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  • Title: Radical SAM-dependent formation of a nitrogenase cofactor core on NifB.
    Author: Liu YA, Quechol R, Solomon JB, Lee CC, Ribbe MW, Hu Y, Hedman B, Hodgson KO.
    Journal: J Inorg Biochem; 2022 Aug; 233():111837. PubMed ID: 35550498.
    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.
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