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