Cross‐Coupling of Mo‐ and V‐Nitrogenases Permits Protein‐Mediated Protection from Oxygen Deactivation

Article Article scientifique Article Cross‐Coupling of Mo‐ and V‐Nitrogenases Permits Protein‐Mediated Protection from Oxygen Deactivation eng 2024-11-23 2024-12-02 author Ratcliff Daniel Department of Inorganic and Analytical Chemistry, Faculty of Science, University of Geneva, Quai Ernest-Ansermet 30, 1205, Geneva, Switzerland.,National Centre of Competence in Research (NCCR) Catalysis, University of Geneva, Switzerland. 852227 Chimie analytique groupe 4 (CHIAL4) author Sedoh Gloria Candy Danielle Department of Inorganic and Analytical Chemistry, Faculty of Science, University of Geneva, Quai Ernest-Ansermet 30, 1205, Geneva, Switzerland.,National Centre of Competence in Research (NCCR) Catalysis, University of Geneva, Switzerland.,Present address: Department of Physical Chemistry, Faculty of Sciences, University of Geneva, Quai Ernest-Ansermet 30, 1205, Geneva, Switzerland. 900500 Chimie physique (groupe 9) (CHIF9) author Milton Ross Dean 0000-0002-2229-0243 Department of Inorganic and Analytical Chemistry, Faculty of Science, University of Geneva, Quai Ernest-Ansermet 30, 1205, Geneva, Switzerland.,National Centre of Competence in Research (NCCR) Catalysis, University of Geneva, Switzerland. 930839 Services communs du dépt. de chimie minérale et analytique (CHIMO) e202400585 10.1002/cbic.202400585 39500732 1439-4227 https://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/cbic.202400585 Nitrogenases catalyze dinitrogen (N2 ) fixation to ammonia (NH3 ). While these enzymes are highly sensitive to deactivation by molecular oxygen (O2 ) they can be produced by obligate aerobes for diazotrophy, necessitating a mechanism by which nitrogenase can be protected from deactivation. In the bacterium Azotobacter vinelandii, one mode of such protection involves an O2 -responsive ferredoxin-type protein ("Shethna protein II", or "FeSII") which is thought to bind with Mo-dependent nitrogenase's two component proteins (NifH and NifDK) to form a catalytically stalled yet O2 -tolerant tripartite protein complex. This protection mechanism has been reported for Mo-nitrogenase, however, in vitro assays with V-nitrogenase suggest that this mechanism is not universal to the three known nitrogenase isoforms. Here we report that the reductase of the V-nitrogenase (VnfH) can engage in this FeSII-mediated protection mechanism when cross-coupled with Mo-nitrogenase NifDK. Interestingly, the cross-coupling of the Mo-nitrogenase reductase NifH with the V-nitrogenase VnfDGK protein does not yield such protection. Ammonia FeSII Nitrogenase Oxygen Shethna Dewey 540 Swiss National Science Foundation NCCR Catalysis (phase I) 180544 CH Programmes 40 Département de chimie minérale, analytique et appliquée 145 false ChemBioChem 25 23 6e3d6d4c-e0e3-4af0-bc5f-20eb48de2f98 Article (Published version) Restricted file.pdf 853613 application/pdf 3c16480b3057c89eb1ae575de2dffe0c3c6d352bbe2fc899efeedc23b222b054 restrictedAccess Faculté des sciences / Section de chimie et biochimie / Département de chimie minérale, analytique et appliquée

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Cross‐Coupling of Mo‐ and V‐Nitrogenases Permits Protein‐Mediated Protection from Oxygen Deactivation	ChemBioChem			2024	33	0

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Sedoh, Gloria Candy Danielle