The coordination and function of the redox centres of the membrane-bound nitrate reductases.
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.
Blasco
F
F
Laboratoire de Chimie Bactérienne, IBSM, CNRS, Marseille, France. blasco@ibsm.cnrs-mrs.fr
Guigliarelli
B
B
Magalon
A
A
Asso
M
M
Giordano
G
G
Rothery
R A
RA
D002462:Cell Membrane / Q000201:enzymology; D003067:Coenzymes / Q000737:chemistry; D004578:Electron Spin Resonance Spectroscopy; D004579:Electron Transport; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D006418:Heme / Q000737:chemistry; D007501:Iron / Q000737:chemistry; D008982:Molybdenum / Q000737:chemistry; D016297:Mutagenesis, Site-Directed; D050901:Nitrate Reductase; D009565:Nitrate Reductases / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D010084:Oxidation-Reduction; D021122:Protein Subunits; D013455:Sulfur / Q000737:chemistry
D003067:Coenzymes; D021122:Protein Subunits; D006418:Heme; D013455:Sulfur; D008982:Molybdenum; D007501:Iron; D009565:Nitrate Reductases; D050901:Nitrate Reductase