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- W59201720 abstract "Since the discovery of the first dinitrogen complex (Allen,Senoff, 1965), it has been generally assumed that the chemistry arising from such systems would enable us to understand the chemistry of nitrogenase, if not sooner then later, and certainly once the structure of nitrogenase had been established. This assumption has been upset by two related sets of events. The first was the discovery that there is more than one kind of nitrogenase (Eady, Leigh, 1994). This caused us to wonder whether molybdenum really is at the active site of conventional nitrogenases. It would appear that vanadium can replace molybdenum in some of its functions, and that iron may be the active metal in all three kinds of nitrogenase recognised hereto. The second was the elucidation of the structures of two different nitrogenase molybdenum-iron (MoFe) proteins (Kim, Rees, 1992; Bolin et al., 1993), which are supposed to contain the active sites for nitrogen fixation. The molybdenum atoms seem coordinatively saturated, and apparently excluded from reaction with dinitrogen, but there is no other obvious active site." @default.
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- W59201720 date "1995-01-01" @default.
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- W59201720 title "The Chemical Mechanism of Biological Nitrogen Fixation and The Chemistry of Model Systems" @default.
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- W59201720 doi "https://doi.org/10.1007/978-94-011-0379-4_19" @default.
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