O2-independent formation of the inactive states of NiFe hydrogenase.

Abbas Abou Hamdan, Bénédicte Burlat, Oscar Gutiérrez-Sanz, Pierre-Pol Liebgott, Carole Baffert, Antonio L De Lacey, Marc Rousset, Bruno Guigliarelli, Christophe Léger, Sébastien Dementin

Nature chemical biology 2013 Jan

filter terms:

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 O(2) is not incorporated as an active site ligand but, rather, acts as an electron acceptor. Our findings offer new ways toward the understanding of O(2) inactivation and O(2) tolerance in NiFe hydrogenases.

Citation

Abbas Abou Hamdan, Bénédicte Burlat, Oscar Gutiérrez-Sanz, Pierre-Pol Liebgott, Carole Baffert, Antonio L De Lacey, Marc Rousset, Bruno Guigliarelli, Christophe Léger, Sébastien Dementin. O2-independent formation of the inactive states of NiFe hydrogenase. Nature chemical biology. 2013 Jan;9(1):15-7