ubiquinol oxidase (H+-transporting) EC#: 7.1.1.3

Product Name ubiquinol oxidase (H+-transporting)
Example Structure Example Structure of ubiquinol oxidase (H+-transporting) EC#: 7.1.1.3
Synonyms appB, AppBC, appC, bd-type quinol oxidase, bo-type ubiquinol oxidase, CydA, CydAB, CydB, CydX, cyoA, cyoB, cyoC, cyoD, cyt bo3, Cyt-bo3, cytochrome bd, cytochrome bd menaquinol oxidase, cytochrome bd oxidase, cytochrome bd ubiquinol oxidase, cytochrome bd-I oxidase, cytochrome bd-I quinol oxidase, cytochrome bd-II oxidase, cytochrome bd-II quinol oxidase, cytochrome bd-II ubiquinol oxidase, cytochrome bd-type menaquinol oxidase, cytochrome bd-type quinol oxidase, cytochrome bo, cytochrome bo oxidase, cytochrome bo quinol oxidase, cytochrome bo terminal oxidase, cytochrome bo ubiquinol oxidase, cytochrome bo(3) ubiquinol oxidase, cytochrome bo-type ubiquinol oxidase, cytochrome bo3, cytochrome bo3 oxidase, cytochrome bo3 ubiquinol oxidase, cytochrome o complex, cytochromes bo3 oxidase, QObo3, ubiquinol oxidase, ubiquinol oxidase:O2 reductase
EC Number 7.1.1.3
CAS Registry Number
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, while for the?bd-II oxidase it is 1.?cf. EC?7.1.1.7, ubiquinol oxidase ubiquinol oxidase (electrogenic, proton-motive force generating).
Cofactor heme Cu cation
History
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