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Information on EC 7.1.1.8 - quinol-cytochrome-c reductase
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7.1.1.8 quinol-cytochrome-c reductaseIUBMB Comments
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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Word Map
- 7.1.1.8
- succinate
-
iron-sulfur
- heme
-
rieske
- antimycin
- rhodobacter
- sphaeroides
- myxothiazol
- epr
- capsulatus
- semiquinone
-
midpoint
- aniline
- stigmatellin
- n-demethylase
- aminopyrine
-
submitochondrial
-
chromatophores
-
nadph-cytochrome
-
protonmotive
- atovaquone
-
electron-transfer
-
succinate-cytochrome
- fe-s
-
supercomplexes
- denitrificans
-
drug-metabolizing
- paracoccus
- presequence
-
nadh:ubiquinone
-
high-potential
-
p-nitroanisole
- maltoside
-
n-demethylation
-
ethoxycoumarin
-
flash-induced
-
mixed-function
-
extramembrane
-
low-potential
- ferrocytochrome
- hexobarbital
-
apocytochrome
- benzphetamine
- ethylmorphine
- dccd
- bacteriochlorophyll
-
p-450-dependent
-
rotenone-sensitive
-
energy-transducing
- medicine
- n,n'-dicyclohexylcarbodiimide
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
cytochrome c reductase, bc1 complex, cytochrome bc1 complex, cytochrome bc1, ubiquinol-cytochrome c reductase, uqcrc1, cytochrome bc, cytochrome b-c1 complex, uqcrb, respiratory complex iii, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ActE
bc1
bc1 complex
coenzyme Q-cytochrome c reductase
-
-
-
-
coenzyme QH2-cytochrome c reductase
-
-
-
-
complex III
coQH2-cytochrome c oxidoreductase
-
-
-
-
cyt bc1
Cyt bc1 complex
cytochrome b-c1 complex
cytochrome b-c2 complex
cytochrome bc
cytochrome bc1 complex
dihydrocoenzyme Q-cytochrome c reductase
-
-
-
-
EC 1.10.2.2
-
-
formerly
-
hydroubiquinone c2 oxidoreductase
mitochondrial electron transport complex III
-
-
-
-
QH2:cyt c oxidoreductase
QH2:cytochrome c oxidoreductase
-
-
-
-
reduced coenzyme Q-cytochrome c reductase
-
-
-
-
reduced ubiquinone-cytochrome c oxidoreductase
-
-
-
-
reduced ubiquinone-cytochrome c reductase, complex III (mitochondrial electron transport)
-
-
-
-
respiratory complex III
ubihydroquinol:cytochrome c oxidoreductase
-
-
-
-
ubiquinol cytochrome c oxidoreductase
ubiquinol-cytochrome c oxidoreductase
-
-
-
-
ubiquinol-cytochrome c reductase
ubiquinol-cytochrome c reductase binding protein
ubiquinol-cytochrome c-2 oxidoreductase
-
-
-
-
ubiquinol-cytochrome c1 oxidoreductase
-
-
-
-
ubiquinol-cytochrome c2 oxidoreductase
ubiquinol-cytochrome c2 reductase
-
-
-
-
ubiquinol:cytochrome c oxidoreductase
ubiquinol:ferricytochrome c oxidoreductase
ubiquinone-cytochrome b-c1 oxidoreductase
-
-
-
-
ubiquinone-cytochrome c oxidoreductase
-
-
-
-
ubiquinone-cytochrome c reductase
-
-
-
-
UQCRB
UQCRC1
UQH2
cytochrome bc1 complex
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2]
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)
-
-
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2]
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
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2]
alternating half-of-sites mechanism of ubiquinol oxidation
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2]
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+[side 2]
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
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2]
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
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2]
substrate binding mechanism at the Qo site of the cytochrome bc1 complex
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2]
substrate binding site Qo structure, conformational changes upon inhibitor binding, overview
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2]
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
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2]
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
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2]
reaction mechanism, kinetic modeling
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2]
reaction mechanism, similar transition states mediate the Q-cycle and superoxide production by the cytochrome bc1 complex
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2]
reaction mechanism of superoxide generation during ubiquinol oxidation by the cytochrome bc1 complex
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2]
reaction mechanism of superoxide generation during ubiquinol oxidation by the cytochrome bc1 complex
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2]
reaction mechanism, structure-function analysis, overview
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2]
reaction mechanism, structure-function analysis, overview
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2]
reaction mechanism, structure-function analysis, overview
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2]
reaction mechanism, structure-function analysis, overview
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2]
reaction mechanism, structure-function analysis, overview
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2]
reaction mechanism, structure-function analysis, overview
-
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2]
reaction mechanism, structure-function analysis, overview
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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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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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 + 2 ferricytochrome c
2,3-dimethoxy-5-methyl-6-(10-bromodecyl)-1,4-benzoquinone + ferrocytochrome c + 2 H+[side 2]
-
-
-
-
?
2,3-dimethoxy-5-methyl-6-decylbenzoquinol + 2 ferricytochrome c
2,3-dimethoxy-5-methyl-6-decylbenzoquinone + 2 ferrocytochrome c + 2 H+[side 2]
-
-
-
-
?
2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinol + 2 ferricytochrome c
2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinone + 2 ferrocytochrome c + H+ [side 2]
-
-
-
-
?
2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinol + 2 ferricytochrome c
2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinone + ferrocytochrome c + H+ [side 2]
-
-
-
-
?
2-azido-3-methyl-5-methoxy-6-geranyl-1,4-benzoquinone + 2 ferricytochrome c1
2-azido-3-methyl-5-methoxy-6-geranyl-1,4-benzoquinol + 2 ferrocytochrome c1 + 2 H+[side 2]
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 + 2 ferricytochrome 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 + 2 ferrocytochrome c + 2 H+
-
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
-
-
?
3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinone + 2 ferricytochrome c1
3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinol + 2 ferrocytochrome c1 + 2 H+
alpha-tocopheryl hydroquinone + ferricytochrome c + H+
alpha-tocopherol + ferrocytochrome c + H2O
-
-
-
-
?
cytochrome b561 + ?
?
-
cytochrome b561, reduced upon flash excitation, is re-oxidized slowly even in the absence of antimycin
-
-
?
decylubiquinol + 2 ferricytochrome c
decylubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
decylubiquinol + 2 ferricytochrome c
decylubiquinone + 2 ferrocytochrome c + H+ [side 2]
-
-
-
-
?
dihydroubiquinone + ferricytochrome c
ubiquinone + ferrocytochrome c + 2 H+
-
-
-
?
naphthoquinol + 2 ferricytochrome c
naphthoquinone + 2 ferrocytochrome c + 2 H+
-
-
naphthoquinone is the pool quinone of the organism
-
?
plastoquinol-1 + 2 ferricytochrome c
plastoquinone-1 + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
plastoquinol-9 + 2 ferricytochrome c
plastoquinone-9 + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
quinol + 2 ferricytochrome c
quinone + 2 ferrocytochrome c + H+ [side 2]
-
-
-
-
?
quinol + 2 horse heart ferricytochrome c1
quinone + 2 horse heart ferrocytochrome c1 + H+ [side 2]
-
-
-
-
?
rhodoquinol-3 + 2 ferricytochrome c
rhodoquinone-3 + 2 ferrocytochrome c + 2 H+
-
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
-
duroquinol
-
-
?
ubiquinol + 2 4-carboxy-2,6-dinitrophenyllysine27-ferricytochrome c
ubiquinone + 2 4-carboxy-2,6-dinitrophenyllysine27-ferrocytochrome c + 2 H+
-
cytochrome c from horse, modified at Lys27
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+[side 2]
-
-
-
-
?
ubiquinol + 2 ferricytochrome c2
ubiquinone + 2 ferrocytochrome c2 + 2 H+[side 2]
-
-
-
-
?
ubiquinol + 2 ferricytochrome c552
ubiquinone + 2 ferrocytochrome c552 + 2 H+
-
-
-
?
ubiquinol + ferricytochrome b-562
ubiquinone + ferrocytochrome b-562
-
-
-
-
?
2-azido-3-methyl-5-methoxy-6-geranyl-1,4-benzoquinone + 2 ferricytochrome c1
2-azido-3-methyl-5-methoxy-6-geranyl-1,4-benzoquinol + 2 ferrocytochrome c1 + 2 H+[side 2]
-
-
-
-
?
2-azido-3-methyl-5-methoxy-6-geranyl-1,4-benzoquinone + 2 ferricytochrome c1
2-azido-3-methyl-5-methoxy-6-geranyl-1,4-benzoquinol + 2 ferrocytochrome c1 + 2 H+[side 2]
-
-
-
-
?
2-azido-3-methyl-5-methoxy-6-geranyl-1,4-benzoquinone + 2 ferricytochrome c1
2-azido-3-methyl-5-methoxy-6-geranyl-1,4-benzoquinol + 2 ferrocytochrome c1 + 2 H+[side 2]
-
-
-
-
?
3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinone + 2 ferricytochrome c1
3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinol + 2 ferrocytochrome c1 + 2 H+
-
-
-
-
?
3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinone + 2 ferricytochrome c1
3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinol + 2 ferrocytochrome c1 + 2 H+
-
-
-
-
?
3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinone + 2 ferricytochrome c1
3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinol + 2 ferrocytochrome c1 + 2 H+
-
-
-
-
?
coenzyme Q1H2 + 2 ferricytochrome c
coenzyme Q1 + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
coenzyme Q1H2 + 2 ferricytochrome c
coenzyme Q1 + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
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
-
-
?
decylbenzohydroquinol + ferricytochrome c
decylbenzohydroquinone + ferrocytochrome c + H+
-
-
-
-
?
decylbenzohydroquinol + ferricytochrome c
decylbenzohydroquinone + ferrocytochrome c + H+
-
-
-
-
?
decylplastoquinol + 2 ferricytochrome c
decylplastoquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
decylplastoquinol + 2 ferricytochrome c
decylplastoquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
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
-
-
?
menaquinol + 2 ferricytochrome c
menaquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
menaquinol + 2 ferricytochrome c
menaquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
nonylubiquinol + 2 ferricytochrome c
nonylubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
nonylubiquinol + 2 ferricytochrome c
nonylubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
plastohydroquinol + 2 ferricytochrome c
plastohydroquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
plastohydroquinol + 2 ferricytochrome c
plastohydroquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
quinol + 2 ferricytochrome c
quinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
quinol + 2 ferricytochrome c
quinone + 2 ferrocytochrome c + H+
-
-
-
-
?
quinol + 2 ferricytochrome c
quinone + 2 ferrocytochrome c + H+
-
-
-
-
?
quinol + 2 ferricytochrome c1
quinone + 2 ferrocytochrome c1 + H+ [side 2]
-
-
-
-
?
quinol + 2 ferricytochrome c1
quinone + 2 ferrocytochrome c1 + H+ [side 2]
-
-
-
-
?
quinol + 2 ferricytochrome c1
quinone + 2 ferrocytochrome c1 + H+ [side 2]
-
-
-
-
?
quinol + 2 ferricytochrome c1
quinone + 2 ferrocytochrome c1 + H+ [side 2]
-
-
-
-
?
quinol + 2 ferricytochrome c1
quinone + 2 ferrocytochrome c1 + H+ [side 2]
-
-
-
-
?
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+
-
-
-
-
?
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+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
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, 686076, 725396
-
-
?
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+
-
-
395300, 439946, 439963, 439965, 439971, 439976, 439977, 439979, 439981, 439988, 439995, 440000, 440009, 440010, 440012, 440015, 440016, 440019, 440030, 440032, 440033, 440036, 724433, 724452, 725396, 725875
-
-
?
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+
-
-
-
-
?
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+
-
-
-
-
?
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+
Fuscovulum blasticum
-
-
-
-
?
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+
-
-
-
-
?
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+
-
-
-
-
?
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+
-
-
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 + 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+
-
-
-
-
?
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+
-
-
-
-
?
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+
-
-
439946, 439976, 439998, 439999, 440003, 440010, 440012, 440015, 440019, 440021, 440022, 440030, 440036, 689387, 724452
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
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 + 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+
-
-
-
-
?
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+
-
-
-
-
?
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+
-
-
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, 724452
-
-
?
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+
-
-
-
-
?
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+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
algal cytochrome c
-
-
?
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+
-
-
-
-
?
ubiquinol + 2 ferricytochrome c
ubiquinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
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 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 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
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
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
binding interaction of ubiquinone with cytochrome b, overview
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
proton-coupled electron transfer at the Qo-site of the bc1 complex controls the rate of ubihydroquinone oxidation
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
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
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
-
-
-
r
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
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
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
enzyme complex is essentially involved in the mitochondrial respiratory electron transfer chain
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
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
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
activity is highest near physiological ionic strength and decreases at higher concentrations
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
anti-cooperative oxidation of ubiquinol, reversible partial reaction
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
ubiquinol binds to the specific binding pocket of the cytochrome bc1 complex
-
-
?
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
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
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
?
-
-
reaction mechanism of superoxide generation by bc1, overview
-
-
?
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
?
-
-
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 SUBSTRATE
NATURAL 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
naphthoquinol + 2 ferricytochrome c
naphthoquinone + 2 ferrocytochrome c + 2 H+
-
-
naphthoquinone is the pool quinone of the organism
-
?
ubiquinol + 2 ferricytochrome c552
ubiquinone + 2 ferrocytochrome c552 + 2 H+
-
-
-
?
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
-
-
?
quinol + 2 ferricytochrome c
quinone + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
quinol + 2 ferricytochrome c
quinone + 2 ferrocytochrome c + H+
-
-
-
-
?
quinol + 2 ferricytochrome c
quinone + 2 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+
-
-
-
-
?
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+
-
-
-
-
?
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
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
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
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
proton-coupled electron transfer at the Qo-site of the bc1 complex controls the rate of ubihydroquinone oxidation
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
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
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
enzyme complex is essentially involved in the mitochondrial respiratory electron transfer chain
-
-
?
ubiquinol-2 + 2 ferricytochrome c
ubiquinone-2 + 2 ferrocytochrome c + 2 H+
-
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
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
ubiquinone-10 + ferricytochrome c
ubiquinol-10 + ferrocytochrome c + 2 H+
-
-
-
-
?
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
?
-
-
reaction mechanism of superoxide generation by bc1, overview
-
-
?
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
?
-
-
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
-
the cytochrome b subunit contains two b-type hemes, bL and bH
-
cytochrome b
two cyt b subunits form the hydrophobic core of the complex, overview
-
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 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+
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+
-
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 complex contains an iron-sulfur protein, and heme groups in the cytochrome molecules
Iron
-
enzyme contains a Rieske [2Fe-2S] cluster required for activity
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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INHIBITOR
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
-
-
antimycin A
-
inhibits the enzyme complex and blocks the cell differentiation, inhibition mechanism
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
-
binding involves conformational change of Glu295, molecular dynamic simulation, mutants E295G, E295D, and E295Q are resistant to inhibition
Stigmatellin
species-specific binding of the inhibitor, binding structure and mechanism, overview
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
-
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
-
additional information
additional information
-
pre-steady-state kinetics of cytochrome b reduction
-
additional information
additional information
-
reaction kinetics of oxidation and electron transfer, complex formation kinetics, pH-dependence
-
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
additional information
additional information
-
rate of direct heme-to-heme electron transfer from the enzyme complex cytochrome c1 to cytochrome c
-
165
2 ferricytochrome c
-
mutant with truncated cytochrome c1, membrane fraction
-
517
2 ferricytochrome c
-
mutant with truncated cytochrome c1, purified bc1 complex
-
140 - 240
decylubiquinol
-
different purified enzyme preparations, in 0.01% Tween 20, 250 mM sucrose
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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 kinetics
-
additional information
additional information
-
inhibition mechanism and kinetics
-
additional information
additional information
-
inhibitor binding and 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
0.00001879
3-[(4-chlorophenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
Sus scrofa
-
pH 7.4, 23°C
0.00005792
3-[(4-methoxyphenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
Sus scrofa
-
pH 7.4, 23°C
0.00002404
3-[[5-methyl-2,4-dioxo-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidin-3-yl]amino]benzoic acid
Sus scrofa
-
pH 7.4, 23°C
0.02
4-ethyl-N-(4-hydroxyphenyl)benzenesulfonamide
Homo sapiens
-
IC50 above 0.02 mM, pH and temperature not specified in the publication
0.008
4-tert-butyl-N-(2-hydroxyphenyl)benzenesulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
0.098
4-tert-butyl-N-(3-hydroxyphenyl)benzenesulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
0.02
4-tert-butyl-N-(4-hydroxynaphthalen-1-yl)benzenesulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
0.005
4-tert-butyl-N-(4-hydroxyphenyl)benzenesulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
0.02
4-tert-butyl-N-(8-hydroxyquinolin-5-yl)benzenesulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
0.001
4-[[5-(6-bromopyridin-3-yl)-5-methyl-2,4-dioxo-1,3-oxazolidin-3-yl]amino]benzonitrile
Sus scrofa
-
above, pH 7.4, 23°C
0.005312
4-[[5-methyl-2,4-dioxo-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidin-3-yl]amino]benzoic acid
Sus scrofa
-
pH 7.4, 23°C
0.0002752
4-[[5-methyl-2,4-dioxo-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidin-3-yl]amino]benzonitrile
Sus scrofa
-
pH 7.4, 23°C
0.001
5-(6-bromopyridin-3-yl)-3-[(2,4-diethylphenyl)amino]-5-methyl-1,3-oxazolidine-2,4-dione
Sus scrofa
-
above, pH 7.4, 23°C
0.001
5-(6-bromopyridin-3-yl)-3-[(2,6-diethylphenyl)amino]-5-methyl-1,3-oxazolidine-2,4-dione
Sus scrofa
-
above, pH 7.4, 23°C
0.001
5-(6-bromopyridin-3-yl)-3-[(4-chlorophenyl)amino]-5-methyl-1,3-oxazolidine-2,4-dione
Sus scrofa
-
above, pH 7.4, 23°C
0.001
5-(6-bromopyridin-3-yl)-3-[(4-methoxyphenyl)amino]-5-methyl-1,3-oxazolidine-2,4-dione
Sus scrofa
-
above, pH 7.4, 23°C
0.001
5-(6-bromopyridin-3-yl)-5-methyl-3-(phenylamino)-1,3-oxazolidine-2,4-dione
Sus scrofa
-
above, pH 7.4, 23°C
0.001
5-(6-bromopyridin-3-yl)-5-methyl-3-[(2-methyl-4-nitrophenyl)amino]-1,3-oxazolidine-2,4-dione
Sus scrofa
-
above, pH 7.4, 23°C
0.001
5-(6-bromopyridin-3-yl)-5-methyl-3-[(4-methylphenyl)amino]-1,3-oxazolidine-2,4-dione
Sus scrofa
-
above, pH 7.4, 23°C
0.001
5-(6-bromopyridin-3-yl)-5-methyl-3-[[4-(trifluoromethyl)phenyl]amino]-1,3-oxazolidine-2,4-dione
Sus scrofa
-
above, pH 7.4, 23°C
0.02
5-(biphenyl-4-ylsulfonamido)-2-hydroxybenzoic acid
Homo sapiens
-
IC50 above 0.02 mM, pH and temperature not specified in the publication
0.00002376
5-methyl-3-[(4-methylphenyl)amino]-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
Sus scrofa
-
pH 7.4, 23°C
0.00006326
5-methyl-5-(6-phenoxypyridin-3-yl)-3-[[4-(trifluoromethyl)phenyl]amino]-1,3-oxazolidine-2,4-dione
Sus scrofa
-
pH 7.4, 23°C
0.005
6-((1-hydroxynaphthalen-4-ylamino)dioxysulfone)-2H-naphtho[1,8-bc]thiophen-2-one
Homo sapiens
-
pH and temperature not specified in the publication
0.000012
ilicicolin H
Saccharomyces cerevisiae
-
a Qn site inhibitor, a 5-(4-hydroxyphenyl)-alpha-pyridone with a decalin ring system, wild-type enzyme IC50: 12 nM
0.02
N-(3-chloro-4-hydroxyphenyl)biphenyl-4-sulfonamide
Homo sapiens
-
IC50 above 0.02 mM, pH and temperature not specified in the publication
0.02
N-(3-fluoro-4-hydroxyphenyl)biphenyl-4-sulfonamide
Homo sapiens
-
IC50 above 0.02 mM, pH and temperature not specified in the publication
0.02
N-(4-hydroxynaphthalen-1-yl)biphenyl-4-sulfonamide
Homo sapiens
-
IC50 above 0.02 mM, pH and temperature not specified in the publication
0.02
N-(4-hydroxyphenyl)-4-methylbenzenesulfonamide
Homo sapiens
-
IC50 above 0.02 mM, pH and temperature not specified in the publication
0.0025
N-(4-hydroxyphenyl)biphenyl-4-sulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
0.02
N-(4-hydroxyphenyl)naphthalene-2-sulfonamide
Homo sapiens
-
IC50 above 0.02 mM, pH and temperature not specified in the publication
0.02
N-(4-hydroxyphenyl)quinoline-8-sulfonamide
Homo sapiens
-
IC50 above 0.02 mM, pH and temperature not specified in the publication
0.02
N-(5-hydroxynaphthalen-1-yl)biphenyl-4-sulfonamide
Homo sapiens
-
IC50 above 0.02 mM, pH and temperature not specified in the publication
0.02
N-(7-hydroxynaphthalen-1-yl)biphenyl-4-sulfonamide
Homo sapiens
-
IC50 above 0.02 mM, pH and temperature not specified in the publication
0.02
N-(8-hydroxyquinolin-5-yl)biphenyl-4-sulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
0.005
potassium 4-(biphenyl-4-ylsulfonamido)phenolate
Homo sapiens
-
pH and temperature not specified in the publication
0.00000944
3-[(4-bromophenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
Sus scrofa
-
pH 7.4, 23°C
0.000337
3-[(4-bromophenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
Sus scrofa
-
in absence of n-dodecyl-beta-D-maltoside, pH 7.4, 23°C
0.001049
3-[(4-bromophenyl)amino]-5-methyl-5-(6-phenoxypyridin-3-yl)-1,3-oxazolidine-2,4-dione
Sus scrofa
-
in presence of n-dodecyl-beta-D-maltoside, pH 7.4, 23°C
0.0000482
5-methyl-5-(4-phenoxyphenyl)-3-(phenylamino)-2,4-oxazolidinedione
Sus scrofa
-
in absence of n-dodecyl-beta-D-maltoside, pH 7.4, 23°C
0.000142
5-methyl-5-(4-phenoxyphenyl)-3-(phenylamino)-2,4-oxazolidinedione
Sus scrofa
-
in presence of n-dodecyl-beta-D-maltoside, pH 7.4, 23°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5 - 8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
23
25
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
temperature dependent activity of complex III in preparations with phospholipids replaced by dimyristoylglycerophosphocholine
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
derived from Saccharomyces cerevisiae KL14-4A
-
-
brenda
formerly Rhodopseudomonas viridis
-
-
brenda
-
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
-
-
brenda
-
439963, 439976, 439979, 440009, 440010, 440012, 440015, 440019, 440030, 440033, 440036, 658194, 724433, 724452, 725396, 725875, 742085
-
-
brenda
formerly Rhodopseudomonas sphaeroides
-
-
brenda
-
395300, 396001, 439942, 439945, 439946, 439951, 439955, 439962, 439967, 439969, 439972, 439977, 439987, 439988, 439990, 439992, 439994, 439997, 440000, 440004, 440015, 440017, 440024, 440030
-
-
brenda
-
-
-
brenda
-
439946, 439976, 439999, 440003, 440010, 440012, 440015, 440019, 440021, 440030, 440036, 685619, 687705, 689387, 724452, 741983
-
-
brenda
-
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
-
-
brenda
parental control diploid strain KM91 obtained by crossing the haploid strain 777-3A with the haploid KL14-4A/60
-
-
brenda
derived from Saccharomyces cerevisiae KL14-4A
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the level of respiratory complexes III is lower in mitochondria from cells grown at pH 6.0 than in mitochondria from cells grown at pH 3.7
brenda
-
transgenic embryonic stem cell line with expression of the green fliuorescent protein under control of the alpha-myosin heavy chain promotor, enzyme expression pattern during cell development
brenda
-
-
395300, 396001, 439942, 439943, 439945, 439946, 439947, 439948, 439950, 439952, 439953, 439955, 439956, 439958, 439960, 439961, 439962, 439964, 439966, 439967, 439970, 439975, 439980, 439983, 439985, 439986, 439988, 439989, 439990, 439991, 439993, 440000, 440003, 440006, 440009, 440012, 440016, 440018, 440023, 440025, 440026, 440027, 440028, 440029, 440030, 440035, 657683, 658009, 658165, 672379, 724452, 725396
brenda
-
highly expressed in heart, the expression increases in hearts of 4-, 10-, and 28-week-old spontaneously hypertensive rats. UCCR7.2 expression is reduced in the absence of ovarian hormones, but is not directly regulated by estrogen in the heart. UCCR7.2 is a steroid hormone-responsive gene in the heart, with expression increased in cardiac hypertrophy and in response to hypertension
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
-
-
brenda
-
inner surface of the chromatophore membrane
-
brenda
-
inner surface of the chromatophore membrane
-
brenda
-
inner surface of the chromatophore membrane
-
-
brenda
-
subunits specified by nuclear genes and sythesized in the cytoplasm
brenda
-
subunits specified by nuclear genes and sythesized in the cytoplasm
brenda
-
analysis of the localization and orientation of the enzyme complex in the membrane bilayer
brenda
-
-
brenda
-
-
brenda
-
membrane localization and organization of enzyme complex domains, overview
brenda
-
membrane localization and organization of enzyme complex domains, overview
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
395300, 396001, 439942, 439944, 439945, 439946, 439948, 439949, 439950, 439952, 439953, 439955, 439956, 439958, 439961, 439964, 439966, 439967, 439970, 439975, 439978, 439979, 439983, 439986, 439988, 439989, 439990, 439991, 439993, 439995, 440003, 440006, 440009, 440012, 440018, 440020, 440023, 440025, 440026, 440027, 440028, 440030, 440035, 657683, 658009, 658165, 672379, 674163, 686076, 724452, 725396
brenda
-
mitochondrial membrane, transmembranous subunit QPc-9.5 kDa, more mass on the matrix side of the membrane
brenda
-
-
395300, 396001, 439942, 439945, 439946, 439951, 439955, 439967, 439969, 439972, 439977, 439987, 439988, 439990, 439992, 439997, 440015, 440024, 440030
brenda
-
matrix space of mitochondria and intermembrane space
brenda
-
mitochondrial membrane, transmembranous subunit QPc-9.5 kDa, more mass on the matrix side of the membrane
brenda
-
the level of respiratory complexes III is lower in mitochondria from cells grown at pH 6.0 than in mitochondria from cells grown at pH 3.7
brenda
-
-
395300, 439942, 439945, 439948, 439949, 439950, 439966, 439972, 439973, 439984, 439988, 439990, 439992, 439997, 440006, 440008, 440009, 440011, 440014, 440015, 440018, 440023, 440026, 440030, 658161, 659443, 674433, 674484, 674721, 700002, 724452
brenda
additional information
-
architecture of the intracytoplasmic membrane, overview
-
brenda
additional information
-
architecture of the intracytoplasmic membrane, overview
-
brenda
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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
-
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
-
the complex III also exhibits enzyme mitochondrial processing peptidase activity
metabolism
-
the complex III also exhibits enzyme mitochondrial processing peptidase activity
metabolism
-
the complex III also exhibits enzyme mitochondrial processing peptidase activity
metabolism
-
the complex III also exhibits enzyme mitochondrial processing peptidase activity, which is inactive in bovine cells, but can be activated through detergents treatment
metabolism
-
the bc1 complex is a functional substituent of CymA in nitrate/nitrite respiration
physiological function
-
reaction mechanism of superoxide generation by bc1, overview
physiological function
-
respiratory complex III is an electron transport complex in mitochondria, related bc complexes, overview
physiological function
-
respiratory complex III is an electron transport complex in mitochondria, related bc complexes, overview
physiological function
-
respiratory complex III is an electron transport complex in mitochondria, related bc complexes, overview
physiological function
-
respiratory complex III is an electron transport complex in mitochondria, related bc complexes, overview
physiological function
-
respiratory complex III is an electron transport complex, related bc complexes, overview
physiological function
-
respiratory complex III is an electron transport complex, related bc complexes, overview
physiological function
-
respiratory complex III is an electron transport complex, related bc complexes, overview
physiological function
-
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
-
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
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
-
the enzyme contributes to the loss-of-cardioprotection model induced by long-term diazoxide treatment and plays a role in delayed cardioprotection
physiological function
-
the overexpression of ubiquinol-cytochrome c reductase core protein 1 can protect H9c2 cardiac cells against simulated ischemia/reperfusion
physiological function
ubiquinolcytochrome c reductase binding protein induces angiogenesis in vitro and in vivo
physiological function
simulation of the enzyme kinetics under a wide range of conditions using a functional dimer model. The model consists of six electronic states characterized by the number of electrons deposited on the complex and is fully reversible. In normal steady-state conditions, only a single Qp site in the dimer is operational per quinol oxidation. The quinone pool is mostly oxidized under normal physiological operation but can switch to a more reduced state when reverse electron transport conditions are in place
physiological function
-
subunit ActE of alternative complex III functions as a direct electron donor to the cytochrome c aa3 oxygen reductase. The reduction potential of ActE is +165 mV, at pH 7.5
physiological function
Rhodothermus marinus PRQ62b
-
subunit ActE of alternative complex III functions as a direct electron donor to the cytochrome c aa3 oxygen reductase. The reduction potential of ActE is +165 mV, at pH 7.5
-
additional information
-
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
-
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
additional information
-
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
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
-
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 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, 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
-
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
Show AA Sequence and Transmembrane Helices (27092 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10000
11000
11200
-
1 * 50000 + 1 * 45000 + 2 * 31000 + 1 * 25000 + 1 * 14000 + 1 * 11500 + 1 * 11200, SDS-PAGE
11500
12000
12700
-
1 * 49000 + 1 * 45000 + 1 * 34000 + 1 * 29000 + 1 * 24000 + 1 * 12700 + 1 * 11000 + 1 * 9000, SDS-PAGE
13000
13345
-
1 * 49209 + 1 * 46520 + 1 * 42588 + 1 * 27285 + 1 * 21608 + 1 * 13345 + 1 * 9588 + 1 * 9174 + 1 * 7955 + 1 * 7326 + 1 * 6519, core protein I, core protein II, cytochrome b, cytochrome c1, iron-sulfur protein, cytochrome b-associated protein, core associated protein, hinge protein, ISP targeting peptide, cytochrome c1-associated protein, ISP-associated protein, calculated from amino acid sequence of the mature protein
13380
-
1 * 48960 + 1 * 46808 + 1 * 42727 + 1 * 27350 + 1 * 21630 + 1 * 13380 + 1 * 9261 + 1 * 8053, calculated from the amino acid sequence of the mature protein
13400
14000
15000
16000
17000
18000
-
1 * 44000 + 1 * 43000 + 1 * 32000 + 1 * 24000 + 1 * 22000 + 1 * 20000 + 1 * 18000, SDS-PAGE, 12% gel
20000
200000
21000
-
1 + 47000 + 1 * 35000 + 1 * 21000 + 1 * 15000 + 1 * 13000, SDS-PAGE
21608
-
1 * 49209 + 1 * 46520 + 1 * 42588 + 1 * 27285 + 1 * 21608 + 1 * 13345 + 1 * 9588 + 1 * 9174 + 1 * 7955 + 1 * 7326 + 1 * 6519, core protein I, core protein II, cytochrome b, cytochrome c1, iron-sulfur protein, cytochrome b-associated protein, core associated protein, hinge protein, ISP targeting peptide, cytochrome c1-associated protein, ISP-associated protein, calculated from amino acid sequence of the mature protein
21630
-
1 * 48960 + 1 * 46808 + 1 * 42727 + 1 * 27350 + 1 * 21630 + 1 * 13380 + 1 * 9261 + 1 * 8053, calculated from the amino acid sequence of the mature protein
21710
-
Rieske iron sulfur protein, holoprotein, including [Fe2-S2] cluster, amino acid sequence
22000
22400
-
1 * 35000 + 1 * 31000 + 1 * 22400, cytochrome b, cytochrome c1 and Rieske iron-sulfur protein, SDS-PAGE
22500
-
1 * 22500 + 1 * 31000/38000 + 1 * 22000 + 1 * 16000 + 1 * 8000, cytochrome b, cytochrome f, Rieske FeS protein, SDS-PAGE
23000
24000
25000
250000
26000
27285
-
1 * 49209 + 1 * 46520 + 1 * 42588 + 1 * 27285 + 1 * 21608 + 1 * 13345 + 1 * 9588 + 1 * 9174 + 1 * 7955 + 1 * 7326 + 1 * 6519, core protein I, core protein II, cytochrome b, cytochrome c1, iron-sulfur protein, cytochrome b-associated protein, core associated protein, hinge protein, ISP targeting peptide, cytochrome c1-associated protein, ISP-associated protein, calculated from amino acid sequence of the mature protein
27350
-
1 * 48960 + 1 * 46808 + 1 * 42727 + 1 * 27350 + 1 * 21630 + 1 * 13380 + 1 * 9261 + 1 * 8053, calculated from the amino acid sequence of the mature protein
28000
285000
29000
30000
31000
32000
33000
-
1 * 44000 + 1 * 33000 + 1 * 24000, cytochrome b, cytochrome c1 and [2Fe-2S] cluster, SDS-PAGE
34000
35000
39000
40000
42588
-
1 * 49209 + 1 * 46520 + 1 * 42588 + 1 * 27285 + 1 * 21608 + 1 * 13345 + 1 * 9588 + 1 * 9174 + 1 * 7955 + 1 * 7326 + 1 * 6519, core protein I, core protein II, cytochrome b, cytochrome c1, iron-sulfur protein, cytochrome b-associated protein, core associated protein, hinge protein, ISP targeting peptide, cytochrome c1-associated protein, ISP-associated protein, calculated from amino acid sequence of the mature protein
42727
-
1 * 48960 + 1 * 46808 + 1 * 42727 + 1 * 27350 + 1 * 21630 + 1 * 13380 + 1 * 9261 + 1 * 8053, calculated from the amino acid sequence of the mature protein
43000
44000
45000
46000
-
1 * 46000 + 1 * 43000 + 1 * 29000 + 1 * 28000 + 1 * 24000 + 1 * 12000 + 1 * 8000 + 1 * 6000, SDS-PAGE
46520
-
1 * 49209 + 1 * 46520 + 1 * 42588 + 1 * 27285 + 1 * 21608 + 1 * 13345 + 1 * 9588 + 1 * 9174 + 1 * 7955 + 1 * 7326 + 1 * 6519, core protein I, core protein II, cytochrome b, cytochrome c1, iron-sulfur protein, cytochrome b-associated protein, core associated protein, hinge protein, ISP targeting peptide, cytochrome c1-associated protein, ISP-associated protein, calculated from amino acid sequence of the mature protein
46808
-
1 * 48960 + 1 * 46808 + 1 * 42727 + 1 * 27350 + 1 * 21630 + 1 * 13380 + 1 * 9261 + 1 * 8053, calculated from the amino acid sequence of the mature protein
47000
48000
48960
-
1 * 48960 + 1 * 46808 + 1 * 42727 + 1 * 27350 + 1 * 21630 + 1 * 13380 + 1 * 9261 + 1 * 8053, calculated from the amino acid sequence of the mature protein
49000
49209
-
1 * 49209 + 1 * 46520 + 1 * 42588 + 1 * 27285 + 1 * 21608 + 1 * 13345 + 1 * 9588 + 1 * 9174 + 1 * 7955 + 1 * 7326 + 1 * 6519, core protein I, core protein II, cytochrome b, cytochrome c1, iron-sulfur protein, cytochrome b-associated protein, core associated protein, hinge protein, ISP targeting peptide, cytochrome c1-associated protein, ISP-associated protein, calculated from amino acid sequence of the mature protein
50000
52000
550000
6000
62000
6400
6519
-
1 * 49209 + 1 * 46520 + 1 * 42588 + 1 * 27285 + 1 * 21608 + 1 * 13345 + 1 * 9588 + 1 * 9174 + 1 * 7955 + 1 * 7326 + 1 * 6519, core protein I, core protein II, cytochrome b, cytochrome c1, iron-sulfur protein, cytochrome b-associated protein, core associated protein, hinge protein, ISP targeting peptide, cytochrome c1-associated protein, ISP-associated protein, calculated from amino acid sequence of the mature protein
7200
7326
-
1 * 49209 + 1 * 46520 + 1 * 42588 + 1 * 27285 + 1 * 21608 + 1 * 13345 + 1 * 9588 + 1 * 9174 + 1 * 7955 + 1 * 7326 + 1 * 6519, core protein I, core protein II, cytochrome b, cytochrome c1, iron-sulfur protein, cytochrome b-associated protein, core associated protein, hinge protein, ISP targeting peptide, cytochrome c1-associated protein, ISP-associated protein, calculated from amino acid sequence of the mature protein
7955
-
1 * 49209 + 1 * 46520 + 1 * 42588 + 1 * 27285 + 1 * 21608 + 1 * 13345 + 1 * 9588 + 1 * 9174 + 1 * 7955 + 1 * 7326 + 1 * 6519, core protein I, core protein II, cytochrome b, cytochrome c1, iron-sulfur protein, cytochrome b-associated protein, core associated protein, hinge protein, ISP targeting peptide, cytochrome c1-associated protein, ISP-associated protein, calculated from amino acid sequence of the mature protein
8000
8053
-
1 * 48960 + 1 * 46808 + 1 * 42727 + 1 * 27350 + 1 * 21630 + 1 * 13380 + 1 * 9261 + 1 * 8053, calculated from the amino acid sequence of the mature protein
88400
-
calculation from subunit composition, assuming stoechiometry of 1:1:1
9000
9174
-
1 * 49209 + 1 * 46520 + 1 * 42588 + 1 * 27285 + 1 * 21608 + 1 * 13345 + 1 * 9588 + 1 * 9174 + 1 * 7955 + 1 * 7326 + 1 * 6519, core protein I, core protein II, cytochrome b, cytochrome c1, iron-sulfur protein, cytochrome b-associated protein, core associated protein, hinge protein, ISP targeting peptide, cytochrome c1-associated protein, ISP-associated protein, calculated from amino acid sequence of the mature protein
9175
9200
9261
-
1 * 48960 + 1 * 46808 + 1 * 42727 + 1 * 27350 + 1 * 21630 + 1 * 13380 + 1 * 9261 + 1 * 8053, calculated from the amino acid sequence of the mature protein
9500
9588
-
1 * 49209 + 1 * 46520 + 1 * 42588 + 1 * 27285 + 1 * 21608 + 1 * 13345 + 1 * 9588 + 1 * 9174 + 1 * 7955 + 1 * 7326 + 1 * 6519, core protein I, core protein II, cytochrome b, cytochrome c1, iron-sulfur protein, cytochrome b-associated protein, core associated protein, hinge protein, ISP targeting peptide, cytochrome c1-associated protein, ISP-associated protein, calculated from amino acid sequence of the mature protein
10000
-
1 * 47000 + 1 * 45000 + 1 * 30000 + 1 * 25000 + 1 * 16000 + 1 * 10000 + 1 * 6000, SDS-PAGE
10000
-
1 * 47000 + 1 * 45000 + 1 * 30000 + 1 * 25000 + 1 * 16000 + 1 * 10000 + 1 * 6000, SDS-PAGE
10000
-
1 * 50000 + 1 * 47000 + 1 * 29000 + 1 * 26000 + 1 * 15000 + 1 * 13000 + 1 * 10000, SDS-PAGE
11000
-
each monomeric subunit contains 2 cytochromes b, 2 * 30000, a cytochrome c1, 1 * 31000, an iron-sulfur subunit, 1 * 25000 and 6 subunits without known prosthetic groups, 1 * 9000, 1 * 11000, 1 * 14000, 1 * 45000 and 1 * 52000
11000
-
1 * 44000 + 1 * 40000 + 2 * 32000 + 1 * 17000 + 1 * 14000 + 1 * 11000, SDS-PAGE
11000
-
1 * 44000 + 1 * 40000 + 2 * 31000 + 1 * 25000 + 1 * 17000 + 1 * 14000 + 1 * 11000, SDS-PAGE
11000
-
1 * 49000 + 1 * 45000 + 1 * 34000 + 1 * 29000 + 1 * 24000 + 1 * 12700 + 1 * 11000 + 1 * 9000, SDS-PAGE
11000
-
11 subunits, cytochrome b, cytochrome c1 and iron-sulfur protein carrying redox centers, 8 surplus subunits lacking redox centers, 2 core proteins and 1 * 6400 + 1 * 7200 + 1 * 9200 + 1 * 11000 and 1 * 13400
11000
-
1 * 49000 + 1 * 45000 + 1 * 34000 + 1 * 29000 + 1 * 24000 + 1 * 13000 + 1 * 11000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Rieske FeS protein, SDS-PAGE
11000
-
1 * 47000 + 1 * 39000 + 2 * 31000 + 1 * 23000 + 1 * 14000 + 1 * 13000 + 1 * 11000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Riseke FeS protein, SDS-PAGE
11500
-
1 * 50000 + 1 * 45000 + 2 * 31000 + 1 * 25000 + 1 * 14000 + 1 * 11500 + 1 * 11200, SDS-PAGE
11500
-
2 * 15000 + 1 * 43000 + 1 * 25000 + 1 * 11500 + 1 * 47000 + 1 * 43000 + 1 * 8000, multicomponent complex with 2 molecules of cytochrome b, one molecule each of cytochrome c1, iron-sulfur protein, antimycin-binding protein, core protein I, core protein II and one unknown peptide, SDS-PAGE
12000
-
1 * 46000 + 1 * 43000 + 1 * 29000 + 1 * 28000 + 1 * 24000 + 1 * 12000 + 1 * 8000 + 1 * 6000, SDS-PAGE
12000
-
1 * 52000 + 1 * 45000 + 1 * 31000 + 1 * 30000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, SDS-PAGE
12000
-
1 * 43000 + 1 * 40000 + 1 * 28000 + 1 * 29000 + 1 * 24000 + 1 * 12000 + 1 * 8000 + 1 * 5000, stoichiometry determination
12000
-
1 * 52000 + 1 * 45000 + 1 * 30000 + 1 * 31000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Riseke FeS protein, SDS-PAGE
13000
-
1 + 47000 + 1 * 35000 + 1 * 21000 + 1 * 15000 + 1 * 13000, SDS-PAGE
13000
-
1 * 50000 + 1 * 47000 + 1 * 29000 + 1 * 26000 + 1 * 15000 + 1 * 13000 + 1 * 10000, SDS-PAGE
13000
-
1 * 49000 + 1 * 45000 + 1 * 34000 + 1 * 29000 + 1 * 24000 + 1 * 13000 + 1 * 11000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Rieske FeS protein, SDS-PAGE
13000
-
1 * 47000 + 1 * 39000 + 2 * 31000 + 1 * 23000 + 1 * 14000 + 1 * 13000 + 1 * 11000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Riseke FeS protein, SDS-PAGE
13400
-
11 subunits, 3 of these proteins carry the 4 redox centres while the 8 surplus subunits do not contain redox centres, 2 core proteins 1 * 47000 + 1 * 45000, ubiquinone-binding protein, 1 * 13400 + 1 * 9500 + 1 * 9200 + 1 * 8000 + 1 * 6400, SDS-PAGE
13400
-
11 subunits, cytochrome b, cytochrome c1 and iron-sulfur protein carrying redox centers, 8 surplus subunits lacking redox centers, 2 core proteins and 1 * 6400 + 1 * 7200 + 1 * 9200 + 1 * 11000 and 1 * 13400
14000
-
each monomeric subunit contains 2 cytochromes b, 2 * 30000, a cytochrome c1, 1 * 31000, an iron-sulfur subunit, 1 * 25000 and 6 subunits without known prosthetic groups, 1 * 9000, 1 * 11000, 1 * 14000, 1 * 45000 and 1 * 52000
14000
-
1 * 44000 + 1 * 40000 + 2 * 32000 + 1 * 17000 + 1 * 14000 + 1 * 11000, SDS-PAGE
14000
-
1 * 52000 + 1 * 45000 + 1 * 31000 + 1 * 30000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, SDS-PAGE
14000
-
1 * 50000 + 1 * 45000 + 2 * 31000 + 1 * 25000 + 1 * 14000 + 1 * 11500 + 1 * 11200, SDS-PAGE
14000
-
1 * 44000 + 1 * 40000 + 2 * 31000 + 1 * 25000 + 1 * 17000 + 1 * 14000 + 1 * 11000, SDS-PAGE
14000
-
1 * 52000 + 1 * 45000 + 1 * 30000 + 1 * 31000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Riseke FeS protein, SDS-PAGE
14000
-
1 * 47000 + 1 * 39000 + 2 * 31000 + 1 * 23000 + 1 * 14000 + 1 * 13000 + 1 * 11000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Riseke FeS protein, SDS-PAGE
15000
-
1 + 47000 + 1 * 35000 + 1 * 21000 + 1 * 15000 + 1 * 13000, SDS-PAGE
15000
-
1 * 50000 + 1 * 47000 + 1 * 29000 + 1 * 26000 + 1 * 15000 + 1 * 13000 + 1 * 10000, SDS-PAGE
15000
-
2 * 15000 + 1 * 43000 + 1 * 25000 + 1 * 11500 + 1 * 47000 + 1 * 43000 + 1 * 8000, multicomponent complex with 2 molecules of cytochrome b, one molecule each of cytochrome c1, iron-sulfur protein, antimycin-binding protein, core protein I, core protein II and one unknown peptide, SDS-PAGE
16000
-
1 * 47000 + 1 * 45000 + 1 * 30000 + 1 * 25000 + 1 * 16000 + 1 * 10000 + 1 * 6000, SDS-PAGE
16000
-
1 * 47000 + 1 * 45000 + 1 * 30000 + 1 * 25000 + 1 * 16000 + 1 * 10000 + 1 * 6000, SDS-PAGE
16000
-
1 * 22500 + 1 * 31000/38000 + 1 * 22000 + 1 * 16000 + 1 * 8000, cytochrome b, cytochrome f, Rieske FeS protein, SDS-PAGE
17000
-
1 * 44000 + 1 * 40000 + 2 * 32000 + 1 * 17000 + 1 * 14000 + 1 * 11000, SDS-PAGE
17000
-
1 * 44000 + 1 * 40000 + 2 * 31000 + 1 * 25000 + 1 * 17000 + 1 * 14000 + 1 * 11000, SDS-PAGE
17000
-
1 * 23000 + 1 * 33000/34000 + 1 * 20000 + 1 * 17000 + 1 * 5000, cytochrome b, cytochrome f, Rieske FeS protein, SDS-PAGE
17000
-
1 * 23000 + 1 * 33000/34000 + 1 * 20000 + 1 * 17000 + 1 * 5000, cytochrome b, cytochrome c1, Rieske FeS protein, SDS-PAGE
20000
-
1 * 44000 + 1 * 43000 + 1 * 32000 + 1 * 24000 + 1 * 22000 + 1 * 20000 + 1 * 18000, SDS-PAGE, 12% gel
20000
-
1 * 23000 + 1 * 33000/34000 + 1 * 20000 + 1 * 17000 + 1 * 5000, cytochrome b, cytochrome f, Rieske FeS protein, SDS-PAGE
20000
-
1 * 23000 + 1 * 33000/34000 + 1 * 20000 + 1 * 17000 + 1 * 5000, cytochrome b, cytochrome c1, Rieske FeS protein, SDS-PAGE
22000
-
1 * 44000 + 1 * 43000 + 1 * 32000 + 1 * 24000 + 1 * 22000 + 1 * 20000 + 1 * 18000, SDS-PAGE, 12% gel
22000
-
1 * 22500 + 1 * 31000/38000 + 1 * 22000 + 1 * 16000 + 1 * 8000, cytochrome b, cytochrome f, Rieske FeS protein, SDS-PAGE
23000
-
1 * 23000 + 1 * 33000/34000 + 1 * 20000 + 1 * 17000 + 1 * 5000, cytochrome b, cytochrome f, Rieske FeS protein, SDS-PAGE
23000
-
1 * 47000 + 1 * 39000 + 2 * 31000 + 1 * 23000 + 1 * 14000 + 1 * 13000 + 1 * 11000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Riseke FeS protein, SDS-PAGE
23000
-
1 * 23000 + 1 * 33000/34000 + 1 * 20000 + 1 * 17000 + 1 * 5000, cytochrome b, cytochrome c1, Rieske FeS protein, SDS-PAGE
24000
-
1 * 44000 + 1 * 33000 + 1 * 24000, cytochrome b, cytochrome c1 and [2Fe-2S] cluster, SDS-PAGE
24000
-
1 * 44000 + 1 * 43000 + 1 * 32000 + 1 * 24000 + 1 * 22000 + 1 * 20000 + 1 * 18000, SDS-PAGE, 12% gel
24000
-
1 * 46000 + 1 * 43000 + 1 * 29000 + 1 * 28000 + 1 * 24000 + 1 * 12000 + 1 * 8000 + 1 * 6000, SDS-PAGE
24000
-
1 * 43000 + 1 * 40000 + 1 * 28000 + 1 * 29000 + 1 * 24000 + 1 * 12000 + 1 * 8000 + 1 * 5000, stoichiometry determination
24000
-
1 * 49000 + 1 * 45000 + 1 * 34000 + 1 * 29000 + 1 * 24000 + 1 * 12700 + 1 * 11000 + 1 * 9000, SDS-PAGE
24000
-
1 * 49000 + 1 * 45000 + 1 * 34000 + 1 * 29000 + 1 * 24000 + 1 * 13000 + 1 * 11000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Rieske FeS protein, SDS-PAGE
25000
-
each monomeric subunit contains 2 cytochromes b, 2 * 30000, a cytochrome c1, 1 * 31000, an iron-sulfur subunit, 1 * 25000 and 6 subunits without known prosthetic groups, 1 * 9000, 1 * 11000, 1 * 14000, 1 * 45000 and 1 * 52000
25000
-
1 * 47000 + 1 * 45000 + 1 * 30000 + 1 * 25000 + 1 * 16000 + 1 * 10000 + 1 * 6000, SDS-PAGE
25000
-
1 * 47000 + 1 * 45000 + 1 * 30000 + 1 * 25000 + 1 * 16000 + 1 * 10000 + 1 * 6000, SDS-PAGE
25000
-
1 * 52000 + 1 * 45000 + 1 * 31000 + 1 * 30000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, SDS-PAGE
25000
-
2 * 15000 + 1 * 43000 + 1 * 25000 + 1 * 11500 + 1 * 47000 + 1 * 43000 + 1 * 8000, multicomponent complex with 2 molecules of cytochrome b, one molecule each of cytochrome c1, iron-sulfur protein, antimycin-binding protein, core protein I, core protein II and one unknown peptide, SDS-PAGE
25000
-
1 * 40000 + 1 * 34000 + 1 * 25000 + 1 + 6000, cytochrome b, cytochrome c1, SDS-PAGE
25000
-
1 * 52000 + 1 * 45000 + 1 * 30000 + 1 * 31000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Riseke FeS protein, SDS-PAGE
28000
-
1 * 46000 + 1 * 43000 + 1 * 29000 + 1 * 28000 + 1 * 24000 + 1 * 12000 + 1 * 8000 + 1 * 6000, SDS-PAGE
28000
-
1 * 43000 + 1 * 40000 + 1 * 28000 + 1 * 29000 + 1 * 24000 + 1 * 12000 + 1 * 8000 + 1 * 5000, stoichiometry determination
29000
-
1 * 46000 + 1 * 43000 + 1 * 29000 + 1 * 28000 + 1 * 24000 + 1 * 12000 + 1 * 8000 + 1 * 6000, SDS-PAGE
29000
-
1 * 43000 + 1 * 40000 + 1 * 28000 + 1 * 29000 + 1 * 24000 + 1 * 12000 + 1 * 8000 + 1 * 5000, stoichiometry determination
29000
-
1 * 49000 + 1 * 45000 + 1 * 34000 + 1 * 29000 + 1 * 24000 + 1 * 12700 + 1 * 11000 + 1 * 9000, SDS-PAGE
29000
-
1 * 49000 + 1 * 45000 + 1 * 34000 + 1 * 29000 + 1 * 24000 + 1 * 13000 + 1 * 11000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Rieske FeS protein, SDS-PAGE
30000
-
each monomeric subunit contains 2 cytochromes b, 2 * 30000, a cytochrome c1, 1 * 31000, an iron-sulfur subunit, 1 * 25000 and 6 subunits without known prosthetic groups, 1 * 9000, 1 * 11000, 1 * 14000, 1 * 45000 and 1 * 52000
30000
-
1 * 47000 + 1 * 45000 + 1 * 30000 + 1 * 25000 + 1 * 16000 + 1 * 10000 + 1 * 6000, SDS-PAGE
30000
-
1 * 47000 + 1 * 45000 + 1 * 30000 + 1 * 25000 + 1 * 16000 + 1 * 10000 + 1 * 6000, SDS-PAGE
30000
-
1 * 52000 + 1 * 45000 + 1 * 31000 + 1 * 30000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, SDS-PAGE
30000
-
1 * 52000 + 1 * 45000 + 1 * 30000 + 1 * 31000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Riseke FeS protein, SDS-PAGE
31000
-
each monomeric subunit contains 2 cytochromes b, 2 * 30000, a cytochrome c1, 1 * 31000, an iron-sulfur subunit, 1 * 25000 and 6 subunits without known prosthetic groups, 1 * 9000, 1 * 11000, 1 * 14000, 1 * 45000 and 1 * 52000
31000
-
1 * 35000 + 1 * 31000 + 1 * 22400, cytochrome b, cytochrome c1 and Rieske iron-sulfur protein, SDS-PAGE
31000
-
1 * 52000 + 1 * 45000 + 1 * 31000 + 1 * 30000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, SDS-PAGE
31000
-
1 * 52000 + 1 * 45000 + 1 * 30000 + 1 * 31000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Riseke FeS protein, SDS-PAGE
31000
-
1 * 47000 + 1 * 39000 + 2 * 31000 + 1 * 23000 + 1 * 14000 + 1 * 13000 + 1 * 11000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Riseke FeS protein, SDS-PAGE
32000
-
1 * 44000 + 1 * 40000 + 2 * 32000 + 1 * 17000 + 1 * 14000 + 1 * 11000, SDS-PAGE
32000
-
1 * 44000 + 1 * 43000 + 1 * 32000 + 1 * 24000 + 1 * 22000 + 1 * 20000 + 1 * 18000, SDS-PAGE, 12% gel
34000
-
1 * 49000 + 1 * 45000 + 1 * 34000 + 1 * 29000 + 1 * 24000 + 1 * 12700 + 1 * 11000 + 1 * 9000, SDS-PAGE
34000
-
1 * 40000 + 1 * 34000 + 1 * 25000 + 1 + 6000, cytochrome b, cytochrome c1, SDS-PAGE
34000
-
1 * 49000 + 1 * 45000 + 1 * 34000 + 1 * 29000 + 1 * 24000 + 1 * 13000 + 1 * 11000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Rieske FeS protein, SDS-PAGE
35000
-
1 * 35000 + 1 * 31000 + 1 * 22400, cytochrome b, cytochrome c1 and Rieske iron-sulfur protein, SDS-PAGE
35000
-
1 + 47000 + 1 * 35000 + 1 * 21000 + 1 * 15000 + 1 * 13000, SDS-PAGE
39000
-
1 * 47000 + 1 * 39000 + 2 * 31000 + 1 * 23000 + 1 * 14000 + 1 * 13000 + 1 * 11000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Riseke FeS protein, SDS-PAGE
40000
-
1 * 44000 + 1 * 40000 + 2 * 32000 + 1 * 17000 + 1 * 14000 + 1 * 11000, SDS-PAGE
40000
-
1 * 43000 + 1 * 40000 + 1 * 28000 + 1 * 29000 + 1 * 24000 + 1 * 12000 + 1 * 8000 + 1 * 5000, stoichiometry determination
40000
-
1 * 44000 + 1 * 40000 + 2 * 31000 + 1 * 25000 + 1 * 17000 + 1 * 14000 + 1 * 11000, SDS-PAGE
40000
-
1 * 40000 + 1 * 34000 + 1 * 25000 + 1 + 6000, cytochrome b, cytochrome c1, SDS-PAGE
43000
-
1 * 44000 + 1 * 43000 + 1 * 32000 + 1 * 24000 + 1 * 22000 + 1 * 20000 + 1 * 18000, SDS-PAGE, 12% gel
43000
-
1 * 46000 + 1 * 43000 + 1 * 29000 + 1 * 28000 + 1 * 24000 + 1 * 12000 + 1 * 8000 + 1 * 6000, SDS-PAGE
43000
-
1 * 43000 + 1 * 40000 + 1 * 28000 + 1 * 29000 + 1 * 24000 + 1 * 12000 + 1 * 8000 + 1 * 5000, stoichiometry determination
43000
-
2 * 15000 + 1 * 43000 + 1 * 25000 + 1 * 11500 + 1 * 47000 + 1 * 43000 + 1 * 8000, multicomponent complex with 2 molecules of cytochrome b, one molecule each of cytochrome c1, iron-sulfur protein, antimycin-binding protein, core protein I, core protein II and one unknown peptide, SDS-PAGE
44000
-
1 * 44000 + 1 * 33000 + 1 * 24000, cytochrome b, cytochrome c1 and [2Fe-2S] cluster, SDS-PAGE
44000
-
1 * 44000 + 1 * 40000 + 2 * 32000 + 1 * 17000 + 1 * 14000 + 1 * 11000, SDS-PAGE
44000
-
1 * 44000 + 1 * 43000 + 1 * 32000 + 1 * 24000 + 1 * 22000 + 1 * 20000 + 1 * 18000, SDS-PAGE, 12% gel
45000
-
each monomeric subunit contains 2 cytochromes b, 2 * 30000, a cytochrome c1, 1 * 31000, an iron-sulfur subunit, 1 * 25000 and 6 subunits without known prosthetic groups, 1 * 9000, 1 * 11000, 1 * 14000, 1 * 45000 and 1 * 52000
45000
-
1 * 47000 + 1 * 45000 + 1 * 30000 + 1 * 25000 + 1 * 16000 + 1 * 10000 + 1 * 6000, SDS-PAGE
45000
-
1 * 47000 + 1 * 45000 + 1 * 30000 + 1 * 25000 + 1 * 16000 + 1 * 10000 + 1 * 6000, SDS-PAGE
45000
-
1 * 52000 + 1 * 45000 + 1 * 31000 + 1 * 30000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, SDS-PAGE
45000
-
1 * 50000 + 1 * 45000 + 2 * 31000 + 1 * 25000 + 1 * 14000 + 1 * 11500 + 1 * 11200, SDS-PAGE
45000
-
1 * 49000 + 1 * 45000 + 1 * 34000 + 1 * 29000 + 1 * 24000 + 1 * 12700 + 1 * 11000 + 1 * 9000, SDS-PAGE
45000
-
11 subunits, 3 of these proteins carry the 4 redox centres while the 8 surplus subunits do not contain redox centres, 2 core proteins 1 * 47000 + 1 * 45000, ubiquinone-binding protein, 1 * 13400 + 1 * 9500 + 1 * 9200 + 1 * 8000 + 1 * 6400, SDS-PAGE
45000
-
1 * 49000 + 1 * 45000 + 1 * 34000 + 1 * 29000 + 1 * 24000 + 1 * 13000 + 1 * 11000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Rieske FeS protein, SDS-PAGE
45000
-
1 * 52000 + 1 * 45000 + 1 * 30000 + 1 * 31000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Riseke FeS protein, SDS-PAGE
47000
-
1 * 47000 + 1 * 45000 + 1 * 30000 + 1 * 25000 + 1 * 16000 + 1 * 10000 + 1 * 6000, SDS-PAGE
47000
-
1 * 47000 + 1 * 45000 + 1 * 30000 + 1 * 25000 + 1 * 16000 + 1 * 10000 + 1 * 6000, SDS-PAGE
47000
-
11 subunits, 3 of these proteins carry the 4 redox centres while the 8 surplus subunits do not contain redox centres, 2 core proteins 1 * 47000 + 1 * 45000, ubiquinone-binding protein, 1 * 13400 + 1 * 9500 + 1 * 9200 + 1 * 8000 + 1 * 6400, SDS-PAGE
47000
-
2 * 15000 + 1 * 43000 + 1 * 25000 + 1 * 11500 + 1 * 47000 + 1 * 43000 + 1 * 8000, multicomponent complex with 2 molecules of cytochrome b, one molecule each of cytochrome c1, iron-sulfur protein, antimycin-binding protein, core protein I, core protein II and one unknown peptide, SDS-PAGE
47000
-
1 * 47000 + 1 * 39000 + 2 * 31000 + 1 * 23000 + 1 * 14000 + 1 * 13000 + 1 * 11000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Riseke FeS protein, SDS-PAGE
49000
-
1 * 49000 + 1 * 45000 + 1 * 34000 + 1 * 29000 + 1 * 24000 + 1 * 12700 + 1 * 11000 + 1 * 9000, SDS-PAGE
49000
-
1 * 49000 + 1 * 45000 + 1 * 34000 + 1 * 29000 + 1 * 24000 + 1 * 13000 + 1 * 11000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Rieske FeS protein, SDS-PAGE
50000
-
1 * 50000 + 1 * 45000 + 2 * 31000 + 1 * 25000 + 1 * 14000 + 1 * 11500 + 1 * 11200, SDS-PAGE
52000
-
each monomeric subunit contains 2 cytochromes b, 2 * 30000, a cytochrome c1, 1 * 31000, an iron-sulfur subunit, 1 * 25000 and 6 subunits without known prosthetic groups, 1 * 9000, 1 * 11000, 1 * 14000, 1 * 45000 and 1 * 52000
52000
-
1 * 52000 + 1 * 45000 + 1 * 31000 + 1 * 30000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, SDS-PAGE
52000
-
1 * 52000 + 1 * 45000 + 1 * 30000 + 1 * 31000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Riseke FeS protein, SDS-PAGE
6000
-
1 * 47000 + 1 * 45000 + 1 * 30000 + 1 * 25000 + 1 * 16000 + 1 * 10000 + 1 * 6000, SDS-PAGE
6000
-
1 * 47000 + 1 * 45000 + 1 * 30000 + 1 * 25000 + 1 * 16000 + 1 * 10000 + 1 * 6000, SDS-PAGE
6000
-
1 * 46000 + 1 * 43000 + 1 * 29000 + 1 * 28000 + 1 * 24000 + 1 * 12000 + 1 * 8000 + 1 * 6000, SDS-PAGE
6400
-
11 subunits, 3 of these proteins carry the 4 redox centres while the 8 surplus subunits do not contain redox centres, 2 core proteins 1 * 47000 + 1 * 45000, ubiquinone-binding protein, 1 * 13400 + 1 * 9500 + 1 * 9200 + 1 * 8000 + 1 * 6400, SDS-PAGE
6400
-
11 subunits, cytochrome b, cytochrome c1 and iron-sulfur protein carrying redox centers, 8 surplus subunits lacking redox centers, 2 core proteins and 1 * 6400 + 1 * 7200 + 1 * 9200 + 1 * 11000 and 1 * 13400
7200
-
11 subunits, cytochrome b, cytochrome c1 and iron-sulfur protein carrying redox centers, 8 surplus subunits lacking redox centers, 2 core proteins and 1 * 6400 + 1 * 7200 + 1 * 9200 + 1 * 11000 and 1 * 13400
8000
-
1 * 46000 + 1 * 43000 + 1 * 29000 + 1 * 28000 + 1 * 24000 + 1 * 12000 + 1 * 8000 + 1 * 6000, SDS-PAGE
8000
-
1 * 43000 + 1 * 40000 + 1 * 28000 + 1 * 29000 + 1 * 24000 + 1 * 12000 + 1 * 8000 + 1 * 5000, stoichiometry determination
8000
-
11 subunits, 3 of these proteins carry the 4 redox centres while the 8 surplus subunits do not contain redox centres, 2 core proteins 1 * 47000 + 1 * 45000, ubiquinone-binding protein, 1 * 13400 + 1 * 9500 + 1 * 9200 + 1 * 8000 + 1 * 6400, SDS-PAGE
8000
-
2 * 15000 + 1 * 43000 + 1 * 25000 + 1 * 11500 + 1 * 47000 + 1 * 43000 + 1 * 8000, multicomponent complex with 2 molecules of cytochrome b, one molecule each of cytochrome c1, iron-sulfur protein, antimycin-binding protein, core protein I, core protein II and one unknown peptide, SDS-PAGE
8000
-
1 * 22500 + 1 * 31000/38000 + 1 * 22000 + 1 * 16000 + 1 * 8000, cytochrome b, cytochrome f, Rieske FeS protein, SDS-PAGE
9000
-
each monomeric subunit contains 2 cytochromes b, 2 * 30000, a cytochrome c1, 1 * 31000, an iron-sulfur subunit, 1 * 25000 and 6 subunits without known prosthetic groups, 1 * 9000, 1 * 11000, 1 * 14000, 1 * 45000 and 1 * 52000
9000
-
1 * 52000 + 1 * 45000 + 1 * 31000 + 1 * 30000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, SDS-PAGE
9000
-
1 * 49000 + 1 * 45000 + 1 * 34000 + 1 * 29000 + 1 * 24000 + 1 * 12700 + 1 * 11000 + 1 * 9000, SDS-PAGE
9000
-
1 * 52000 + 1 * 45000 + 1 * 30000 + 1 * 31000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Riseke FeS protein, SDS-PAGE
9200
-
11 subunits, 3 of these proteins carry the 4 redox centres while the 8 surplus subunits do not contain redox centres, 2 core proteins 1 * 47000 + 1 * 45000, ubiquinone-binding protein, 1 * 13400 + 1 * 9500 + 1 * 9200 + 1 * 8000 + 1 * 6400, SDS-PAGE
9200
-
11 subunits, cytochrome b, cytochrome c1 and iron-sulfur protein carrying redox centers, 8 surplus subunits lacking redox centers, 2 core proteins and 1 * 6400 + 1 * 7200 + 1 * 9200 + 1 * 11000 and 1 * 13400
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heptamer
nonamer
octamer
oligomer
pentamer
tetramer
trimer
undecamer
additional information
?
-
x * 18000, SDS-PAGE of subunit ActE, truncated protein lacking 26 amino acid signal sequence
?
Rhodothermus marinus PRQ62b
-
x * 18000, SDS-PAGE of subunit ActE, truncated protein lacking 26 amino acid signal sequence
-
dimer
-
subunit I: 50000 Da, subunit II: 45000 Da, Rieske iron-sulfur protein 22000 Da and for subunits from 14000-8000 Da
dimer
-
each monomeric subunit contains 2 cytochromes b, 2 * 30000, a cytochrome c1, 1 * 31000, an iron-sulfur subunit, 1 * 25000 and 6 subunits without known prosthetic groups, 1 * 9000, 1 * 11000, 1 * 14000, 1 * 45000 and 1 * 52000
dimer
-
each monomeric subunit contains 2 cytochromes b, 2 * 30000, a cytochrome c1, 1 * 31000, an iron-sulfur subunit, 1 * 25000 and 6 subunits without known prosthetic groups, 1 * 9000, 1 * 11000, 1 * 14000, 1 * 45000 and 1 * 52000
-
dimer
truncation of the organism-specific, acidic N-terminus of cytochrome c1 changes the oligomerization state of the enzyme to a dimer
dimer
-
complex composition, binding structure of cytochromes, crystal structure, overview
heptamer
-
1 * 47000 + 1 * 45000 + 1 * 30000 + 1 * 25000 + 1 * 16000 + 1 * 10000 + 1 * 6000, SDS-PAGE
heptamer
-
1 * 44000 + 1 * 43000 + 1 * 32000 + 1 * 24000 + 1 * 22000 + 1 * 20000 + 1 * 18000, SDS-PAGE, 12% gel
heptamer
-
1 * 50000 + 1 * 47000 + 1 * 29000 + 1 * 26000 + 1 * 15000 + 1 * 13000 + 1 * 10000, SDS-PAGE
heptamer
-
1 * 47000 + 1 * 45000 + 1 * 30000 + 1 * 25000 + 1 * 16000 + 1 * 10000 + 1 * 6000, SDS-PAGE
heptamer
-
1 * 44000 + 1 * 40000 + 2 * 32000 + 1 * 17000 + 1 * 14000 + 1 * 11000, SDS-PAGE
octamer
-
1 * 46000 + 1 * 43000 + 1 * 29000 + 1 * 28000 + 1 * 24000 + 1 * 12000 + 1 * 8000 + 1 * 6000, SDS-PAGE
octamer
-
1 * 43000 + 1 * 40000 + 1 * 28000 + 1 * 29000 + 1 * 24000 + 1 * 12000 + 1 * 8000 + 1 * 5000, stoichiometry determination
octamer
-
1 * 49000 + 1 * 45000 + 1 * 34000 + 1 * 29000 + 1 * 24000 + 1 * 12700 + 1 * 11000 + 1 * 9000, SDS-PAGE
octamer
-
1 * 48960 + 1 * 46808 + 1 * 42727 + 1 * 27350 + 1 * 21630 + 1 * 13380 + 1 * 9261 + 1 * 8053, calculated from the amino acid sequence of the mature protein
octamer
-
1 * 52000 + 1 * 45000 + 1 * 31000 + 1 * 30000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, SDS-PAGE
octamer
-
1 * 50000 + 1 * 45000 + 2 * 31000 + 1 * 25000 + 1 * 14000 + 1 * 11500 + 1 * 11200, SDS-PAGE
octamer
-
composed of 8 different subunits with molecular weights ranging from 11-44 kDa
octamer
-
1 * 44000 + 1 * 40000 + 2 * 31000 + 1 * 25000 + 1 * 17000 + 1 * 14000 + 1 * 11000, SDS-PAGE
oligomer
-
2 * 15000 + 1 * 43000 + 1 * 25000 + 1 * 11500 + 1 * 47000 + 1 * 43000 + 1 * 8000, multicomponent complex with 2 molecules of cytochrome b, one molecule each of cytochrome c1, iron-sulfur protein, antimycin-binding protein, core protein I, core protein II and one unknown peptide, SDS-PAGE
oligomer
-
1 * 49000 + 1 * 45000 + 1 * 34000 + 1 * 29000 + 1 * 24000 + 1 * 13000 + 1 * 11000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Rieske FeS protein, SDS-PAGE
oligomer
-
1 * 40000 + 1 * 34000 + 1 * 25000 + 1 + 6000, cytochrome b, cytochrome c1, SDS-PAGE
oligomer
-
1 * 52000 + 1 * 45000 + 1 * 30000 + 1 * 31000 + 1 * 25000 + 1 * 14000 + 1 * 12000 + 1 * 9000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Riseke FeS protein, SDS-PAGE
oligomer
-
1 * 47000 + 1 * 39000 + 2 * 31000 + 1 * 23000 + 1 * 14000 + 1 * 13000 + 1 * 11000, core protein 1, core protein 2, cytochrome b, cytochrome c1, Riseke FeS protein, SDS-PAGE
oligomer
-
1 * 23000 + 1 * 33000/34000 + 1 * 20000 + 1 * 17000 + 1 * 5000, cytochrome b, cytochrome f, Rieske FeS protein, SDS-PAGE
oligomer
-
1 * 23000 + 1 * 33000/34000 + 1 * 20000 + 1 * 17000 + 1 * 5000, cytochrome b, cytochrome c1, Rieske FeS protein, SDS-PAGE
oligomer
-
1 * 22500 + 1 * 31000/38000 + 1 * 22000 + 1 * 16000 + 1 * 8000, cytochrome b, cytochrome f, Rieske FeS protein, SDS-PAGE
pentamer
-
1 + 47000 + 1 * 35000 + 1 * 21000 + 1 * 15000 + 1 * 13000, SDS-PAGE
trimer
-
1 * 62000 + 1 * 39000 + 1 * 20000, cytochrome c1, cytochrome b, Rieske-type iron-sulfur protein, SDS-PAGE
trimer
-
1 * 44000 + 1 * 33000 + 1 * 24000, cytochrome b, cytochrome c1 and [2Fe-2S] cluster, SDS-PAGE
trimer
-
1 * 44000 + 1 * 33000 + 1 * 24000, cytochrome b, cytochrome c1 and [2Fe-2S] cluster, SDS-PAGE
-
trimer
-
1 * 35000 + 1 * 31000 + 1 * 22400, cytochrome b, cytochrome c1 and Rieske iron-sulfur protein, SDS-PAGE
undecamer
-
11 subunits, 3 of these proteins carry the 4 redox centres while the 8 surplus subunits do not contain redox centres, 2 core proteins 1 * 47000 + 1 * 45000, ubiquinone-binding protein, 1 * 13400 + 1 * 9500 + 1 * 9200 + 1 * 8000 + 1 * 6400, SDS-PAGE
undecamer
-
1 * 49209 + 1 * 46520 + 1 * 42588 + 1 * 27285 + 1 * 21608 + 1 * 13345 + 1 * 9588 + 1 * 9174 + 1 * 7955 + 1 * 7326 + 1 * 6519, core protein I, core protein II, cytochrome b, cytochrome c1, iron-sulfur protein, cytochrome b-associated protein, core associated protein, hinge protein, ISP targeting peptide, cytochrome c1-associated protein, ISP-associated protein, calculated from amino acid sequence of the mature protein
undecamer
-
11 subunits, cytochrome b, cytochrome c1 and iron-sulfur protein carrying redox centers, 8 surplus subunits lacking redox centers, 2 core proteins and 1 * 6400 + 1 * 7200 + 1 * 9200 + 1 * 11000 and 1 * 13400
additional information
-
enzyme complex subunit composition and stoichiometry, subunits of 14, 21, 25, 32, 40, and 55 kDa, overview
additional information
-
enzyme is part of the mitochondrial cytochrome bc1 complex
additional information
-
separation of multienzyme complex III components, mass spectrometral analysis, complex composition, overview
additional information
-
structural organization of complex III, subunit composition of bc1, and structures of the bc1 subunits essential for electron transport function, overview
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
additional information
-
structural organization of complex III, subunit composition of bc1, and structures of the bc1 subunits essential for electron transport function, overview
additional information
-
the Rhodobacter sphaeroides complex contains four protein subunits: three core subunits and one supernumerary subunit
additional information
-
structural organization of complex III, subunit composition of bc1, and structures of the bc1 subunits essential for electron transport function, overview
additional information
-
separation of multienzyme complex III components, mass spectrometral analysis, complex composition, overview
additional information
-
spectroscopic enzyme complex composition analysis, structural changes upon cofactor or substrate binding, overview
additional information
-
structural organization of complex III, subunit composition of bc1, and structures of the bc1 subunits essential for electron transport function, overview
additional information
-
enzyme complex is a dimer of oligomeric complexes with 11 subunits, composition analysis by mass spectrometry, overview
additional information
-
structural organization of complex III, subunit composition of bc1, and structures of the bc1 subunits essential for electron transport function, overview
additional information
-
interaction analysis between monomers of the dimeric enzyme complex
additional information
-
modeling the variations in cytochrome b structure with the mutated bc1 complexes
additional information
-
secondary structure of yeast cytochrome b and a view of center N, overview
additional information
-
blue-native PAGE analysis: supercomplex composed of dimeric complex III and two copies of monomeric complex IV, supercomplex composed of dimeric complex III and one copy of monomeric complex IV, dimeric complex III
additional information
-
structural organization of complex III, subunit composition of bc1, and structures of the bc1 subunits essential for electron transport function, overview
additional information
-
structural organization of complex III, subunit composition of bc1, and structures of the bc1 subunits essential for electron transport function, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
lipoprotein
phospholipoprotein
proteolytic modification
lipoprotein
-
post-translational modification covalently binds a lipid to the cysteine residue included in the lipobox segment
lipoprotein
Rhodothermus marinus PRQ62b
-
post-translational modification covalently binds a lipid to the cysteine residue included in the lipobox segment
-
proteolytic modification
-
sequence contains an N-terminal signal sequence of 26 amino acids
proteolytic modification
Rhodothermus marinus PRQ62b
-
sequence contains an N-terminal signal sequence of 26 amino acids
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified cytochrome bc1 complex with bound inhibitors 2,3,4-trimethoxy-5-decyl-6-methyl-phenol or 2,3,4-trimethoxy-5-methyl-6-decyl-phenol, the latter in a 4fold molar excess, 2-4 weeks, X-ray diffraction structure determination and analysis
-
purified native oxidized enzyme complex or enzyme bound to antimycin A1 or 2-nonyl-4-hydroxyquinoline N-oxide, hanging drop vapour diffusion method, 20 mg/ml protein in 50 mM MOPS, pH 7.2, 20 mM ammonium acetate, 20% w/v glycerol, and either 0.1% decanoyl-N-methylglucamide or 0.1% diheptanoyl phosphatidylcholine, or 0.16% sucrose monocaprate, mixed with precipitant solution, X-ray diffraction structure determination and analysis at 2.4-3.2 A resolution, modeling
-
bc1 from Rhodobacter sphaeroides can only be crystallized bound to certain types of inhibitors such as stigmatellin and famoxadone, bc1 crystal structure analysis
-
multilayer membrane crystals of cytochrome reductase formed by the dialysis method at pH 5.5
-
purified recombinant fully functional complex, hanging drop vapour diffusion method, 20 mg/ml protein in 25 mM sodium phosphate, pH 7.5, 250 mM NaCl and 0.02% beta-ddodecyl-malto-pyranoside is mixed with reservoir solution, containing 100 mM sodium acetate, pH 4.6, 50 mM NaCl, 33% 2-methyl-2,4-pentandiol, in a 1:2 ratio, 18°C, 4 days, X-ray diffraction structure determination and analysis at 2.7 A resolution, molecular replacement
crystallization of the enzyme cytochrome bc1 complex with mitochondrial cytochrome c and the antibody fragment FV18E11, protein solution with 120 mM ionic strength is rapidly mixed with precipitation solution containing 12% PEG 4000, 20 mM Tris-HCl, pH 7.5, hanging drop vapour diffusion method, 3 weeks at 4°C, X-ray diffraction structure determination and analysis, modeling
-
crystallized in the presence of stigmatellin or hexahydrodibenzothiophene, bc1 crystal structure analysis
-
purified enzyme with inhibitor 5-n-heptyl-6-hydroxy-4,7-dioxobenzothiazole bound, microseeding and vapour diffusion method, protein solution contains 50 mg/ml protein, mixing with precipitant solution containing 5% PEG 4000, Tris-HCl, pH 7.5, 0.05% n-undecyl-beta-D-maltopyranoside, 0.01 mM 5-n-heptyl-6-hydroxy-4,7-dioxobenzothiazole, room temperature, a few days, X-ray diffraction structure determination and analysis at 2.5 A resolution
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E295D
-
site-directed mutagenesis, mutant is insensitive to stigmatellin inhibition, mutant shows slightly increased Km for ubiquinol, and lowered electron transfer rates compared to the wild-type
E295G
-
site-directed mutagenesis, mutant is insensitive to stigmatellin inhibition, mutant shows slightly increased Km for ubiquinol, and lowered electron transfer rates compared to the wild-type
E295Q
-
site-directed mutagenesis, mutant is insensitive to stigmatellin inhibition, mutant shows slightly increased Km for ubiquinol, and lowered electron transfer rates compared to the wild-type
H111N
-
site-directed mutagenesis, the rate of heme bL reduction in the H111N mutant complex increases in the presence of oxygen, no altered effect of superoxide dismutase on the oxygen increased rate of heme bL reduction in the H111N mutant complex compaired to the wild-type enzyme, overview
Y156W
-
site-directed mutagenesis, mutant enzyme shows altered pH-dependence compared to the wild-type enzyme
H291L
E272Q
-
mutation in cytochrome b, elimination of the proton acceptor in cytochrome b, decreased rate of quinol oxidation
F278I
-
site-directed mutagenesis, the mutation does not affect the residues of the EF helix of cytochrome b, the mutant shows similar ubiquinol-binding as the wild-type complex
G37D
-
site-directed mutagenesis, the mutation is located on exon 1, the mutant is less sensitive to ilicicolin H, compared to the wild-type, and shows normal growth
G37S
-
site-directed mutagenesis, the mutation is located on exon 1, the mutant is less sensitive to ilicicolin H, compared to the wild-type, and shows impaired growth
I269M
-
site-directed mutagenesis, the mutation affects the residues of the EF helix of cytochrome b, the mutant shows modified ubiquinol-binding compared to the wild-type complex
L198F
L282V
-
site-directed mutagenesis, the mutation affects the residues of the EF helix of cytochrome b, the mutant shows modified ubiquinol-binding compared to the wild-type complex, the mutant is resistant to inhibition by atovaquone
Q22E
Q22T
S183A
-
site-directed mutagenesis, kinetic parameters compared to the wild-type enzyme
S183T
-
site-directed mutagenesis, kinetic parameters compared to the wild-type enzyme
S20L
-
site-directed mutagenesis, the mutation is located on exon 1, the mutant is resistant to ilicicolin H and shows impaired growth
S20T
Y185F
Y185F/E272Q
-
mutation (185) in the Rieske protein, mutation (272) in cytochrome b, decreased rate of quinol oxidation
Y279C
-
site-directed mutagenesis, the mutation affects the residues of the EF helix of cytochrome b, the mutant shows modified ubiquinol-binding compared to the wild-type complex, the mutant is resistant to inhibition by atovaquone
Y279S
-
site-directed mutagenesis, the mutation affects the residues of the EF helix of cytochrome b, the mutant shows modified ubiquinol-binding compared to the wild-type complex, the mutant is resistant to inhibition by atovaquone
additional information
H291L
-
the mutant shows reduced activity compared to the wild type enzyme
H291L
-
the mutant shows reduced activity compared to the wild type enzyme
-
L198F
-
site-directed mutagenesis, the mutation is located on exon 4, the mutant is less sensitive to ilicicolin H, compared to the wild-type, and shows normal growth
L198F
-
mutation in the yeast bc1 complex conferrs resistance to ilicicolin H
Q22E
-
site-directed mutagenesis, the mutation is located on exon 1, the mutant is resistant to ilicicolin H and shows normal growth
Q22E
-
mutation in the yeast bc1 complex conferrs resistance to ilicicolin H
Q22T
-
site-directed mutagenesis, the mutation is located on exon 1, the mutant is resistant to ilicicolin H and shows normal growth
Q22T
-
mutation in the yeast bc1 complex conferrs resistance to ilicicolin H
S20T
-
site-directed mutagenesis, the mutation is located on exon 1, the mutant is resistant to ilicicolin H and shows normal growth
S20T
-
mutation in the yeast bc1 complex conferrs resistance to ilicicolin H
Y185F
-
iron-sulfur protein mutant, pre-steady-state and steady-state kinetic analysis in comparison to the wild-type enzyme
Y185F
-
site-directed mutagenesis, kinetic parameters compared to the wild-type enzyme
Y185F
-
mutation in the Rieske protein, decreased redox potential of the FeS cluster, decreased rate of quinol oxidation
additional information
-
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
additional information
-
a functional cyt bc1 complex with a truncated cyt c1: the coding region of the fbcC gene between triplet 39 and 202, specifying the complete highly acidic domain of the Paracoccus denitrificans cyt c1, is deleted in frame (removing nucleotides 2279 to 2766)
additional information
truncation of the organism-specific, acidic N-terminus of cytochrome c1 changes the oligomerization state of the enzyme to a dimer
additional information
-
construction of several mutants, some of which are resistant to center N site enzyme inhibitors, such as ilicicolin H or antimycin, genomic structure of mutants, effects of the cytochrome b mutations on respiratory growth and cross-resistance to other Qn site inhibitors, overview
additional information
-
cytochrome b mutations that modify the ubiquinol-binding pocket of the cytochrome bc1 complex and confer anti-malarial drug resistance in Saccharomyces cerevisiae, modeling the variations in cytochrome b structure and atovaquone binding with the mutated bc1 complexes, overview
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9.5
-
irreversibly denatured at pH lower than 5.0, stable at neutral pH, at pH 9.5 40% of the enzyme is irreversibly denatured after 19h
439979
5.5 - 9
-
activity decreases drastically if pH is higher than 9.0 or lower than 5.5
439971
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
37
-
stable at lower temperatures, becomes less stable when incubation temperature is raised, half-life time at 37°C is 15 min
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 50% w/v glycerol, spectral properties and reductase activity unaltered after 2 months, but decrease in electron transfer ratio
-20°C, isolated complex III is stored in presence of 50% glycerol, can be used for functional studies up to a month, for preparation of subunits only freshly prepared bc1 complex, because storage leads to partial degradation of some subunits by proteases
-
-70°C, 50 mM Tris-HCl buffer, pH 8.0, 200 mM NaCl, 0.1 mg/ml dodecylmaltoside, 50% glycerol
-
-80C
4°C, 0.003 mM purified enzyme, 0.01% Tween 20, 250 mM sucrose, 1 week, stable
-
-20C, 50% w/v glycerol, spectral properties and reductase activity unaltered after 2 months, but decrease in electron transfer ratio
-
-20C, 50% w/v glycerol, spectral properties and reductase activity unaltered after 2 months, but decrease in electron transfer ratio
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
isolation of mitochondria, solubilizatioin of membranes, sucrose gradient ultracentrifugation
-
native enzyme complex from membranes, recombinant membraneous and soluble [2Fe-2S] proteins from Escherichia coli to homogeneity
-
purification of cytochrome c1, and the Rieske ISP with soluble fragments
-
separation of multienzyme complex III components from heart mitochondria
-
-
-
-
-
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
all of the genes for the subunits of the yeast including QCR6, the nuclear gene encoding subunit 6 have been cloned and sequenced
-
CBP3 gene cloned by transformation of a mutant from complementation group G28 with a yeast genomic library
-
cloning and mapping of the yeast nuclear genes for the core II and Rieske iron-sulphur protein, reintroduced into yeast cells on multi-copy plasmids
-
cloning of human mitochondrial genes, comparison with bovine mitochondrial genes
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cloning of the structural gene for the 40-kDa subunit II in pEMBL and M13 vectors and DNA sequence analysis
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complete sequence of bovine mitochondrial DNA in a clone library in multicopy plasmid vectors
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cytochrome b gene, DNA sequence determination of wild-type and mutant strains
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DNA sequence of the Rieske ISP determined
expression of the Rieske [2Fe-2S] cluster from gene petA in Escherichia coli as full length membraneous protein or as truncated soluble protein, phylogenetic analysis of Rieske ISPs, genes petA and petB
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nuclear genes coding for the 17000 kDa, 14000 kDa and 11000 kDa subunits isolated from a clone bank of yeast nuclear DNA
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operon encoding the bc1 complex cloned and sequenced, operon disrupted by transposon insertion
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petABC operon encoding the subunits of the cytochrome bc1 complex sequenced, petB gene cloned
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recombinant expression of cyt bc1DELTAac complex fused with a C-terminal deca-histidine-tag at cyt b
segment of the iron-sulfur protein gene from Neurospora crassa used to detect the yeast gene by Southern analysis, yeast gene, which contains no introns, expressed in Escherichia coli
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strain pMTO-404/MTRKB1 constructed by deletion of the chromosomal copy of the pet operon from green strain MT1131 and genetic complementation with a plasmid pMTO-404 containing the operon and a tetracycline resistance gene
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structural genes petA for the Rieske FeS protein, petB for cytochrome b and petC for cytochrome c1 cloned by complementation, using a mutant defective in this complex
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
long-term diazoxide treatment up-regulates ubiquinol-cytochrome c reductase core protein 1 expression
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serum enzyme level in patients with lung adenocarcinoma is significantly increased compared with that of pneumonia patients and normal control subjects
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the enzyme is specifically downregulated in clear cell renal cell carcinoma, compared with papillary and chromophobe renal cell carcinoma
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the expression of the bc1 complex does not respond to either nitrate, nitrate, Crp or ArcA proteins
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the expression of the bc1 complex is favoured in oxygen-abundant environments
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
reconstitution
reconstitution of the solubilized membrane-protein complex in phospholipid vesicles
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
additional information
the complex from the alpha-proteobacterium Paracoccus denitrificans is a model for the medically relevant mitochondrial complexes
medicine
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test of respiratory-chain dysfunction in human mitochondrial myopathies
medicine
-
serum ubiquinol cytochrome c reductase hinge is a diagnostic biomarker for lung adenocarcinoma
medicine
-
the enzyme is a potential independent favorable prognostic factor for recurrence and survival of patients with clear cell renal cell carcinoma after nephrectomy
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Release 2023.1 (January 2023)
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