Abstract
Biological nitrogen fixation is catalyzed by the nitrogenase system, which consists of two component metalloproteins, the iron (Fe-) protein and the molybdenum iron (MoFe-) protein. During substrate reduction, the two proteins associate to form a transient complex where electron transfer from the Fe-protein to the MoFe-protein is coupled to MgATP hydrolysis. Ultimately, electrons and protons are transferred to substrates bound to the active metallocenter of the MoFe-protein to generate reduced products.
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© 1998 Springer Science+Business Media Dordrecht
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Rees, D.C. et al. (1998). Complex Structures 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_3
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DOI: https://doi.org/10.1007/978-94-011-5159-7_3
Publisher Name: Springer, Dordrecht
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