PTHR22888

CYTOCHROME C OXIDASE, SUBUNIT II

PANTHER entry
Member databasePANTHER
PANTHER typefamily

Description
Imported from IPR045187

Cytochrome c oxidase (
7.1.1.9
)
[2, 3]
is an oligomeric enzymatic complex which is a component of the respiratory chain and is involved in the transfer of electrons from cytochrome c to oxygen. In eukaryotes this enzyme complex is located in the mitochondrial inner membrane; in aerobic prokaryotes it is found in the plasma membrane. The number of polypeptides in the complex ranges from 3-4 (prokaryotes), up to 13 (mammals). In Archaea, a cytochrome-c-type oxidase from Natronobacterium (cytochrome ba3) has been shown to consists of four subunits
[1]
.

Subunit 2 (CO II) transfers the electrons from cytochrome c to the catalytic subunit 1. It contains two adjacent transmembrane regions in its N terminus and the major part of the protein is exposed to the periplasmic or to the mitochondrial intermembrane space, respectively. CO II provides the substrate-binding site and contains a copper centre called Cu(A), probably the primary acceptor in cytochrome c oxidase. An exception is the corresponding subunit of the cbb3-type oxidase which lacks the copper A redox-centre. Several bacterial CO II have a C-terminal extension that contains a covalently bound haem c.

References
Imported from IPR045187

1.Cytochrome ba3 from Natronobacterium pharaonis--an archaeal four-subunit cytochrome-c-type oxidase. Mattar S, Engelhard M. Eur. J. Biochem. 250, 332-41, (1997). View articlePMID: 9428682

2.Structure of cytochrome c oxidase. Capaldi RA, Malatesta F, Darley-Usmar VM. Biochim. Biophys. Acta 726, 135-48, (1983). View articlePMID: 6307356

3.The superfamily of heme-copper respiratory oxidases. Garcia-Horsman JA, Barquera B, Rumbley J, Ma J, Gennis RB. J. Bacteriol. 176, 5587-600, (1994). View articlePMID: 8083153

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