reduction rate of cytochrome bL in bc1 complex by ubiquinol and effect of oxygen on the kinetics, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
140 - 240
Abz-VAA
-
different purified enzyme preparations, in 0.01% Tween 20, 250 mM sucrose
additional information
additional information
-
rate of direct heme-to-heme electron transfer from the enzyme complex cytochrome c1 to cytochrome c
-
165
cytochrome c
-
mutant with truncated cytochrome c1, membrane fraction
517
cytochrome c
-
mutant with truncated cytochrome c1, purified bc1 complex
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000329
3-[(4-bromophenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
-
pH 7.4, 23°C
0.00000362
5-methyl-5-(4-phenoxyphenyl)-3-(phenylamino)-2,4-oxazolidinedione
-
noncompetitive versus cytochrome c, pH 7.4, 23°C
0.00005143
5-methyl-5-(4-phenoxyphenyl)-3-(phenylamino)-2,4-oxazolidinedione
-
competitive versus decylubiquinol, pH 7.4, 23°C
additional information
additional information
-
inhibition mechanism and kinetics
-
additional information
additional information
-
inhibitor binding and inhibition kinetics
-
additional information
additional information
-
inhibition kinetics
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00001593
3-[(2,4-diethylphenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
Sus scrofa
-
pH 7.4, 23°C
0.001517
3-[(2,6-diethylphenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
Sus scrofa
-
pH 7.4, 23°C
0.001
3-[(2-bromo-4-fluorophenyl)amino]-5-(6-bromopyridin-3-yl)-5-methyl-1,3-oxazolidine-2,4-dione
Sus scrofa
-
above, pH 7.4, 23°C
0.00005998
3-[(2-bromo-4-fluorophenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
Sus scrofa
-
pH 7.4, 23°C
0.001
3-[(4-bromophenyl)amino]-5-(6-bromopyridin-3-yl)-5-methyl-1,3-oxazolidine-2,4-dione
Sus scrofa
-
above, pH 7.4, 23°C
0.00000944 - 0.001049
3-[(4-bromophenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione