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Hoppe Seylers Z Physiol Chem. 1979 Apr;360(4):613-9.

Studies on cytochrome c oxidase, IV[1--3]. Primary structure and function of subunit II.

Abstract

The amino acid sequence of polypeptide II from beef heart cytochrome c oxidase is described. Comparision of this primary structure with those of azurins, plastocyanins and stellacyanins reveals clear homologies among them. Thus subunit II of the oxidase is a member of this copper protein family. The sequence homology indicates a copper binding site consisting of two invariant histidines and two sulfur-containing amino acids. Thus subunit II is like a blue copper protein with type I copper.

PMID:
220175
[Indexed for MEDLINE]

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