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  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., 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.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0009-EC99-1 Version Permalink: https://hdl.handle.net/21.11116/0000-000D-179D-9
Genre: Book Chapter

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 Creators:
Wiig, J. A., Author
Lee, C. C., Author
Rebelein, J. G.1, Author                 
Sickerman, N. S., Author
Tanifuji, K., Author
Stiebritz, M. T., Author
Hu, Y., Author
Ribbe, M. W., Author
Affiliations:
1Emmy Noether research Group Microbial Metalloenzymes, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266294              

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 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.

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 Dates: 2017
 Publication Status: Issued
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 Identifiers: URI: https://books.rsc.org/books/edited-volume/1483/chapter-abstract/1054787/Biosynthesis-of-the-M-Cluster-of-Mo-Nitrogenase?redirectedFrom=fulltext
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Title: Molybdenum and Tungsten Enzymes: Biochemistry
Source Genre: Book
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Publ. Info: The Royal Society of Chemistry
Pages: - Volume / Issue: - Sequence Number: - Start / End Page: 297 - 312 Identifier: ISBN: 978-1-78262-089-1