The coordination and function of the redox centres of the membrane-bound nitrate reductases |
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| Authors: | F Blasco B Guigliarelli A Magalon M Asso G Giordano R A Rothery |
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| Institution: | (1) Laboratoire de Chimie Bactérienne, IBSM, CNRS, 31 chemin Joseph Aiguier, F-13402 Marseille Cedex 20 (France), Fax +33 04 91 71 89 14, e-mail: blasco@ibsm.cnrs-mrs.fr , FR;(2) Laboratoire de Bioénergétique et Ingénierie des Protéines, IBSM, CNRS, 31 chemin Joseph Aiguier, 13402 Marseille Cedex 20 (France) , FR;(3) Department of Biochemistry, 474 Medical Science Building, University of Alberta, Edmonton, Alberta T6G 2H7 (Canada) , CA |
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| Abstract: | Under anaerobic conditions and in the presence of nitrate, the facultative anaerobe Escherichia coli synthesises an electron-transport chain comprising a primary dehydrogenase and the terminal membrane-bound nitrate reductase
A (NarGHI). This review focuses on recent advances obtained on the structure and function of the three protein subunits of
membrane-bound nitrate reductases. We discuss a global architecture for the Mo-bisMGD-containing subunit (NarG) and a coordination
model for the four Fe–S] centres of the electron-transfer subunit (NarH) and for the two b-type haems of the anchor subunit NarI. |
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| Keywords: | , Nitrate reductase, molybdenum cofactor, [Fe–,S] centres, haems, |
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