Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase.
Science
; 280(5370): 1723-9, 1998 Jun 12.
Article
em En
| MEDLINE
| ID: mdl-9624044
ABSTRACT
Crystal structures of bovine heart cytochrome c oxidase in the fully oxidized, fully reduced, azide-bound, and carbon monoxide-bound states were determined at 2.30, 2.35, 2.9, and 2.8 angstrom resolution, respectively. An aspartate residue apart from the O2 reduction site exchanges its effective accessibility to the matrix aqueous phase for one to the cytosolic phase concomitantly with a significant decrease in the pK of its carboxyl group, on reduction of the metal sites. The movement indicates the aspartate as the proton pumping site. A tyrosine acidified by a covalently linked imidazole nitrogen is a possible proton donor for the O2 reduction by the enzyme.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Bombas de Próton
/
Complexo IV da Cadeia de Transporte de Elétrons
/
Miocárdio
Limite:
Animals
Idioma:
En
Revista:
Science
Ano de publicação:
1998
Tipo de documento:
Article
País de afiliação:
Japão