Studies on cytochrome c oxidase, IV[1--3]. Primary structure and function of subunit II.
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.
D000595:Amino Acid Sequence; D000818:Animals; D001400:Azurin; D002417:Cattle; D003300:Copper / Q000032:analysis; D003576:Electron Transport Complex IV; D046911:Macromolecular Substances; D009206:Myocardium / Q000201:enzymology; D010970:Plastocyanin; D011485:Protein Binding; D013045:Species Specificity
D046911:Macromolecular Substances; D001400:Azurin; D003300:Copper; D010970:Plastocyanin; D003576:Electron Transport Complex IV