| Literature DB >> 35550498 |
Yiling A Liu1, Robert Quechol1, Joseph B Solomon2, Chi Chung Lee1, Markus W Ribbe3, Yilin Hu4, Britt Hedman5, Keith O Hodgson6.
Abstract
Nitrogenase is a versatile metalloenzyme that reduces N2, 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.Entities:
Keywords: Biosynthesis; FeS cluster; M-cluster; NifB; Nitrogenase; Radical SAM enzyme
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Year: 2022 PMID: 35550498 PMCID: PMC9526504 DOI: 10.1016/j.jinorgbio.2022.111837
Source DB: PubMed Journal: J Inorg Biochem ISSN: 0162-0134 Impact factor: 4.336