A model for dinitrogen binding in the E₄ state of nitrogenase.

ABSTRACT: Molybdenum nitrogenase is one of the most intriguing metalloenzymes in nature, featuring an exotic iron-molybdenum-sulfur cofactor, FeMoco, whose mode of action remains elusive. In particular, the molecular and electronic structure of the N₂-binding E₄ state is not known. In this study we present theoretical QM/MM calculations of new structural models of the E₄ state of molybdenum-dependent nitrogenase and compare to previously suggested models for this enigmatic redox state. We propose two models as possible candidates for the E₄ state. Both models feature two hydrides on the FeMo cofactor, bridging atoms Fe₂ and Fe₆ with a terminal sulfhydryl group on either Fe₂ or Fe₆ (derived from the S2B bridge) an

SUBMITTER: Thorhallsson AT 

PROVIDER: S-EPMC7069239 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature