Azotobacter vinelandii scaffold protein NifU transfers iron to NifQ as part of the iron-molybdenum cofactor biosynthesis pathway for nitrogenase.

ABSTRACT: The Azotobacter vinelandii molybdenum nitrogenase obtains molybdenum from NifQ, a monomeric iron-sulfur molybdoprotein. This protein requires an existing [Fe-S] cluster to form a [Mo-Fe₃-S₄] group, which acts as a specific molybdenum donor during nitrogenase FeMo-co biosynthesis. Here, we show biochemical evidence supporting the role of NifU as the [Fe-S] cluster donor. Protein-protein interaction studies involving apo-NifQ and as-isolated NifU demonstrated their interaction, which was only effective when NifQ lacked its [Fe-S] cluster. Incubation of apo-NifQ with [Fe₄-S₄]-loaded NifU increased the iron content of the former, contingent on both proteins being able to interact with one another. As a result of this interaction, a [Fe₄-S<

SUBMITTER: Barahona E 

PROVIDER: S-EPMC11605450 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature