Journal
MOLECULAR MICROBIOLOGY
Volume 117, Issue 5, Pages 1080-1088Publisher
WILEY
DOI: 10.1111/mmi.14890
Keywords
Azotobacter vinelandii; FeFe protein; FeV-cofactor; metalloprotein; nitrogen fixation; nitrogenase
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Funding
- Bill and Melinda Gates Foundation [OPP1143172]
- BNF Cereals Phase III [INV-005889]
- U.S Department of Energy, Basic Energy Sciences [DE-SC0010687]
- U.S. Department of Energy (DOE) [DE-SC0010687] Funding Source: U.S. Department of Energy (DOE)
- Bill and Melinda Gates Foundation [INV-005889, OPP1143172] Funding Source: Bill and Melinda Gates Foundation
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Azotobacter vinelandii produces three genetically distinct nitrogenase isozymes, among which Fe-only nitrogenase has lower catalytic activity for N-2 fixation and is only produced when Mo and V are not available.
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 N-2 binding and reduction, are, respectively, designated as FeMo-cofactor, FeV-cofactor, and FeFe-cofactor. Fe-only nitrogenase is a poor catalyst for N-2 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 N-2. 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.
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