Cherimolin-1, new selective inhibitor of the first energy-coupling site of the NADH: ubiquinone oxidoreductase (complex I).
Biochem Biophys Res Commun
; 240(1): 234-8, 1997 Nov 07.
Article
em En
| MEDLINE
| ID: mdl-9367916
ABSTRACT
The mechanism linking electron transport to proton translocation in the NADHubiquinone oxidoreductase (complex I of the mitochondrial respiratory chain) is still unclear. Inhibitors acting at different sites of the enzyme are powerful tools to clarify this mechanism. Up to now, a unique inhibitor, the Annonaceous acetogenin rolliniastatin-2, selectively blocks the most internal proton-translocation site. This study introduces cherimolin-1, a new acetogenin that inhibits the complex I with this special mode of action, which is more easily available from the plant material. Moreover, the mode of action of this scarce type of complex I inhibitor is further characterized.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Extratos Vegetais
/
NAD(P)H Desidrogenase (Quinona)
/
Frutas
/
Furanos
/
Lactonas
Limite:
Animals
Idioma:
En
Ano de publicação:
1997
Tipo de documento:
Article