Skip to Main content Skip to Navigation
Journal articles

O2-independent formation of the inactive states of NiFe hydrogenase

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.
Complete list of metadata
Contributor : LAURE AZZOPARDI Connect in order to contact the contributor
Submitted on : Wednesday, July 5, 2017 - 4:29:54 PM
Last modification on : Tuesday, October 19, 2021 - 10:50:10 PM




Abbas Abou Hamdan, Benedicte Burlat, Oscar Gutierrez-Sanz, Pierre-Pol Liebgott, Carole Baffert, et al.. O2-independent formation of the inactive states of NiFe hydrogenase. Nature Chemical Biology, Nature Publishing Group, 2013, 9 (1), pp.15 - 17. ⟨10.1038/nchembio.1110⟩. ⟨hal-01556905⟩



Record views