Ubiquinol oxidase (H+-transporting)
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 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. 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
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