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Updated: Jul 22, 2026

EPR Monitored Redox Titration of the Cofactors of Saccharomyces cerevisiae Nar1
Published on: November 26, 2014
The coordination and function of the redox centres of the membrane-bound nitrate reductases
F Blasco1, B Guigliarelli, A Magalon
1Laboratoire de Chimie Bactérienne, IBSM, CNRS, Marseille, France. blasco@ibsm.cnrs-mrs.fr
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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