Abstract
At present, three kinds of nitrogenases are known, i.e. the molybdenum-containing nitrogenase (Mo nitrogenase), the vanadium-containing nitrogenase (V nitrogenase), and a third nitrogen fixation system (nitrogenase 3). The last one has more complicated components, and its activities are lower than those of the former, and the nitrogen fixation mechanism of nitrogenase 3 has not yet become clear (Chisnell et al. 1988). Similar to the Mo nitrogenase, V nitrogenase requires MgATP and a source of low-potential electrons to reduce substrates such as H+, N2, and C2H2, (Eady et al. 1987). The kinetic and spectroscopic data suggest the same sequence of electron-transfer reactions and a similar overall mechanism (Eady et al. 1987; Dilworth et al. 1988; Hales et al. 1986, a, b). However, obvious differences in substrate specificity have been observed, i.e., Mo nitrogenase reduces C2H2, to C2H4, whereas V nitrogenase reduces C2H2 to C2H4 and C2H6 (Dilworth 1988). As the assay temperature was lowered from 30 to 5 °C, nitrogen remained an effective substrate for V nitrogenase, but not for Mo nitrogenase (Miller et al. 1988).
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Liu, CW., Lu, JX. (1992). Systematic Investigations on the Bonding Property of the M—Fe—S (M = Mo, V, and W) Cluster Compounds and Novel Assumption on the Active Center Models of 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_8
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