Abstract
The X-ray crystal structure of the active centre of molybdenum nitrogenase, FeMoco, in Azotobacter vinelandii (Peters et al., 1997) (Figure 1) has raised the question:- where on this cluster, and by implication the corresponding clusters in the alternative V- and Fe-nitrogenases (Eady, 1991) are substrates bound and reduced? This review discusses this question in the light of the reactions of isolated FeMoco and of metal complexes, cluster or otherwise, which give important information on the binding and reduction of nitrogenase substrates at metal centres. Reactions of FeMoco within the protein (e. g. binding of CO, George et al., 1997) are discussed elsewhere in this volume.
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Richards, R.L. (1998). Chemical Models for the Function of Nitrogenase. In: Elmerich, C., Kondorosi, A., Newton, W.E. (eds) Biological Nitrogen Fixation for the 21st Century. Current Plant Science and Biotechnology in Agriculture, vol 31. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-5159-7_4
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