KEGG   ENZYME: 1.10.3.10Help
Entry
EC 1.10.3.10                Enzyme                                 

Name
ubiquinol oxidase (H+-transporting);
cytochrome bb3 oxidase;
cytochrome bo oxidase;
cytochrome bd-II oxidase
Class
Oxidoreductases;
Acting on diphenols and related substances as donors;
With oxygen as acceptor
BRITE hierarchy
Sysname
ubiquinol:O2 oxidoreductase (H+-transporting)
Reaction(IUBMB)
2 ubiquinol + O2 + n H+[side 1] = 2 ubiquinone + 2 H2O + n H+[side 2] [RN:R09504]
Reaction(KEGG)
Substrate
ubiquinol [CPD:C00390];
O2 [CPD:C00007];
H+[side 1]
Product
ubiquinone [CPD:C00399];
H2O [CPD:C00001];
H+[side 2]
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
EC 1.10.3.10 created 2011, modified 2014
Reference
1  [PMID:11017202]
  Authors
Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, Wikstrom M
  Title
The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site.
  Journal
Nat. Struct. Biol. 7 (2000) 910-7.
  Sequence
[up:P0ABI8]
Reference
2  [PMID:20416270]
  Authors
Yap LL, Lin MT, Ouyang H, Samoilova RI, Dikanov SA, Gennis RB
  Title
The quinone-binding sites of the cytochrome bo3 ubiquinol oxidase from Escherichia coli.
  Journal
Biochim. Biophys. Acta. 1797 (2010) 1924-32.
Reference
3  [PMID:20392690]
  Authors
Shepherd M, Sanguinetti G, Cook GM, Poole RK
  Title
Compensations for diminished terminal oxidase activity in Escherichia coli: cytochrome bd-II-mediated respiration and glutamate metabolism.
  Journal
J. Biol. Chem. 285 (2010) 18464-72.
Reference
4  [PMID:21987791]
  Authors
Borisov VB, Murali R, Verkhovskaya ML, Bloch DA, Han H, Gennis RB, Verkhovsky MI
  Title
Aerobic respiratory chain of Escherichia coli is not allowed to work in fully uncoupled mode.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 108 (2011) 17320-4.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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