The oxidation of cytochrome-c oxidase vesicles by hemoglobin.
Biochim Biophys Acta
; 1208(1): 38-44, 1994 Sep 21.
Article
em En
| MEDLINE
| ID: mdl-8086437
ABSTRACT
Human hemoglobin has been used as a pro-oxidant for artificial unilamellar phospholipid vesicles, containing cytochrome-c oxidase inserted into the bilayer. This experimental system was suitable to follow directly the kinetics of lipid oxidation and the effects on both the vesicle membrane permeability and the functional state of cytochrome-c oxidase. Following mixing of vesicles with hemoglobin, an oxygen dependent, peroxyl radical mediated, rapid oxidation (taking a few minutes) of the lipid was found to occur. On a similar time scale the membrane became ion-leaky and cytochrome-c oxidase damaged. The pro-oxidant effects of hemoglobin in various oxidation and ligation states were studied and a mechanism, based on a ferric/ferryl redox cycle of the heme-iron is proposed to account for these observations.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Hemoglobinas
/
Peroxidação de Lipídeos
/
Complexo IV da Cadeia de Transporte de Elétrons
/
Lipossomos
Limite:
Humans
Idioma:
En
Revista:
Biochim Biophys Acta
Ano de publicação:
1994
Tipo de documento:
Article
País de afiliação:
Itália