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ENZYME

ENZYME entry: EC 7.1.1.7

PURL: https://purl.expasy.org/enzyme/EC/7.1.1.7
Accepted Name
ubiquinol oxidase (electrogenic, proton-motive force generating)
Alternative Name(s)
cytochrome bd-I oxidase
Reaction catalysed
2 a ubiquinol + O2(in) + 4 H(+)(in) = 2 a ubiquinone + 2 H2O(in) + 4 H(+)(out)
Comment(s)
  • This terminal oxidase enzyme is unable to pump protons but generates a proton motive force by transmembrane charge separation resulting from utilizing protons and electrons originating from opposite sides of the membrane to generate water.
  • The bioenergetic efficiency (the number of charges driven across the membrane per electron used to reduce oxygen to water) is 1.
  • The bd-I oxidase from the bacterium Escherichia coli is the predominant respiratory oxygen reductase that functions under microaerophilic conditions in that organism. cf. EC 7.1.1.3.
  • Formerly EC 1.10.3.14.
Cross-references
BRENDA7.1.1.7
EC2PDB7.1.1.7
ExplorEnz7.1.1.7
KEGG Ligand Database for Enzyme Nomenclature7.1.1.7
IUBMB Enzyme Nomenclature7.1.1.7
MEDLINEFind literature relating to 7.1.1.7
MetaCyc7.1.1.7
Rhea expert-curated reactions7.1.1.7
UniProtKB/Swiss-Prot
Q09049, CYDA_AZOVIP94364, CYDA_BACSUP0ABK0, CYDA_ECOL6
P0ABJ9, CYDA_ECOLIP0ABK1, CYDA_SHIFLP94365, CYDB_BACSU
P0ABK4, CYDB_ECO57P0ABK3, CYDB_ECOL6P0ABK2, CYDB_ECOLI
Q2YKD6, CYDX_BRUA2P56100, CYDX_ECOLI

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 7.1.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 7.1.-.-
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