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| Name = Ubiquinol oxidase (H+-transporting)
| EC_number = 1.10.3.10
| CAS_number =
| IUBMB_EC_number = 1/10/3/10
| GO_code =
| image =
| width =
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}}Ubiquinol oxidase (H+-transporting) ({{EC number|1.10.3.10}}, cytochrome bb3 oxidase, cytochrome bo oxidase, cytochrome bd-I oxidase) is an enzyme with systematic name ubiquinol:O2 oxidoreductase (H+-transporting).[1][2][3][4] This enzyme catalyses the following chemical reaction
2 ubiquinol + O2 + n H+in2 ubiquinone + 2 H2O + n H+out
Ubiquinol oxidase contains a dinuclear centre comprising two hemes, or heme and copper.
References
1. ^{{cite journal | vauthors = Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, Wikström M | title = The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site | journal = Nature Structural Biology | volume = 7 | issue = 10 | pages = 910–7 | date = October 2000 | pmid = 11017202 | doi = 10.1038/82824 }}
2. ^{{cite journal | vauthors = Belevich I, Borisov VB, Zhang J, Yang K, Konstantinov AA, Gennis RB, Verkhovsky MI | title = Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electron-proton coupling in the di-heme active site | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 102 | issue = 10 | pages = 3657–62 | date = March 2005 | pmid = 15728392 | pmc = 553295 | doi = 10.1073/pnas.0405683102 }}
3. ^{{cite journal | vauthors = Yap LL, Lin MT, Ouyang H, Samoilova RI, Dikanov SA, Gennis RB | title = The quinone-binding sites of the cytochrome bo3 ubiquinol oxidase from Escherichia coli | journal = Biochimica et Biophysica Acta | volume = 1797 | issue = 12 | pages = 1924–32 | date = December 2010 | pmid = 20416270 | pmc = 2922442 | doi = 10.1016/j.bbabio.2010.04.011 }}
4. ^{{cite journal | vauthors = Shepherd M, Sanguinetti G, Cook GM, Poole RK | title = Compensations for diminished terminal oxidase activity in Escherichia coli: cytochrome bd-II-mediated respiration and glutamate metabolism | journal = The Journal of Biological Chemistry | volume = 285 | issue = 24 | pages = 18464–72 | date = June 2010 | pmid = 20392690 | pmc = 2881772 | doi = 10.1074/jbc.M110.118448 }}
2. ^{{cite journal | vauthors = Belevich I, Borisov VB, Zhang J, Yang K, Konstantinov AA, Gennis RB, Verkhovsky MI | title = Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electron-proton coupling in the di-heme active site | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 102 | issue = 10 | pages = 3657–62 | date = March 2005 | pmid = 15728392 | pmc = 553295 | doi = 10.1073/pnas.0405683102 }}
3. ^{{cite journal | vauthors = Yap LL, Lin MT, Ouyang H, Samoilova RI, Dikanov SA, Gennis RB | title = The quinone-binding sites of the cytochrome bo3 ubiquinol oxidase from Escherichia coli | journal = Biochimica et Biophysica Acta | volume = 1797 | issue = 12 | pages = 1924–32 | date = December 2010 | pmid = 20416270 | pmc = 2922442 | doi = 10.1016/j.bbabio.2010.04.011 }}
4. ^{{cite journal | vauthors = Shepherd M, Sanguinetti G, Cook GM, Poole RK | title = Compensations for diminished terminal oxidase activity in Escherichia coli: cytochrome bd-II-mediated respiration and glutamate metabolism | journal = The Journal of Biological Chemistry | volume = 285 | issue = 24 | pages = 18464–72 | date = June 2010 | pmid = 20392690 | pmc = 2881772 | doi = 10.1074/jbc.M110.118448 }}
External links
- {{MeshName|Ubiquinol+oxidase+(H+-transporting)}}
1 : EC 1.10.3