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 structu...

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Veröffentlicht in:Cellular and molecular life sciences : CMLS 2001-02, Vol.58 (2), p.179-193
Hauptverfasser: Blasco, F, Guigliarelli, B, Magalon, A, Asso, M, Giordano, G, Rothery, R A
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Sprache:eng
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Zusammenfassung: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.
ISSN:1420-682X
1420-9071
DOI:10.1007/PL00000846