Studies on Cytochrome C Oxidase, IV[1--3]. Primary Structure and Function of Subunit II

Overview

Journal Hoppe Seylers Z Physiol Chem

Specialty Biochemistry

Date 1979 Apr 1

PMID 220175

Citations 43

Authors

G J Steffens

G Buse

Affiliations

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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.

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