Abstract
We studied the mechanism of aerobic inactivation of Desulfovibrio fructosovorans nickel-iron (NiFe) hydrogenase by quantitatively examining the results of electrochemistry, EPR and FTIR experiments. They suggest that, contrary to the commonly accepted mechanism, the attacking O2 is not incorporated as an active site ligand but, rather, acts as an electron acceptor. Our findings offer new ways toward the understanding of O2 inactivation and O2 tolerance in NiFe hydrogenases.
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Acknowledgements
We thank J. Hadj-Saïd for performing preliminary electrochemical experiments and P. Bertrand, V. Fourmond and V. Fernández for helpful discussions. This work was funded by the CNRS, the Agence Nationale de la Recherche, the Aix-Marseille Université, the City of Marseilles and the Spanish Ministerio de Ciencia e Innovación (MICINN) (project CTQ2009-12649) and was supported by the Pôle de Compétitivité Capénergies. A.A.H. thanks the CNRS and the Région Provence-Alpes Côte d'Azur for financial support. O.G.-S. thanks the MICINN for a Formación de Personal Investigador (FPI) grant.
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A.A.H. carried out the enzyme purification, electrochemical and EPR experiments, and analyzed the data with the support of S.D., M.R., C.B., C.L., B.B. and B.G. O.G.-S. performed FTIR experiments and analyzed the data with the support of A.L.D.L. P.-P.L. performed preliminary electrochemical experiments and analyzed the data. The research was designed by A.A.H., B.B., M.R., B.G., C.L. and S.D. S.D. and C.L. wrote the manuscript.
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Abou Hamdan, A., Burlat, B., Gutiérrez-Sanz, O. et al. O2-independent formation of the inactive states of NiFe hydrogenase. Nat Chem Biol 9, 15–17 (2013). https://doi.org/10.1038/nchembio.1110
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DOI: https://doi.org/10.1038/nchembio.1110
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