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Published December 15, 2011 | public
Book Section - Chapter



Nitrogenase catalyzes the enzymatic reduction of atmospheric dinitrogen to ammonia during the process of biological nitrogen fixation. Nitrogenase consists of two component metalloproteins, the iron (Fe-) protein and the molybdenum-iron (MoFe-) protein, that together mediate the ATP-hydrolysis–dependent reduction of substrates to products. Crystallographic studies have established the structures of the component proteins and the associated complex metallocenters of nitrogenase, including the iron-molybdenum cofactor that provides the active site for substrate reduction and the P-cluster that participates in electron transfer between the Fe-protein and MoFe-protein. Striking parallels are evident in the interaction of the nucleotides with the Fe-protein and with a broad class of nucleotide-binding proteins involved in signal and energy transduction processes. Together with kinetic, spectroscopic, and synthetic model compound studies, these structures provide a framework for addressing the mechanism of substrate reduction by nitrogenase.

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© 2011 John Wiley & Sons, Ltd. Research on nitrogenase carried out in the author's laboratories was supported by a grant from the National Institutes of Health.

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