ExplorEnz: EC 7.1.1.3

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7.1.1.3

Accepted name:

ubiquinol oxidase (H⁺-transporting)

Reaction:

2 ubiquinol + O₂ + n H⁺_{[side 1]} = 2 ubiquinone + 2 H₂O + n H⁺_{[side 2]}

Other name(s):

cyoABCD (gene names); cytochrome bo₃ oxidase; cytochrome bb₃ oxidase; cytochrome bo oxidase; ubiquinol:O₂ oxidoreductase (H⁺-transporting)

Systematic name:

ubiquinol:oxygen oxidoreductase (H⁺-transporting)

Comments:

Contains a dinuclear centre comprising two hemes, or heme and copper. This terminal oxidase enzyme generates proton motive force by two mechanisms: (1) transmembrane charge separation resulting from utilizing protons and electrons originating from opposite sides of the membrane to generate water, and (2) active pumping of protons across the membrane. The bioenergetic efficiency (the number of charges driven across the membrane per electron used to reduce oxygen to water) depends on the enzyme; for example, for the bo₃ oxidase it is 2. cf. EC 7.1.1.7, ubiquinol oxidase ubiquinol oxidase (electrogenic, proton-motive force generating).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Abramson, J., Riistama, S., Larsson, G., Jasaitis, A., Svensson-Ek, M., Laakkonen, L., Puustinen, A., Iwata, S. and Wikstrom, M. The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site. Nat. Struct. Biol. 7 (2000) 910–917. [DOI] [PMID: 11017202]
2.	Stenberg, F., von Heijne, G. and Daley, D.O. Assembly of the cytochrome bo₃ complex. J. Mol. Biol. 371 (2007) 765–773. [PMID: 17583738]
3.	Yap, L.L., Lin, M.T., Ouyang, H., Samoilova, R.I., Dikanov, S.A. and Gennis, R.B. The quinone-binding sites of the cytochrome bo₃ ubiquinol oxidase from Escherichia coli. Biochim. Biophys. Acta 1797 (2010) 1924–1932. [DOI] [PMID: 20416270]
4.	Choi, S.K., Lin, M.T., Ouyang, H. and Gennis, R.B. Searching for the low affinity ubiquinone binding site in cytochrome bo₃ from Escherichia coli. Biochim Biophys Acta Bioenerg 1858 (2017) 366–370. [PMID: 28235459]
5.	Choi, S.K., Schurig-Briccio, L., Ding, Z., Hong, S., Sun, C. and Gennis, R.B. Location of the Substrate Binding Site of the Cytochrome bo₃ Ubiquinol Oxidase from Escherichia coli. J. Am. Chem. Soc. 139 (2017) 8346–8354. [PMID: 28538096]

[EC 7.1.1.3 created 2011 as EC 1.10.3.10, modified 2014, transferred 2018 to EC 7.1.1.3]