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Título: | AnfO controls fidelity of nitrogenase FeFe protein maturation by preventing misincorporation of FeV-cofactor |
Autor: | Pérez-González, Ana; Jiménez-Vicente, Emilio; Salinero-Lanzarote, Alvaro; Harris, Derek F; Seefeldt, Lance C.; Dean, Dennis R. | Palabras clave: | Azotobacter vinelandii FeFe protein FeV-cofactor Metalloprotein Nitrogen fixation Nitrogenase |
Fecha de publicación: | 27-feb-2022 | Editor: | John Wiley & Sons | Citación: | Molecular Microbiology 00:1–9 (2022) | Resumen: | 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. | Versión del editor: | https://doi.org/10.1111/mmi.14890 | URI: | http://hdl.handle.net/10261/269355 | DOI: | 10.1111/mmi.14890 | ISSN: | 0950-382X |
Aparece en las colecciones: | (INIA) Artículos |
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AnfO-controls-fidelit- of-nitrogenase.pdf | artículo | 637,2 kB | Adobe PDF | Visualizar/Abrir |
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