Tuning Reactivity of Bioinspired [NiFe]-Hydrogenase Models by Ligand Design and Modeling the CO Inhibition Process

Despite the report of several structural and functional models of the [NiFe]-hydrogenases, it is still unclear how the succession of electron and proton transfers during H2 production catalysis are controlled in terms of both sequence (order of the chemical or redox steps) and sites (metal and/or ligand). To address this issue, the structure of the previously described bioinspired [NiFe]-hydrogenase complex [LN2S2NiIIFeIICp(CO)]+ (LNiIIFeIICp, with LN2S2 = 2,2′-(2,2′-bipyridine-6,6′-diyl)bis(1,1′-diphenylethanethiolate) and Cp = cyclopentadienyl) has been fine-tuned by modifying exclusively the Fe site. In [LN2S2NiIIFeIICp*(CO)]+ (LNiIIFeIICp*, with Cp* = pentamethylcyclopentadienyl), the Cp– ligand has been replaced by Cp*– to change both the redox and structural properties of the overall complex as a consequence of the steric hindrance of Cp*–. The LNiIIFeIICp* complex acts as an efficient electrocatalyst to produce H2. Density functional theory (DFT) calculations support a CEEC cycle, following an init...