Structural and biochemical characterization of a quinol binding site of Escherichia coli nitrate reductase A |
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Authors: | Bertero Michela G Rothery Richard A Boroumand Nasim Palak Monica Blasco Francis Ginet Nicolas Weiner Joel H Strynadka Natalie C J |
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Institution: | Department of Biochemistry, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada. |
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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 quinol:nitrate 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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