Electron Redistribution within the Nitrogenase Active Site FeMo-Cofactor During Reductive Elimination of H₂ to Achieve N≡N Triple-Bond Activation.

ABSTRACT: Nitrogen fixation by nitrogenase begins with the accumulation of four reducing equivalents at the active-site FeMo-cofactor (FeMo-co), generating a state (denoted E₄(4H)) with two [Fe-H-Fe] bridging hydrides. Recently, photolytic reductive elimination (re) of the E₄(4H) hydrides showed that enzymatic re of E₄(4H) hydride yields an H₂-bound complex (E₄(H₂,2H)), in a process corresponding to a formal 2-electron reduction of the metal-ion core of FeMo-co. The resulting electron-density redistribution from Fe-H bonds to the metal ions themselves enables N₂ to bind with concomitant H₂ release, a process illuminated here by QM/MM molecular dynamics simulations. What is the nature of this redistr

SUBMITTER: Lukoyanov DA 

PROVIDER: S-EPMC7783777 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature