Molecular sorting of nitrogenase catalytic cofactors.

ABSTRACT: The free-living diazotroph Azotobacter vinelandii produces three genetically distinct but functionally and mechanistically similar nitrogenase isozymes, designated as Mo-dependent, V-dependent, and Fe-only. They respectively harbor nearly identical catalytic cofactors that are distinguished by a heterometal site occupied by Mo (FeMo-cofactor), V (FeV-cofactor), or Fe (FeFe-cofactor). Completion of FeMo-cofactor and FeV-cofactor formation occurs on molecular scaffolds prior to delivery to their catalytic partners. In contrast, completion of FeFe-cofactor assembly occurs directly within its cognate catalytic partner. Because hybrid nitrogenase species that contain the incorrect cofactor type cannot reduce N₂ to support diazotrophic growth, there must be a way to prevent misincorpo

SUBMITTER: Salinero-Lanzarote A 

PROVIDER: S-EPMC11938142 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature