Structural and biochemical characterization of a quinol binding site of Escherichia coli nitrate reductase A.
J Biol Chem
; 280(15): 14836-43, 2005 Apr 15.
Article
em En
| MEDLINE
| ID: mdl-15615728
ABSTRACT
The crystal structure of Escherichia coli nitrate reductase A (NarGHI) in complex with pentachlorophenol has been determined to 2.0 A of resolution. We have shown that pentachlorophenol is a potent inhibitor of quinolnitrate oxidoreductase activity and that it also perturbs the EPR spectrum of one of the hemes located in the membrane anchoring subunit (NarI). This new structural information together with site-directed mutagenesis data, biochemical analyses, and molecular modeling provide the first molecular characterization of a quinol binding and oxidation site (Q-site) in NarGHI. A possible proton conduction pathway linked to electron transfer reactions has also been defined, providing fundamental atomic details of ubiquinol oxidation by NarGHI at the bacterial membrane.
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Base de dados:
MEDLINE
Assunto principal:
Ubiquinona
/
Escherichia coli
/
Nitrato Redutases
Idioma:
En
Revista:
J Biol Chem
Ano de publicação:
2005
Tipo de documento:
Article
País de afiliação:
Canadá