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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Binding Sites
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Cell Membrane / metabolism
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Crystallography, X-Ray
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Dose-Response Relationship, Drug
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Electron Spin Resonance Spectroscopy
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Escherichia coli / enzymology*
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Escherichia coli / metabolism
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Heme / chemistry
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Histidine / chemistry
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Hydroxyquinolines / chemistry
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Kinetics
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Lysine / chemistry
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Models, Chemical
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Models, Molecular
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Mutation
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Naphthols / chemistry
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Nitrate Reductase
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Nitrate Reductases / chemistry*
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Oxidoreductases / chemistry
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Oxygen / chemistry
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Pentachlorophenol / chemistry
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Plasmids / metabolism
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Protein Binding
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Protons
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Terpenes / chemistry
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Ubiquinone / analogs & derivatives*
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Ubiquinone / chemistry
Substances
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Hydroxyquinolines
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Naphthols
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Protons
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Terpenes
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Ubiquinone
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2-(n-heptyl)-4-hydroxyquinoline N-oxide
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menaquinol 6
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Heme
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Histidine
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Pentachlorophenol
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Oxidoreductases
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Nitrate Reductases
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Nitrate Reductase
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Lysine
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ubiquinol
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Oxygen
Associated data
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PDB/1Y4Z
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PDB/1Y5I
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PDB/1Y5L
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PDB/1Y5N