Interplay of hemilability and redox activity in models of hydrogenase active sites

Abstract

The hydrogen evolution reaction, as catalyzed by two electrocatalysts [M(N2S2)·Fe(NO)2]+, [Fe-Fe]+ (M = Fe(NO)) and [Ni-Fe]+ (M = Ni) was investigated by computational chemistry. As nominal models of hydrogenase active sites, these bimetallics feature two kinds of actor ligands: Hemilabile, MN2S2 ligands and redox-active, nitrosyl ligands, whose interplay guides the H2 production mechanism. The requisite base and metal open site are masked in the resting state but revealed within the catalytic cycle by cleavage of the MS–Fe(NO)2 bond from the hemilabile metallodithiolate ligand. Introducing two electrons and two protons to [Ni-Fe]+ produces H2 from coupling a hydride temporarily stored on Fe(NO)2 (Lewis acid) and a proton accommodated on the exposed sulfur of the MN2S2 thiolate (Lewis base). This Lewis acid–base pair is initiated and preserved by disrupting the dative donation through protonation on the thiolate or reduction on the thiolate-bound metal. Either manipulation modulates the electron density of the pair to prevent it from reestablishing the dative bond. The electron-buffering nitrosyl’s role is subtler as a bifunctional electron reservoir. With more nitrosyls as in [Fe-Fe]+, accumulated electronic space in the nitrosyls’ π*-orbitals makes reductions easier, but redirects the protonation and reduction to sites that postpone the actuation of the hemilability. Additionally, two electrons donated from two nitrosyl-buffered irons, along with two external electrons, reduce two protons into two hydrides, from which reductive elimination generates H2.