PMID:15615728
| Citation |
Bertero, MG, Rothery, RA, Boroumand, N, Palak, M, Blasco, F, Ginet, N, Weiner, JH and Strynadka, NC (2005) Structural and biochemical characterization of a quinol binding site of Escherichia coli nitrate reductase A. J. Biol. Chem. 280:14836-43 |
|---|---|
| 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. |
| Links |
PubMed Online version:10.1074/jbc.M410457200 |
| Keywords |
Binding Sites; Cell Membrane/metabolism; Crystallography, X-Ray; Dose-Response Relationship, Drug; Electron Spin Resonance Spectroscopy; Escherichia coli/enzymology; Escherichia coli/metabolism; Heme/chemistry; Histidine/chemistry; Hydroxyquinolines/chemistry; Kinetics; Lysine/chemistry; Models, Chemical; Models, Molecular; Mutation; Naphthols/chemistry; Nitrate Reductase; Nitrate Reductases/chemistry; Oxidoreductases/chemistry; Oxygen/chemistry; Pentachlorophenol/chemistry; Plasmids/metabolism; Protein Binding; Protons; Terpenes/chemistry; Ubiquinone/analogs & derivatives; Ubiquinone/chemistry |
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