| Ubiquinol oxidase (H+-transporting) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 7.1.1.3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Ubiquinol oxidase (H+-transporting) ( EC 7.1.1.3, 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+in 2 ubiquinone + 2 H2O + n H+out
Ubiquinol oxidase contains a dinuclear centre comprising two hemes, or heme and copper.
References
- ^ Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, Wikström M (October 2000). "The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site". Nature Structural Biology. 7 (10): 910–7. doi: 10.1038/82824. PMID 11017202. S2CID 6300175.
- ^ Belevich I, Borisov VB, Zhang J, Yang K, Konstantinov AA, Gennis RB, Verkhovsky MI (March 2005). "Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electron-proton coupling in the di-heme active site". Proceedings of the National Academy of Sciences of the United States of America. 102 (10): 3657–62. Bibcode: 2005PNAS..102.3657B. doi: 10.1073/pnas.0405683102. PMC 553295. PMID 15728392.
- ^ Yap LL, Lin MT, Ouyang H, Samoilova RI, Dikanov SA, Gennis RB (December 2010). "The quinone-binding sites of the cytochrome bo3 ubiquinol oxidase from Escherichia coli". Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1797 (12): 1924–32. doi: 10.1016/j.bbabio.2010.04.011. PMC 2922442. PMID 20416270.
- ^ Shepherd M, Sanguinetti G, Cook GM, Poole RK (June 2010). "Compensations for diminished terminal oxidase activity in Escherichia coli: cytochrome bd-II-mediated respiration and glutamate metabolism". The Journal of Biological Chemistry. 285 (24): 18464–72. doi: 10.1074/jbc.M110.118448. PMC 2881772. PMID 20392690.
External links
- Ubiquinol+oxidase+(H+-transporting) at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
| Ubiquinol oxidase (H+-transporting) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 7.1.1.3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Ubiquinol oxidase (H+-transporting) ( EC 7.1.1.3, 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+in 2 ubiquinone + 2 H2O + n H+out
Ubiquinol oxidase contains a dinuclear centre comprising two hemes, or heme and copper.
References
- ^ Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, Wikström M (October 2000). "The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site". Nature Structural Biology. 7 (10): 910–7. doi: 10.1038/82824. PMID 11017202. S2CID 6300175.
- ^ Belevich I, Borisov VB, Zhang J, Yang K, Konstantinov AA, Gennis RB, Verkhovsky MI (March 2005). "Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electron-proton coupling in the di-heme active site". Proceedings of the National Academy of Sciences of the United States of America. 102 (10): 3657–62. Bibcode: 2005PNAS..102.3657B. doi: 10.1073/pnas.0405683102. PMC 553295. PMID 15728392.
- ^ Yap LL, Lin MT, Ouyang H, Samoilova RI, Dikanov SA, Gennis RB (December 2010). "The quinone-binding sites of the cytochrome bo3 ubiquinol oxidase from Escherichia coli". Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1797 (12): 1924–32. doi: 10.1016/j.bbabio.2010.04.011. PMC 2922442. PMID 20416270.
- ^ Shepherd M, Sanguinetti G, Cook GM, Poole RK (June 2010). "Compensations for diminished terminal oxidase activity in Escherichia coli: cytochrome bd-II-mediated respiration and glutamate metabolism". The Journal of Biological Chemistry. 285 (24): 18464–72. doi: 10.1074/jbc.M110.118448. PMC 2881772. PMID 20392690.
External links
- Ubiquinol+oxidase+(H+-transporting) at the U.S. National Library of Medicine Medical Subject Headings (MeSH)