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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Blasco*, F., Guigliarelli, B., Magalon, A. et al. The coordination and function of the redox centres of the membrane-bound nitrate reductases . CMLS, Cell. Mol. Life Sci. 58, 179–193 (2001). https://doi.org/10.1007/PL00000846
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DOI: https://doi.org/10.1007/PL00000846