Cellular and Molecular Life Sciences CMLS

, Volume 58, Issue 2, pp 179–193

The coordination and function of the redox centres of the membrane-bound nitrate reductases

  • F. Blasco*
  • B. Guigliarelli
  • A. Magalon
  • M. Asso
  • G. Giordano
  • R. A. Rothery

DOI: 10.1007/PL00000846

Cite this article as:
Blasco*, F., Guigliarelli, B., Magalon, A. et al. CMLS, Cell. Mol. Life Sci. (2001) 58: 179. doi:10.1007/PL00000846
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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.

Key words. Nitrate reductase; molybdenum cofactor; [Fe–S] centres; haems.

Copyright information

© Birkhäuser Verlag Basel, 2001

Authors and Affiliations

  • F. Blasco*
    • 1
  • B. Guigliarelli
    • 2
  • A. Magalon
    • 1
  • M. Asso
    • 2
  • G. Giordano
    • 1
  • R. A. Rothery
    • 3
  1. 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. 2.Laboratoire de Bioénergétique et Ingénierie des Protéines, IBSM, CNRS, 31 chemin Joseph Aiguier, 13402 Marseille Cedex 20 (France) FR
  3. 3.Department of Biochemistry, 474 Medical Science Building, University of Alberta, Edmonton, Alberta T6G 2H7 (Canada) CA