Ubiquinol oxidase (H+-transporting)

Ubiquinol oxidase (H+-transporting)
Identifiers
EC number 1.10.3.10
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 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+in \rightleftharpoons 2 ubiquinone + 2 H2O + n H+out

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

References

  1. Abramson, J., Riistama, S., Larsson, G., Jasaitis, A., Svensson-Ek, M., Laakkonen, L., Puustinen, A., Iwata, S. and Wikstrom, M. (2000). "The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site". Nat. Struct. Biol. 7: 910–917. doi:10.1038/82824. PMID 11017202.
  2. Belevich, I., Borisov, V.B., Zhang, J., Yang, K., Konstantinov, A.A., Gennis, R.B. and Verkhovsky, M.I. (2005). "Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electron-proton coupling in the di-heme active site". Proc. Natl. Acad. Sci. USA 102 (10): 3657–3662. doi:10.1073/pnas.0405683102. PMC 553295. PMID 15728392.
  3. Yap, L.L., Lin, M.T., Ouyang, H., Samoilova, R.I., Dikanov, S.A. and Gennis, R.B. (2010). "The quinone-binding sites of the cytochrome bo3 ubiquinol oxidase from Escherichia coli". Biochim. Biophys. Acta 1797 (12): 1924–1932. doi:10.1016/j.bbabio.2010.04.011. PMC 2922442. PMID 20416270.
  4. Shepherd, M., Sanguinetti, G., Cook, G.M. and Poole, R.K. (2010). "Compensations for diminished terminal oxidase activity in Escherichia coli: cytochrome bd-II-mediated respiration and glutamate metabolism". J. Biol. Chem. 285 (24): 18464–18472. doi:10.1074/jbc.M110.118448. PMC 2881772. PMID 20392690.

External links

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