Structural and Biochemical Characterization of a Quinol Binding Site of Escherichia coli Nitrate Reductase A
| Autor: | Michela G. Bertero, Richard A. Rothery, Nasim Boroumand, Monica Palak, Natalie C. J. Strynadka, Joel H. Weiner, Nicolas Ginet, Francis Blasco |
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| Rok vydání: | 2005 |
| Předmět: |
Models
Molecular Ubiquinol Pentachlorophenol Molecular model Ubiquinone Protein subunit Heme Naphthols macromolecular substances Crystallography X-Ray Nitrate reductase medicine.disease_cause Nitrate Reductase Biochemistry chemistry.chemical_compound Nitrate Reductases Oxidoreductase Escherichia coli medicine Histidine Molecular Biology chemistry.chemical_classification Binding Sites Dose-Response Relationship Drug Terpenes Lysine Cell Membrane Mutagenesis Electron Spin Resonance Spectroscopy Cell Biology Oxygen Kinetics Membrane Models Chemical chemistry Mutation Hydroxyquinolines Protons Oxidoreductases Plasmids Protein Binding |
| Zdroj: | Journal of Biological Chemistry. 280:14836-14843 |
| ISSN: | 0021-9258 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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