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Published on Web 02/01/2010 Is Mo Involved in Hydride Binding by the Four-Electron Reduced (E4) Intermediate of the Nitrogenase MoFe Protein?

By Dmitriy Lukoyanov, Zhi-yong Yang, Dennis R. Dean, Lance C. Seefeldt and Brian M. Hoffman


The X-ray structure 1 of the nitrogenase 2 molydenum-iron (MoFe) protein reveals the active-site FeMo-cofactor (FeMo-co) to be an unprecedented [Fe7S9MoX; homocitrate] cluster, Figure 1, but does not define the location of substrate binding and reduction. Mo is an obvious candidate, as it is the catalytic metal in the only known inorganic metal complexes that catalytically reduce N2. 3 However, Fe is no less a candidate, given that it is the catalytic metal in the commercial Haber-Bosch process for NH3 formation and that there are V and Fe nitrogenases that reduce N2 but do not have Mo. 4 Figure 1. FeMo-co from PDB coordinate file 1M1N.pdb: Fe, rust; Mo

Year: 2009
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