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MetaCyc Reaction: 1.10.2.2

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical ReactionsComposite ReactionsElectron-Transfer-Reactions
Reactions Classified By Conversion TypeSimple ReactionsChemical ReactionsProtein-Modification Reactions
Reactions Classified By SubstrateMacromolecule ReactionsProtein-ReactionsProtein-Modification Reactions

EC Number: 1.10.2.2

Enzymes and Genes:

Arabidopsis thaliana col: ubiquinol-cytochrome c oxidoreductaseTraceable author statement to experimental support: at3g16480, at1g51980, at3g02090, at3g27240, at5g40810, at5g13440
Nitrosomonas europaea: cytochrome cm552Inferred from experiment: cycB
Saccharomyces cerevisiae: ubiquinol-cytochrome C oxidoreductase: QCR10

In Pathway: ammonia oxidation IV (autotrophic ammonia oxidizers), aerobic respiration II (cytochrome c) (yeast), aerobic respiration I (cytochrome c)

Note that this reaction equation differs from the official Enzyme Commission reaction equation for this EC number, which can be found here .

Transport reaction diagram

Reaction Locations: mitochondrial inner membrane, inner membrane (sensu Gram-negative Bacteria)

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Enzyme Commission Primary Name: quinol—cytochrome-c reductase

Enzyme Commission Synonyms: ubiquinol-cytochrome-c reductase, coenzyme Q-cytochrome c reductase, dihydrocoenzyme Q-cytochrome c reductase, reduced ubiquinone-cytochrome c reductase, complex III (mitochondrial electron transport), ubiquinone-cytochrome c reductase, ubiquinol-cytochrome c oxidoreductase, reduced coenzyme Q-cytochrome c reductase, ubiquinone-cytochrome c oxidoreductase, reduced ubiquinone-cytochrome c oxidoreductase, mitochondrial electron transport complex III, ubiquinol-cytochrome c-2 oxidoreductase, ubiquinone-cytochrome b-c1 oxidoreductase, ubiquinol-cytochrome c2 reductase, ubiquinol-cytochrome c1 oxidoreductase, CoQH2-cytochrome c oxidoreductase, ubihydroquinol:cytochrome c oxidoreductase, coenzyme QH2-cytochrome c reductase, QH2:cytochrome c oxidoreductase, ubiquinol:ferricytochrome-c oxidoreductase

Standard Gibbs Free Energy (ΔrG in kcal/mol): -23.014221Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
Contains cytochromes b-562, b-566 and c1, and a 2-iron ferredoxin. Depending on the organism and physiological conditions, either two or four protons are extruded from the cytoplasmic to the non-cytoplasmic compartment (cf. EC 1.6.99.3 NADH dehydrogenase).

Citations: [Marres77, Rieske76, Wikstrom81]

Gene-Reaction Schematic

Gene-Reaction Schematic

Relationship Links: BRENDA:EC:1.10.2.2, ENZYME:EC:1.10.2.2, IUBMB-ExplorEnz:EC:1.10.2.2, UniProt:RELATED-TO:O03176, UniProt:RELATED-TO:O03548, UniProt:RELATED-TO:O21291, UniProt:RELATED-TO:O21337, UniProt:RELATED-TO:O26064, UniProt:RELATED-TO:O26065, UniProt:RELATED-TO:O44512, UniProt:RELATED-TO:O47499, UniProt:RELATED-TO:O47545, UniProt:RELATED-TO:O47575, UniProt:RELATED-TO:O47878, UniProt:RELATED-TO:O54070, UniProt:RELATED-TO:O63585, UniProt:RELATED-TO:O63621, UniProt:RELATED-TO:O63748, UniProt:RELATED-TO:O63910, UniProt:RELATED-TO:O66459, UniProt:RELATED-TO:O66460, UniProt:RELATED-TO:O79386, UniProt:RELATED-TO:O79413, UniProt:RELATED-TO:O79558, UniProt:RELATED-TO:O79571, UniProt:RELATED-TO:O79680, UniProt:RELATED-TO:O79715, UniProt:RELATED-TO:O79717, UniProt:RELATED-TO:O97134, UniProt:RELATED-TO:O99606, UniProt:RELATED-TO:O99815, UniProt:RELATED-TO:O99828, UniProt:RELATED-TO:O99971, UniProt:RELATED-TO:P00125, UniProt:RELATED-TO:P00126, UniProt:RELATED-TO:P00127, UniProt:RELATED-TO:P00128, UniProt:RELATED-TO:P00130, UniProt:RELATED-TO:P00157, UniProt:RELATED-TO:P00158, UniProt:RELATED-TO:P00159, UniProt:RELATED-TO:P00160, UniProt:RELATED-TO:P00161, UniProt:RELATED-TO:P00162, UniProt:RELATED-TO:P00163, UniProt:RELATED-TO:P00164, UniProt:RELATED-TO:P04165, UniProt:RELATED-TO:P05417, UniProt:RELATED-TO:P05418, UniProt:RELATED-TO:P05718, UniProt:RELATED-TO:P07056, UniProt:RELATED-TO:P07142, UniProt:RELATED-TO:P07143, UniProt:RELATED-TO:P07256, UniProt:RELATED-TO:P07257, UniProt:RELATED-TO:P07704, UniProt:RELATED-TO:P07747, UniProt:RELATED-TO:P07919, UniProt:RELATED-TO:P08067, UniProt:RELATED-TO:P08500, UniProt:RELATED-TO:P08501, UniProt:RELATED-TO:P08502, UniProt:RELATED-TO:P08525, UniProt:RELATED-TO:P08574, UniProt:RELATED-TO:P09843, UniProt:RELATED-TO:P11669, UniProt:RELATED-TO:P12778, UniProt:RELATED-TO:P13271, UniProt:RELATED-TO:P13272, UniProt:RELATED-TO:P13627, UniProt:RELATED-TO:P14548, UniProt:RELATED-TO:P15547, UniProt:RELATED-TO:P15585, UniProt:RELATED-TO:P16357, UniProt:RELATED-TO:P16358, UniProt:RELATED-TO:P16359, UniProt:RELATED-TO:P16360, UniProt:RELATED-TO:P16363, UniProt:RELATED-TO:P16364, UniProt:RELATED-TO:P16366, UniProt:RELATED-TO:P16367, UniProt:RELATED-TO:P16536, UniProt:RELATED-TO:P18935, UniProt:RELATED-TO:P18946, UniProt:RELATED-TO:P20114, UniProt:RELATED-TO:P20788, UniProt:RELATED-TO:P21713, UniProt:RELATED-TO:P21714, UniProt:RELATED-TO:P21715, UniProt:RELATED-TO:P21716, UniProt:RELATED-TO:P21717, UniProt:RELATED-TO:P21718, UniProt:RELATED-TO:P21719, UniProt:RELATED-TO:P21720, UniProt:RELATED-TO:P21721, UniProt:RELATED-TO:P21722, UniProt:RELATED-TO:P21723, UniProt:RELATED-TO:P22289, UniProt:RELATED-TO:P22695, UniProt:RELATED-TO:P23004, UniProt:RELATED-TO:P23134, UniProt:RELATED-TO:P23135, UniProt:RELATED-TO:P23136, UniProt:RELATED-TO:P23663, UniProt:RELATED-TO:P24878, UniProt:RELATED-TO:P24890, UniProt:RELATED-TO:P24950, UniProt:RELATED-TO:P24951, UniProt:RELATED-TO:P24952, UniProt:RELATED-TO:P24953, UniProt:RELATED-TO:P24954, UniProt:RELATED-TO:P24955, UniProt:RELATED-TO:P24956, UniProt:RELATED-TO:P24957, UniProt:RELATED-TO:P24958, UniProt:RELATED-TO:P24959, UniProt:RELATED-TO:P24960, UniProt:RELATED-TO:P24962, UniProt:RELATED-TO:P24964, UniProt:RELATED-TO:P24965, UniProt:RELATED-TO:P24966, UniProt:RELATED-TO:P24992, UniProt:RELATED-TO:P25076, UniProt:RELATED-TO:P26852, UniProt:RELATED-TO:P29630, UniProt:RELATED-TO:P29631, UniProt:RELATED-TO:P29632, UniProt:RELATED-TO:P29633, UniProt:RELATED-TO:P29634, UniProt:RELATED-TO:P29635, UniProt:RELATED-TO:P29636, UniProt:RELATED-TO:P29637, UniProt:RELATED-TO:P29638, UniProt:RELATED-TO:P29639, UniProt:RELATED-TO:P29640, UniProt:RELATED-TO:P29641, UniProt:RELATED-TO:P29757, UniProt:RELATED-TO:P31800, UniProt:RELATED-TO:P31930, UniProt:RELATED-TO:P32551, UniProt:RELATED-TO:P34197, UniProt:RELATED-TO:P34844, UniProt:RELATED-TO:P34845, UniProt:RELATED-TO:P34861, UniProt:RELATED-TO:P34863, UniProt:RELATED-TO:P37299, UniProt:RELATED-TO:P37841, UniProt:RELATED-TO:P38593, UniProt:RELATED-TO:P38594, UniProt:RELATED-TO:P41280 ... [212 more not displayed]

Credits:
Revised 26-Jul-2012 by Caspi R, SRI International


References

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Marres77: Marres CM, Slater EC (1977). "Polypeptide composition of purified QH2:cytochrome c oxidoreductase from beef-heart mitochondria." Biochim Biophys Acta 462(3);531-48. PMID: 597492

Rieske76: Rieske JS (1976). "Composition, structure, and function of complex III of the respiratory chain." Biochim Biophys Acta 456(2);195-247. PMID: 788795

Wikstrom81: Wikstrom M, Krab K, Saraste M (1981). "Proton-translocating cytochrome complexes." Annu Rev Biochem 50;623-55. PMID: 6267990


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by Pathway Tools version 19.5 (software by SRI International) on Tue May 3, 2016, biocyc14.