Synthetic models of the nitrogenase FeMo cofactor.

ABSTRACT: The FeMo cofactor (FeMoco), the key active site in the Mo-based nitrogenase, is one of the most complicated metalloenzyme molecules. Synthesis of the FeMoco model cluster ([MoFe₇S₉C]) is essential to understanding its function in dinitrogen binding, activation, and conversion. However, the complex framework of the FeMoco cluster, which features a unique trigonal prismatic [Fe₆C] moiety comprising a µ₆-bridging carbide, has made the synthesis of the cluster a persistent challenge. In this work, two analogous mimics of FeMoco have been synthesized, using a cluster-coupling synthetic strategy facilitated by the fabrication of unsaturated ligand/metal coordination. The incorporation of a µ₆-X (X = C^4- or N^3-</

SUBMITTER: Xu YY 

PROVIDER: S-EPMC12184401 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature