O-2-independent formation of the inactive states of NiFe hydrogenase

[摘要]：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.

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