Journal
JOURNAL OF INORGANIC BIOCHEMISTRY
Volume 233, Issue -, Pages -Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.jinorgbio.2022.111837
Keywords
Nitrogenase; Biosynthesis; FeS cluster; M-cluster; NifB; Radical SAM enzyme
Funding
- NIH-NIGMS [P41GM103393, P30GM133894, GM67626, GM141046]
- DOE Office of Biological and Environmental Research
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This review focuses on the recent work that sheds light on the role of NifB in the formation of the [Fe8S9C] core of the nitrogenase cofactor, highlighting the structure, function, and mechanism of this unique radical SAM methyltransferase.
Nitrogenase is a versatile metalloenzyme that reduces N-2, CO and CO2 at its cofactor site. Designated the M-cluster, this complex cofactor has a composition of [(R-homocitrate)MoFe7S9C], and it is assembled through the generation of a unique [Fe8S9C] core prior to the insertion of Mo and homocitrate. NifB is a radical S-adenosyl-L-methionine (SAM) enzyme that is essential for nitrogenase cofactor assembly. This review focuses on the recent work that sheds light on the role of NifB in the formation of the [Fe8S9C] core of the nitrogenase cofactor, highlighting the structure, function and mechanism of this unique radical SAM methyltransferase.
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