Tracing the incorporation of the "ninth sulfur" into the nitrogenase cofactor precursor with selenite and tellurite.

ABSTRACT: Molybdenum nitrogenase catalyses the reduction of N₂ to NH₃ at its cofactor, an [(R-homocitrate)MoFe₇S₉C] cluster synthesized via the formation of a [Fe₈S₉C] L-cluster prior to the insertion of molybdenum and homocitrate. We have previously identified a [Fe₈S₈C] L*-cluster, which is homologous to the core structure of the L-cluster but lacks the 'ninth sulfur' in the belt region. However, direct evidence and mechanistic details of the L*- to L-cluster conversion upon 'ninth sulfur' insertion remain elusive. Here we trace the 'ninth sulfur' insertion using SeO₃^2- and TeO₃^2- as 'labelled' SO₃^2-. Biochemical, electron paramagnetic resonance

SUBMITTER: Tanifuji K 

PROVIDER: S-EPMC8629924 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature