Radical SAM-dependent formation of a nitrogenase cofactor core on NifB.

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.

SUBMITTER: Liu YA 

PROVIDER: S-EPMC9526504 | biostudies-literature | 2022 Aug

REPOSITORIES: biostudies-literature