A conformational role for NifW in the maturation of molybdenum nitrogenase P-cluster.

ABSTRACT: Reduction of dinitrogen by molybdenum nitrogenase relies on complex metalloclusters: the [8Fe:7S] P-cluster and the [7Fe:9S:Mo:C:homocitrate] FeMo-cofactor. Although both clusters bear topological similarities and require the reductive fusion of [4Fe:4S] sub-clusters to achieve their respective assemblies, P-clusters are assembled directly on the NifD₂K₂ polypeptide prior to the insertion of FeMo-co, which is fully assembled separately from NifD₂K₂. P-cluster maturation involves the iron protein NifH₂ as well as several accessory proteins, whose role has not been elucidated. In the present work, two NifD₂K₂ species bearing immature P-clusters were isolated from an Azotobacter vinelandii strain in which the

SUBMITTER: Van Stappen C 

PROVIDER: S-EPMC8943848 | biostudies-literature | 2022 Mar

REPOSITORIES: biostudies-literature