Biology:Ubiquinol oxidase (H+-transporting)

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Ubiquinol oxidase (H+-transporting)
Identifiers
EC number7.1.1.3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB 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 [math]\displaystyle{ \rightleftharpoons }[/math] 2 ubiquinone + 2 H2O + n H+out

Ubiquinol oxidase contains a dinuclear centre comprising two hemes, or heme and copper.

References

  1. "The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site". Nature Structural Biology 7 (10): 910–7. October 2000. doi:10.1038/82824. PMID 11017202. 
  2. "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. March 2005. doi:10.1073/pnas.0405683102. PMID 15728392. Bibcode2005PNAS..102.3657B. 
  3. "The quinone-binding sites of the cytochrome bo3 ubiquinol oxidase from Escherichia coli". Biochimica et Biophysica Acta (BBA) - Bioenergetics 1797 (12): 1924–32. December 2010. doi:10.1016/j.bbabio.2010.04.011. PMID 20416270. 
  4. "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. June 2010. doi:10.1074/jbc.M110.118448. PMID 20392690. 

External links