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Studies on the Mechanism of Nitrogenase Catalysis— Substrates-Cluster-Coordination-Chemistry Approach

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The Nitrogen Fixation and its Research in China

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Abstract

Nitrogenase is a complex metalloenzyme reversibly dissociable into two metallo- protein components: component 1, the MoFe-protein, a tetramer (α 2 β 2) with 2 Mo, about 30 Fe and about the same number of acid-labile S, and a molecular weight of about 220 kDa, carries the binding sites for the reducible substrates; and component 2, the Fe-protein, a dimer (Γ 2), with a 4Fe-4S cluster and a molecular weight of about 60 kDa, serves as a specific electron carrier to transfer electrons to the MoFe-protein with the aid of the “electron activator” ATP, which goes into the enzyme complex as MgATP bound to the Fe-protein and is hydrolyzed into ADP and inorganic phosphate, Pi, concomitant with the electron transfer; each dimeric molecule of Fe-protein being able to bind reversibly one or two molecules of MgATP or MgADP. However, MgATP appears to be a nonreducible substrate of nitrogenase, its hydrolysis may, or may not be coupled to electron transfer in nitrogenase reactions, as to be discussed later.

This work is supported by the National Natural Science Foundation of China and has also been supported by grants from the National Science Technology Commission administered through Academia Sinica and through National Education Commission.

To whom correspondence should be addressed.

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  1. K. R. Tsai
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  2. H.-L. Wan
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  3. H.-T. Zhang
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  4. L.-S. Xu
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  1. Shanghai Institute of Biochemistry, Academia Sinica, 320 Yue-Yang Road, 200031, Shanghai, PR China

    Guo-Fan Hong

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Tsai, K.R., Wan, HL., Zhang, HT., Xu, LS. (1992). Studies on the Mechanism of Nitrogenase Catalysis— Substrates-Cluster-Coordination-Chemistry Approach. 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_4

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