J Biol Chem. 2005 Apr 15;280(15):14836-43. Epub 2004 Dec 22.

Structural and biochemical characterization of a quinol binding site of Escherichia coli nitrate reductase A.

Bertero MG, Rothery RA, Boroumand N, Palak M, Blasco F, Ginet N, Weiner JH, Strynadka NC.

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Department of Biochemistry, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada.

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.

PMID:: 15615728; [PubMed - indexed for MEDLINE]

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Structures reported by this article

The Crystal Structure Of The Narghi Mutant Nari-K86a In Complex With Pentachlorophenol

PDB: 1Y5N

Source: Escherichia coli

Method: X-Ray Diffraction

Resolution: 2.5 Å

See all 4 structures...

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