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Synthesis, Structure and Properties of some Mo—Fe—S, Mo—S Model Compounds for the Mo—Fe Center and the First Coordination Sphere of the Mo—Atom in Nitrogenase

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The Nitrogen Fixation and its Research in China

Abstract

Nitrogenase is a two-component redox enzyme that catalyzes the reduction of dinitrogen to ammonia. The structure and function of Mo in the MoFe-protein of this enzyme has been the subject of a number of investigations including the use of EPR, Mössbauer (Muenck et al. 1975; Zimmermann et al. 1978; Huynh et al. 1979) and X-ray absorption spectroscopy (XAS) which includes the extended X-ray absorption fine structure (EXAFS) and X-ray absorption near edge structure (XANES) (Cramer et al. 1978, 1978a; Conradson et al. 1987, 1985). The recent results of these investigations on the MoFe-protein and its FeMo-co have revealed that the active center responsible for catalyzing the reduction of nitrogen to ammonia in nitrogenase involves a iron—molybdenum—sulfur aggregate with the ratio of Fe: Mo:S of 1:6–8:4–9 (Shah et al. 1977; Yang et al. 1982; Nelson et al. 1983; Burgess et al. 1983) and the environment of the molybdenum atom of FeMo-co in and after extrusion from the MoFe-protein matrix contains two to three oxygen atoms at 2.10 Å, three to four sulfur atoms at 2.37 Å and three to four iron atoms at 2.70 Å. (Conradson et al. 1987, 1985).

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Zhuang, BT., Huang, LR., Zhao, XT., Chen, PC., Lan, AJ., Lu, JX. (1992). Synthesis, Structure and Properties of some Mo—Fe—S, Mo—S Model Compounds for the Mo—Fe Center and the First Coordination Sphere of the Mo—Atom in Nitrogenase. In: Hong, GF. (eds) The Nitrogen Fixation and its Research in China. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-10385-2_7

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