7.1.1.8 2,3-dimethoxy-5-methyl-6-(10-bromodecyl)-1,4-benzoquinol + 2 ferricytochrome c - Rhodospirillum rubrum 2,3-dimethoxy-5-methyl-6-(10-bromodecyl)-1,4-benzoquinone + ferrocytochrome c + 2 H+[side 2] - ? 289174 7.1.1.8 2,3-dimethoxy-5-methyl-6-decylbenzoquinol + 2 ferricytochrome c - Bos taurus 2,3-dimethoxy-5-methyl-6-decylbenzoquinone + 2 ferrocytochrome c + 2 H+[side 2] - ? 289173 7.1.1.8 2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinol + 2 ferricytochrome c - Paracoccus denitrificans 2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinone + ferrocytochrome c + H+ [side 2] - ? 453798 7.1.1.8 2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinol + 2 ferricytochrome c - Paracoccus denitrificans 2,3-dimethoxy-5-methyl-6-geranyl-1,4-benzoquinone + 2 ferrocytochrome c + H+ [side 2] - ? 454110 7.1.1.8 2-azido-3-methyl-5-methoxy-6-geranyl-1,4-benzoquinone + 2 ferricytochrome c1 - Cereibacter sphaeroides 2-azido-3-methyl-5-methoxy-6-geranyl-1,4-benzoquinol + 2 ferrocytochrome c1 + 2 H+[side 2] - ? 289175 7.1.1.8 2-azido-3-methyl-5-methoxy-6-geranyl-1,4-benzoquinone + 2 ferricytochrome c1 - Cereibacter sphaeroides GA 2-azido-3-methyl-5-methoxy-6-geranyl-1,4-benzoquinol + 2 ferrocytochrome c1 + 2 H+[side 2] - ? 289175 7.1.1.8 2-azido-3-methyl-5-methoxy-6-geranyl-1,4-benzoquinone + 2 ferricytochrome c1 - Cereibacter sphaeroides R-26 2-azido-3-methyl-5-methoxy-6-geranyl-1,4-benzoquinol + 2 ferrocytochrome c1 + 2 H+[side 2] - ? 289175 7.1.1.8 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 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 Bos taurus 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+ - ? 395638 7.1.1.8 3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinone + 2 ferricytochrome c1 - Cereibacter sphaeroides 3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinol + 2 ferrocytochrome c1 + 2 H+ - ? 289176 7.1.1.8 3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinone + 2 ferricytochrome c1 - Cereibacter sphaeroides GA 3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinol + 2 ferrocytochrome c1 + 2 H+ - ? 289176 7.1.1.8 3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinone + 2 ferricytochrome c1 - Cereibacter sphaeroides R-26 3-azido-2-methyl-5-methoxy-6-geranyl-1,4-benzoquinol + 2 ferrocytochrome c1 + 2 H+ - ? 289176 7.1.1.8 alpha-tocopheryl hydroquinone + ferricytochrome c + H+ - Bos taurus alpha-tocopherol + ferrocytochrome c + H2O - ? 396400 7.1.1.8 coenzyme Q1H2 + 2 ferricytochrome c - Paracoccus denitrificans coenzyme Q1 + 2 ferrocytochrome c + 2 H+ - ? 404691 7.1.1.8 coenzyme Q1H2 + 2 ferricytochrome c - Rattus norvegicus coenzyme Q1 + 2 ferrocytochrome c + 2 H+ - ? 404691 7.1.1.8 cytochrome b561 + ? cytochrome b561, reduced upon flash excitation, is re-oxidized slowly even in the absence of antimycin Roseobacter denitrificans ? - ? 404751 7.1.1.8 cytochrome c551 + ? - Roseobacter denitrificans ? - ? 404754 7.1.1.8 decyl-ubiquinol + ferricytochrome c - Saccharomyces cerevisiae decyl-ubiquinone + ferrocytochrome c - r 376658 7.1.1.8 decyl-ubiquinol + ferricytochrome c - Bos taurus decyl-ubiquinone + ferrocytochrome c - ? 376658 7.1.1.8 decyl-ubiquinol + ferricytochrome c anti-cooperative oxidation of ubiquinol, reversible partial reaction Saccharomyces cerevisiae decyl-ubiquinone + ferrocytochrome c - ? 376658 7.1.1.8 decylbenzohydroquinol + ferricytochrome c - Rhodobacter capsulatus decylbenzohydroquinone + ferrocytochrome c + H+ - ? 441272 7.1.1.8 decylbenzohydroquinol + ferricytochrome c - Rhodobacter capsulatus MT-RBC1 decylbenzohydroquinone + ferrocytochrome c + H+ - ? 441272 7.1.1.8 decylplastoquinol + 2 ferricytochrome c - Saccharomyces cerevisiae decylplastoquinone + 2 ferrocytochrome c + 2 H+ - ? 289170 7.1.1.8 decylplastoquinol + 2 ferricytochrome c - Bos taurus decylplastoquinone + 2 ferrocytochrome c + 2 H+ - ? 289170 7.1.1.8 decylubiquinol + 2 ferricytochrome c - Sus scrofa decylubiquinone + 2 ferrocytochrome c + 2 H+ - ? 426276 7.1.1.8 decylubiquinol + 2 ferricytochrome c - Saccharomyces cerevisiae decylubiquinone + 2 ferrocytochrome c + H+ [side 2] - ? 454114 7.1.1.8 decylubiquinol + ferricytochrome c - Saccharomyces cerevisiae decylubiquinone + ferrocytochrome c - ? 388504 7.1.1.8 decylubiquinol + ferricytochrome c horse heart cytochrome c, half of the center N sites was insensitive to decylubiquinol Saccharomyces cerevisiae decylubiquinone + ferrocytochrome c - ? 388504 7.1.1.8 dihydroubiquinone + ferricytochrome c - Bos taurus ubiquinone + ferrocytochrome c + 2 H+ - ? 289177 7.1.1.8 menaquinol + 2 ferricytochrome c - Saccharomyces cerevisiae menaquinone + 2 ferrocytochrome c + 2 H+ - ? 289171 7.1.1.8 menaquinol + 2 ferricytochrome c - Shewanella oneidensis menaquinone + 2 ferrocytochrome c + 2 H+ - ? 289171 7.1.1.8 additional information - Bos taurus ? - ? 89 7.1.1.8 additional information almost inert towards mammalian cytochrome c Spinacia oleracea ? - ? 89 7.1.1.8 additional information dihydroubiquinone-1 is not a suitable substrate, as it reacts nonenzymically with cytochrome c at a rapid rate Bos taurus ? - ? 89 7.1.1.8 additional information activity of enzyme complex III of the mitochondrial electron transport chain is essential for early heart muscle cell differentiation Mus musculus ? - ? 89 7.1.1.8 additional information enzyme complex III is part of the mitochondrial membrane electron transport chain Rattus norvegicus ? - ? 89 7.1.1.8 additional information enzyme is a central component of cellular energy conservation machinery Bos taurus ? - ? 89 7.1.1.8 additional information enzyme is part of the Knallgas reaction pathway Aquifex aeolicus ? - ? 89 7.1.1.8 additional information the Qo-cycle, overview Cereibacter sphaeroides ? - ? 89 7.1.1.8 additional information electron transfer takes place between the 2 cytochrome b subunits Saccharomyces cerevisiae ? - ? 89 7.1.1.8 additional information protonation reactions coupled to quinone binding, binding of 2.3-2.6 quinones per enzyme monomer at the Qo side, conformational changes Paracoccus denitrificans ? - ? 89 7.1.1.8 additional information the enzyme is a component of the multienzyme complex III Mus musculus ? - ? 89 7.1.1.8 additional information the enzyme is a component of the multienzyme complex III Bos taurus ? - ? 89 7.1.1.8 additional information the physiological impact of a mixed Q pool in RQ-producing organisms, overview Saccharomyces cerevisiae ? - ? 89 7.1.1.8 additional information model of half-of-the-sites activity in the dimeric cytochrome bc1 complex, overview Saccharomyces cerevisiae ? - ? 89 7.1.1.8 additional information substrate synthesis and substrate specificity, overview Saccharomyces cerevisiae ? - ? 89 7.1.1.8 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 Bos taurus ? - ? 89 7.1.1.8 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 Rhodobacter capsulatus ? - ? 89 7.1.1.8 additional information reaction mechanism of superoxide generation by bc1, overview Cereibacter sphaeroides ? - ? 89 7.1.1.8 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 Bos taurus ? - ? 89 7.1.1.8 naphthoquinol + 2 ferricytochrome c - Aquifex aeolicus naphthoquinone + 2 ferrocytochrome c + 2 H+ - ? 375196 7.1.1.8 naphthoquinol + 2 ferricytochrome c - Aquifex aeolicus naphthoquinone + 2 ferrocytochrome c + 2 H+ naphthoquinone is the pool quinone of the organism ? 375196 7.1.1.8 nonylubiquinol + 2 ferricytochrome c - Saccharomyces cerevisiae nonylubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289169 7.1.1.8 nonylubiquinol + 2 ferricytochrome c - Bos taurus nonylubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289169 7.1.1.8 plastohydroquinol + 2 ferricytochrome c - Saccharomyces cerevisiae plastohydroquinone + 2 ferrocytochrome c + 2 H+ - ? 289166 7.1.1.8 plastohydroquinol + 2 ferricytochrome c - Bos taurus plastohydroquinone + 2 ferrocytochrome c + 2 H+ - ? 289166 7.1.1.8 plastoquinol-1 + 2 ferricytochrome c - Cereibacter sphaeroides plastoquinone-1 + 2 ferrocytochrome c + 2 H+ - ? 289164 7.1.1.8 plastoquinol-9 + 2 ferricytochrome c - Cereibacter sphaeroides plastoquinone-9 + 2 ferrocytochrome c + 2 H+ - ? 289165 7.1.1.8 quinol + 2 ferricytochrome c - Mammalia quinone + 2 ferrocytochrome c + 2 H+ - ? 424987 7.1.1.8 quinol + 2 ferricytochrome c - Sus scrofa quinone + 2 ferrocytochrome c + 2 H+ - ? 424987 7.1.1.8 quinol + 2 ferricytochrome c - Bos taurus quinone + 2 ferrocytochrome c + 2 H+ - ? 424987 7.1.1.8 quinol + 2 ferricytochrome c - Cereibacter sphaeroides quinone + 2 ferrocytochrome c + 2 H+ - ? 424987 7.1.1.8 quinol + 2 ferricytochrome c - Homo sapiens quinone + 2 ferrocytochrome c + H+ - ? 440386 7.1.1.8 quinol + 2 ferricytochrome c - Cereibacter sphaeroides quinone + 2 ferrocytochrome c + H+ - ? 440386 7.1.1.8 quinol + 2 ferricytochrome c - Paracoccus denitrificans quinone + 2 ferrocytochrome c + H+ [side 2] - ? 454113 7.1.1.8 quinol + 2 ferricytochrome c1 - Paracoccus denitrificans quinone + 2 ferrocytochrome c1 + H+ [side 2] - ? 454112 7.1.1.8 quinol + 2 ferricytochrome c1 - Rhodobacter capsulatus quinone + 2 ferrocytochrome c1 + H+ [side 2] - ? 454112 7.1.1.8 quinol + 2 ferricytochrome c1 - Bacillus sp. (in: Bacteria) quinone + 2 ferrocytochrome c1 + H+ [side 2] - ? 454112 7.1.1.8 quinol + 2 ferricytochrome c1 - Rhodospirillum rubrum quinone + 2 ferrocytochrome c1 + H+ [side 2] - ? 454112 7.1.1.8 quinol + 2 ferricytochrome c1 - Trichormus variabilis quinone + 2 ferrocytochrome c1 + H+ [side 2] - ? 454112 7.1.1.8 quinol + 2 horse heart ferricytochrome c1 - Cereibacter sphaeroides quinone + 2 horse heart ferrocytochrome c1 + H+ [side 2] - ? 454111 7.1.1.8 rhodoquinol-3 + 2 ferricytochrome c a substrate-induced wQ-cycle bypass reaction leading to production of superoxide Saccharomyces cerevisiae rhodoquinone-3 + 2 ferrocytochrome c + 2 H+ i.e. 2-amino-5-farnesyl-3-methoxy-6-methyl-1,4-benzoquinone ? 389657 7.1.1.8 tetramethyl-p-benzoquinol + cytochrome c duroquinol Bos taurus tetramethyl-p-benzoquinone + reduced cytochrome c - ? 289172 7.1.1.8 ubideuteroquinol + cytochrome c - Saccharomyces cerevisiae ubideuteroquinone + reduced cytochrome c - ? 289168 7.1.1.8 ubideuteroquinol + cytochrome c - Bos taurus ubideuteroquinone + reduced cytochrome c - ? 289168 7.1.1.8 ubihydroquinol + cytochrome c - Saccharomyces cerevisiae ubihydroquinone + reduced cytochrome c - ? 289167 7.1.1.8 ubihydroquinol + cytochrome c - Bos taurus ubihydroquinone + reduced cytochrome c - ? 289167 7.1.1.8 ubiquinol + 2 4-carboxy-2,6-dinitrophenyllysine27-ferricytochrome c cytochrome c from horse, modified at Lys27 Bos taurus ubiquinone + 2 4-carboxy-2,6-dinitrophenyllysine27-ferrocytochrome c + 2 H+ - ? 289155 7.1.1.8 ubiquinol + 2 ferricyanide - Bos taurus ubiquinone + 2 ferrocyanide + 2 H+ - ? 427151 7.1.1.8 ubiquinol + 2 ferricyanide - Cereibacter sphaeroides ubiquinone + 2 ferrocyanide + 2 H+ - ? 427151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Gallus gallus ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Chlorobium limicola ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Paracoccus denitrificans ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Saccharomyces pastorianus ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Mammalia ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Tetradesmus obliquus ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Cyberlindnera jadinii ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Mus musculus ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Thermus thermophilus ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Homo sapiens ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Rattus norvegicus ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Sus scrofa ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Saccharomyces cerevisiae ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Bos taurus ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Euglena gracilis ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Neurospora crassa ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Cereibacter sphaeroides ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Ovis aries ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Bradyrhizobium japonicum ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Spinacia oleracea ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Solanum tuberosum ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Rubrivivax gelatinosus ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Rhodopseudomonas palustris ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Trypanosoma brucei ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Pseudomonas stutzeri ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Rhodobacter capsulatus ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Neisseria meningitidis ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Bacillus sp. (in: Bacteria) ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Leishmania tarentolae ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Helianthus tuberosus ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Rhodospirillum rubrum ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Allochromatium vinosum ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Trichormus variabilis ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Rhizobium phaseoli ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Nostoc sp. ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Alkalihalobacillus alcalophilus ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Magnetospirillum molischianum ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Chloroflexus aurantiacus ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Gallus sp. ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Columba sp. ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Blastochloris viridis ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Pseudomonas cichorii ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Heliobacterium chlorum ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Paramecium aurelia ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Fuscovulum blasticum ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Rhodovulum sulfidophilum ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Bos taurus ubiquinone + 2 ferrocytochrome c + 2 H+ interaction with ubiquinone at the QN site, overview ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c algal cytochrome c Spinacia oleracea ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c under physiological conditions, the dimeric cytochrome bc1 complex is suggested to be continually primed by prompt oxidation of membrane ubiquinol via center N yielding a bound semiquinone in this center and a reduced, high-potential heme b in the other monomer of the enzyme. Then the oxidation of each ubiquinol molecule in center P is followed by ubiquinol formation in center N, proton translocation and generation of membrane voltage Rhodobacter capsulatus ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c 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 Paracoccus denitrificans ubiquinone + 2 ferrocytochrome c + 2 H+ interaction with ubiquinone at the QN site, overview ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c 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 Cereibacter sphaeroides ubiquinone + 2 ferrocytochrome c + 2 H+ interaction with ubiquinone at the QN site, overview ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c 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 Rhodobacter capsulatus ubiquinone + 2 ferrocytochrome c + 2 H+ interaction with ubiquinone at the QN site, overview ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c 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 Gallus gallus ubiquinone + 2 ferrocytochrome c + 2 H+ interaction with ubiquinone at the QN site, overview ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c 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 Saccharomyces cerevisiae ubiquinone + 2 ferrocytochrome c + 2 H+ interaction with ubiquinone at the QN site, overview ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c 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 Bos taurus ubiquinone + 2 ferrocytochrome c + 2 H+ interaction with ubiquinone at the QN site, overview ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c 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 Spinacia oleracea ubiquinone + 2 ferrocytochrome c + 2 H+ interaction with ubiquinone at the QN site, overview ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Saccharomyces pastorianus NCYC74 ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Neurospora crassa SL 74OR23-1A FGSC No. 987 ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Rhodobacter capsulatus pMTO-404/MTRKB1 ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Rhodospirillum rubrum S1 ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Cereibacter sphaeroides BC17 ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Cereibacter sphaeroides GA ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Rhodopseudomonas palustris Morita ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Saccharomyces cerevisiae D 273-10B ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Saccharomyces cerevisiae DL1 ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Rhodobacter capsulatus SB1003 ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Cereibacter sphaeroides R-26 ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Neurospora crassa 74A ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Saccharomyces cerevisiae FL100 ubiquinone + 2 ferrocytochrome c + 2 H+ - ? 289151 7.1.1.8 ubiquinol + 2 ferricytochrome c - Homo sapiens ubiquinone + 2 ferrocytochrome c + 2 H+[side 2] - ? 453799 7.1.1.8 ubiquinol + 2 ferricytochrome c2 - Cereibacter sphaeroides ubiquinone + 2 ferrocytochrome c2 + 2 H+[side 2] - ? 453800 7.1.1.8 ubiquinol + 2 ferricytochrome c552 - Paracoccus denitrificans ubiquinone + 2 ferrocytochrome c552 + 2 H+ - ? 425066 7.1.1.8 ubiquinol + cytochrome c2 - Rhodopseudomonas palustris ubiquinone + reduced cytochrome c2 - ? 289152 7.1.1.8 ubiquinol + cytochrome c2 - Rhodopseudomonas palustris Morita ubiquinone + reduced cytochrome c2 - ? 289152 7.1.1.8 ubiquinol + ferricytochrome b-561 - Cereibacter sphaeroides ubiquinone + ferrocytochrome b-561 - ? 289156 7.1.1.8 ubiquinol + ferricytochrome b-561 - Cereibacter sphaeroides GA ubiquinone + ferrocytochrome b-561 - ? 289156 7.1.1.8 ubiquinol + ferricytochrome b-562 - Cereibacter sphaeroides ubiquinone + ferrocytochrome b-562 - ? 289157 7.1.1.8 ubiquinol + ferricytochrome c - Saccharomyces cerevisiae ubiquinone + ferrocytochrome c - ? 386729 7.1.1.8 ubiquinol + ferricytochrome 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 Saccharomyces cerevisiae ubiquinone + ferrocytochrome c - ? 386729 7.1.1.8 ubiquinol + ferricytochrome c - Plasmodium berghei ubiquinone + ferrocytochrome c + H+ - ? 440416 7.1.1.8 ubiquinol + ferricytochrome c - Shewanella oneidensis ubiquinone + ferrocytochrome c + H+ - ? 440416 7.1.1.8 ubiquinol + ferricytochrome c - Trichophyton mentagrophytes ubiquinone + ferrocytochrome c + H+ - ? 440416 7.1.1.8 ubiquinol + ferricytochrome c - Plasmodium berghei ANKA ubiquinone + ferrocytochrome c + H+ - ? 440416 7.1.1.8 ubiquinol + horse heart cytochrome c - Saccharomyces cerevisiae ? - ? 289154 7.1.1.8 ubiquinol + horse heart cytochrome c - Cereibacter sphaeroides ? - ? 289154 7.1.1.8 ubiquinol + horse heart cytochrome c - Rhodopseudomonas palustris ? - ? 289154 7.1.1.8 ubiquinol + horse heart cytochrome c - Cereibacter sphaeroides GA ? - ? 289154 7.1.1.8 ubiquinol + horse heart cytochrome c - Rhodopseudomonas palustris Morita ? - ? 289154 7.1.1.8 ubiquinol + horse heart cytochrome c - Cereibacter sphaeroides R-26 ? - ? 289154 7.1.1.8 ubiquinol + plastocyanin - Spinacia oleracea ? - ? 289153 7.1.1.8 ubiquinol 10 + cytochrome c - Bos taurus ubiquinone 10 + reduced cytochrome c - ? 289163 7.1.1.8 ubiquinol 10 + cytochrome c - Cereibacter sphaeroides ubiquinone 10 + reduced cytochrome c - ? 289163 7.1.1.8 ubiquinol 10 + cytochrome c - Cereibacter sphaeroides GA ubiquinone 10 + reduced cytochrome c - ? 289163 7.1.1.8 ubiquinol 10 + cytochrome c - Cereibacter sphaeroides R-26 ubiquinone 10 + reduced cytochrome c - ? 289163 7.1.1.8 ubiquinol 2 + cytochrome c - Saccharomyces cerevisiae ubiquinone 2 + reduced cytochrome c - ? 289159 7.1.1.8 ubiquinol 2 + cytochrome c - Bos taurus ubiquinone 2 + reduced cytochrome c - ? 289159 7.1.1.8 ubiquinol 2 + cytochrome c - Helianthus tuberosus ubiquinone 2 + reduced cytochrome c - ? 289159 7.1.1.8 ubiquinol 2 + cytochrome c - Saccharomyces cerevisiae D 273-10B ubiquinone 2 + reduced cytochrome c - ? 289159 7.1.1.8 ubiquinol 3 + cytochrome c - Bos taurus ubiquinone 3 + reduced cytochrome c - ? 289160 7.1.1.8 ubiquinol 4 + cytochrome c - Cereibacter sphaeroides ubiquinone 4 + reduced cytochrome c - ? 289161 7.1.1.8 ubiquinol 4 + cytochrome c - Cereibacter sphaeroides GA ubiquinone 4 + reduced cytochrome c - ? 289161 7.1.1.8 ubiquinol 9 + cytochrome c - Bos taurus ubiquinone 9 + reduced cytochrome c - ? 289162 7.1.1.8 ubiquinol 9 + cytochrome c - Neurospora crassa ubiquinone 9 + reduced cytochrome c - ? 289162 7.1.1.8 ubiquinol 9 + cytochrome c - Cereibacter sphaeroides ubiquinone 9 + reduced cytochrome c - ? 289162 7.1.1.8 ubiquinol 9 + cytochrome c - Cereibacter sphaeroides GA ubiquinone 9 + reduced cytochrome c - ? 289162 7.1.1.8 ubiquinol-1 + cytochrome c - Saccharomyces cerevisiae ubiquinone-1 + reduced cytochrome c - ? 289158 7.1.1.8 ubiquinol-1 + cytochrome c - Bos taurus ubiquinone-1 + reduced cytochrome c - ? 289158 7.1.1.8 ubiquinol-1 + cytochrome c - Cereibacter sphaeroides ubiquinone-1 + reduced cytochrome c - ? 289158 7.1.1.8 ubiquinol-1 + cytochrome c - Cereibacter sphaeroides GA ubiquinone-1 + reduced cytochrome c - ? 289158 7.1.1.8 ubiquinol-1 + cytochrome c - Saccharomyces cerevisiae D 273-10B ubiquinone-1 + reduced cytochrome c - ? 289158 7.1.1.8 ubiquinol-2 + 2 ferricytochrome c - Paracoccus denitrificans ubiquinone-2 + 2 ferrocytochrome c + 2 H+ - ? 375266 7.1.1.8 ubiquinol-2 + 2 ferricytochrome c - Mus musculus ubiquinone-2 + 2 ferrocytochrome c + 2 H+ - ? 375266 7.1.1.8 ubiquinol-2 + 2 ferricytochrome c - Saccharomyces cerevisiae ubiquinone-2 + 2 ferrocytochrome c + 2 H+ - ? 375266 7.1.1.8 ubiquinol-2 + 2 ferricytochrome c - Saccharomyces cerevisiae ubiquinone-2 + 2 ferrocytochrome c + 2 H+ - r 375266 7.1.1.8 ubiquinol-2 + 2 ferricytochrome c - Bos taurus ubiquinone-2 + 2 ferrocytochrome c + 2 H+ - ? 375266 7.1.1.8 ubiquinol-2 + 2 ferricytochrome c electron transfer between yeast cytochrome bc1 complex and cytochrome c is coupled to proton transport across the inner mitochondrial membrane delivering a membrane potential, enzyme complex is important in cell respiration and photosynthesis Saccharomyces cerevisiae ubiquinone-2 + 2 ferrocytochrome c + 2 H+ - ? 375266 7.1.1.8 ubiquinol-2 + 2 ferricytochrome c enzyme catalyzes the electron transfer from a quinol molecule to cytochrome c, and concomitantly translocates protons across membranes for ATP synthesis and various cellular processes Bos taurus ubiquinone-2 + 2 ferrocytochrome c + 2 H+ - ? 375266 7.1.1.8 ubiquinol-2 + 2 ferricytochrome c enzyme complex is essentially involved in the mitochondrial respiratory electron transfer chain Saccharomyces cerevisiae ubiquinone-2 + 2 ferrocytochrome c + 2 H+ - ? 375266 7.1.1.8 ubiquinol-2 + 2 ferricytochrome c proton-coupled electron transfer at the Qo-site of the bc1 complex controls the rate of ubihydroquinone oxidation Cereibacter sphaeroides ubiquinone-2 + 2 ferrocytochrome c + 2 H+ - ? 375266 7.1.1.8 ubiquinol-2 + 2 ferricytochrome c ubiquinol oxidation is part of the protonmotive Q cycle mechanism, overview, half-of-the sites mechanism with reciprocal control between high potential and low potential redox components involved in ubiquinol oxidation Saccharomyces cerevisiae ubiquinone-2 + 2 ferrocytochrome c + 2 H+ - ? 375266 7.1.1.8 ubiquinol-2 + 2 ferricytochrome c activity is highest near physiological ionic strength and decreases at higher concentrations Saccharomyces cerevisiae ubiquinone-2 + 2 ferrocytochrome c + 2 H+ - ? 375266 7.1.1.8 ubiquinol-2 + 2 ferricytochrome c anti-cooperative oxidation of ubiquinol, reversible partial reaction Saccharomyces cerevisiae ubiquinone-2 + 2 ferrocytochrome c + 2 H+ - ? 375266 7.1.1.8 ubiquinol-2 + 2 ferricytochrome c binding interaction of ubiquinone with cytochrome b, overview Bos taurus ubiquinone-2 + 2 ferrocytochrome c + 2 H+ - ? 375266 7.1.1.8 ubiquinol-2 + 2 ferricytochrome c rate-limiting is the transfer of the first electron from ubiquinol to the [2Fe-2S] cluster of the Rieske iron-sulfur-protein at the Qo-side, reaction energy profile Cereibacter sphaeroides ubiquinone-2 + 2 ferrocytochrome c + 2 H+ - ? 375266 7.1.1.8 ubiquinol-2 + 2 ferricytochrome c ubiquinol binds to the specific binding pocket of the cytochrome bc1 complex Saccharomyces cerevisiae ubiquinone-2 + 2 ferrocytochrome c + 2 H+ - ? 375266 7.1.1.8 ubiquinol-2 + ferricytochrome c the cytochrome bc1 complex is the central segment of the respiratory chain in mitochondria Bos taurus ubiquinone-2 + ferrocytochrome c - ? 375336 7.1.1.8 ubiquinol-2 + ferricytochrome 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 Bos taurus ubiquinone-2 + ferrocytochrome c - ? 375336 7.1.1.8 ubiquinone-10 + ferricytochrome c - Paracoccus denitrificans ubiquinol-10 + ferrocytochrome c + 2 H+ - ? 370274 7.1.1.8 ubiquinone-10 + ferricytochrome c - Cyberlindnera jadinii ubiquinol-10 + ferrocytochrome c + 2 H+ - ? 370274 7.1.1.8 ubiquinone-10 + ferricytochrome c - Homo sapiens ubiquinol-10 + ferrocytochrome c + 2 H+ - ? 370274 7.1.1.8 ubiquinone-10 + ferricytochrome c - Rattus norvegicus ubiquinol-10 + ferrocytochrome c + 2 H+ - ? 370274 7.1.1.8 ubiquinone-10 + ferricytochrome c - Saccharomyces cerevisiae ubiquinol-10 + ferrocytochrome c + 2 H+ - ? 370274 7.1.1.8 ubiquinone-10 + ferricytochrome c - Bos taurus ubiquinol-10 + ferrocytochrome c + 2 H+ - ? 370274 7.1.1.8 ubiquinone-10 + ferricytochrome c - Neurospora crassa ubiquinol-10 + ferrocytochrome c + 2 H+ - ? 370274 7.1.1.8 ubiquinone-10 + ferricytochrome c - Cereibacter sphaeroides ubiquinol-10 + ferrocytochrome c + 2 H+ - ? 370274 7.1.1.8 ubiquinone-10 + ferricytochrome c - Spinacia oleracea ubiquinol-10 + ferrocytochrome c + 2 H+ - ? 370274 7.1.1.8 ubiquinone-10 + ferricytochrome c - Rhodopseudomonas palustris ubiquinol-10 + ferrocytochrome c + 2 H+ - ? 370274 7.1.1.8 ubiquinone-10 + ferricytochrome c - Rhodobacter capsulatus ubiquinol-10 + ferrocytochrome c + 2 H+ - ? 370274 7.1.1.8 ubiquinone-10 + ferricytochrome c - Bacillus sp. (in: Bacteria) ubiquinol-10 + ferrocytochrome c + 2 H+ - ? 370274 7.1.1.8 ubiquinone-10 + ferricytochrome c - Rhodospirillum rubrum ubiquinol-10 + ferrocytochrome c + 2 H+ - ? 370274 7.1.1.8 ubiquinone-10 + ferricytochrome c - Trichormus variabilis ubiquinol-10 + ferrocytochrome c + 2 H+ - ? 370274 7.1.1.8 ubiquinone-10 + ferricytochrome c - Columba sp. ubiquinol-10 + ferrocytochrome c + 2 H+ - ? 370274 7.1.1.8 ubiquinone-10 + ferricytochrome c - Rhodospirillum rubrum S1 ubiquinol-10 + ferrocytochrome c + 2 H+ - ? 370274 7.1.1.8 ubiquinone-10 + ferricytochrome c - Cereibacter sphaeroides GA ubiquinol-10 + ferrocytochrome c + 2 H+ - ? 370274 7.1.1.8 ubiquinone-10 + ferricytochrome c - Rhodopseudomonas palustris Morita ubiquinol-10 + ferrocytochrome c + 2 H+ - ? 370274 7.1.1.8 ubiquinone-10 + ferricytochrome c - Cereibacter sphaeroides R-26 ubiquinol-10 + ferrocytochrome c + 2 H+ - ? 370274