Evidence of substrate binding and product release via belt-sulfur mobilization of the nitrogenase cofactor.

ABSTRACT: The Mo-nitrogenase catalyses the ambient reduction of N₂ to NH₃ at the M-cluster, a complex cofactor that comprises two metal-sulphur partial cubanes ligated by an interstitial carbide and three belt-sulphurs. A recent crystallographic study suggests binding of N₂ via displacement of the belt-sulphur(s) of the M-cluster upon turnover. However, the direct proof of N₂ binding and belt-sulphur mobilization during catalysis remains elusive. Here we show that N₂ is captured on the M-cluster via electron- and sulphur-depletion, and that the N₂-captured state is catalytically competent in generating NH₃. Moreover, we demonstrate that product release only occurs when sulphite is supplied along with a reductant, that sulph

SUBMITTER: Lee CC 

PROVIDER: S-EPMC9540607 | biostudies-literature | 2022 May

REPOSITORIES: biostudies-literature