AnfO Controls Fidelity of Nitrogenase FeFe Protein Maturation by Preventing Misincorporation Of FeV-Cofactor
Document Type
Article
Journal/Book Title
Molecular Microbiology
Publication Date
2-27-2022
Publisher
Wiley-Blackwell Publishing Ltd.
Volume
117
Issue
5
First Page
1080
Last Page
1088
Abstract
Azotobacter vinelandii produces three genetically distinct, but structurally and mechanistically similar nitrogenase isozymes designated as Mo-dependent, V-dependent, or Fe-only based on the heterometal contained within their associated active site cofactors. These catalytic cofactors, which provide the site for N2 binding and reduction, are, respectively, designated as FeMo-cofactor, FeV-cofactor, and FeFe-cofactor. Fe-only nitrogenase is a poor catalyst for N2 fixation, when compared to the Mo-dependent and V-dependent nitrogenases and is only produced when neither Mo nor V is available. Under conditions favoring the production of Fe-only nitrogenase a gene product designated AnfO preserves the fidelity of Fe-only nitrogenase by preventing the misincorporation of FeV-cofactor, which results in the accumulation of a hybrid enzyme that cannot reduce N2. These results are interpreted to indicate that AnfO controls the fidelity of Fe-only nitrogenase maturation during the physiological transition from conditions that favor V-dependent nitrogenase utilization to Fe-only nitrogenase utilization to support diazotrophic growth.
Recommended Citation
Pérez-González, A., Jimenez-Vicente, E., Salinero-Lanzarote, A., Harris, D. F., Seefeldt, L. C., and Dean, D. R. (2022) AnfO controls fidelity of nitrogenase FeFe protein maturation by preventing misincorporation of FeV-cofactor. Molecular Micro.117, 1080–1088.
