CHAPTER 9 Biosynthesis of the M-Cluster of Mo-Nitrogenase

Wiig, J. A.; Lee, C. C.; Rebelein, J. G.; Sickerman, N. S.; Tanifuji, K.; Stiebritz, M. T.; Hu, Y.; Ribbe, M. W.

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CHAPTER 9 Biosynthesis of the M-Cluster of Mo-Nitrogenase

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Rebelein, J. G.
Emmy Noether research Group Microbial Metalloenzymes, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Wiig, J. A., Lee, C. C., Rebelein, J. G., Sickerman, N. S., Tanifuji, K., Stiebritz, M. T., et al. (2017). CHAPTER 9 Biosynthesis of the M-Cluster of Mo-Nitrogenase. In Molybdenum and Tungsten Enzymes: Biochemistry (pp. 297-312). The Royal Society of Chemistry.

Cite as: https://hdl.handle.net/21.11116/0000-0009-EC99-1

Abstract

The nitrogenase complex is responsible for the reduction of an inert gas, dinitrogen (N2), to a bioavailable form of nitrogen, ammonia (NH3). At the heart of the catalytic component of molybdenum (Mo) nitrogenase resides the iron-molybdenum (FeMo) cofactor (also termed the M-cluster). This chapter will describe the key proteins involved in the biosynthesis of the M-cluster and how simple [Fe4S4] clusters are transformed into a complex, [MoFe7S9C-homocitrate] M-cluster and subsequently transferred to the active site of nitrogenase.