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EC 1.10.3.10 Details

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EC number

1.10.3.10

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)

cytochrome bb₃ oxidase, cytochrome bo oxidase, cytochrome bd-II oxidase, ubiquinol:O₂ oxidoreductase (H⁺-transporting)

Systematic name

ubiquinol:oxygen oxidoreductase (H⁺-transporting)

Comment

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, while for the bd-II oxidase it is 1. cf. EC 1.10.3.14, ubiquinol oxidase (electrogenic, non H⁺-transporting).

History

created 2011, modified 2014, deleted 2018

EC Tree

1 Oxidoreductases

1.1 Acting on the CH-OH group of donors

1.2 Acting on the aldehyde or oxo group of donors

1.3 Acting on the CH-CH group of donors

1.4 Acting on the CH-NH₂ group of donors

1.5 Acting on the CH-NH group of donors

1.6 Acting on NADH or NADPH

1.7 Acting on other nitrogenous compounds as donors

1.8 Acting on a sulfur group of donors

1.9 Acting on a heme group of donors

1.10 Acting on diphenols and related substances as donors

1.11 Acting on a peroxide as acceptor

1.12 Acting on hydrogen as donor

1.12.1 With NAD⁺ or NADP⁺ as acceptor

1.12.1.1 created 1965, deleted 1972

1.12.1.2 hydrogen dehydrogenase

1.12.1.3 hydrogen dehydrogenase (NADP⁺)

1.12.1.4 hydrogenase (NAD⁺, ferredoxin)

1.12.1.5 hydrogen dehydrogenase [NAD(P)⁺]

1.12.2 With a cytochrome as acceptor

1.12.5 With a quinone or similar compound as acceptor

1.12.7 With an iron-sulfur protein as acceptor

1.12.98 With other, known, physiological acceptors

1.12.99 With unknown physiological acceptors

1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)

1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

1.15 Acting on superoxide as acceptor

1.16 Oxidizing metal ions

1.17 Acting on CH or CH₂ groups

1.17.1 With NAD⁺ or NADP⁺ as acceptor

1.17.2 With a cytochrome as acceptor

1.17.3 With oxygen as acceptor

1.17.4 With a disulfide as acceptor

1.17.5 With a quinone or similar compound as acceptor

1.17.7 With an iron-sulfur protein as acceptor

1.17.8 With a flavin as acceptor

1.17.9 With a copper protein as acceptor

1.17.98 With other, known, physiological acceptors

1.17.99 With unknown physiological acceptors

1.18 Acting on iron-sulfur proteins as donors

1.19 Acting on reduced flavodoxin as donor

1.20 Acting on phosphorus or arsenic in donors

1.21 Catalysing the reaction X-H + Y-H = X-Y

1.22 Acting on halogen in donors

1.23 Reducing C-O-C group as acceptor

1.97 Other oxidoreductases

1.98 Enzymes using H₂ as reductant (deleted subclass)

1.99 Other enzymes using O₂ as oxidant (deleted subclass)