Abstract
Abstract[NiFe]‐hydrogenase enzymes are efficient catalysts for H2 evolution but their synthetic models have not been reported to be active under aqueous conditions so far. Here we show that a close model of the [NiFe]‐hydrogenase active site can work as a very active and stable heterogeneous H2 evolution catalyst under mildly acidic aqueous conditions. Entry in catalysis is a NiIFeII complex, with electronic structure analogous to the Ni‐L state of the enzyme, corroborating the mechanism modification recently proposed for [NiFe]‐hydrogenases.
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