Identity and function of an essential nitrogen ligand of the nitrogenase cofactor biosynthesis protein NifB.

ABSTRACT: NifB is a radical S-adenosyl-L-methionine (SAM) enzyme that is essential for nitrogenase cofactor assembly. Previously, a nitrogen ligand was shown to be involved in coupling a pair of [Fe₄S₄] clusters (designated K1 and K2) concomitant with carbide insertion into an [Fe₈S₉C] cofactor core (designated L) on NifB. However, the identity and function of this ligand remain elusive. Here, we use combined mutagenesis and pulse electron paramagnetic resonance analyses to establish histidine-43 of Methanosarcina acetivorans NifB (MaNifB) as the nitrogen ligand for K1. Biochemical and continuous wave electron paramagnetic resonance data demonstrate the inability of MaNifB to serve as a source for cofactor maturation upon substitution of histidine-43 with

SUBMITTER: Rettberg LA 

PROVIDER: S-EPMC7145814 | biostudies-literature | 2020 Apr

REPOSITORIES: biostudies-literature