Biomimics of [FeFe]-hydrogenases incorporating redox-active ligands: Ferrocene-bridged dithiolate complexes [Fe2(CO)6(μ-EC5H4FeC5H4E)] (E = S, Se)

Ferrocene-bridged dithiolate complexes [Fe-2(CO)(6)(mu-EC5H4FeC5H4E)] (E = S, Se) ( 1-2 ) have been stud-ied as biomimics of [FeFe]-hydrogenases, ferrocene taking the role of an Fe4S4 surrogate. Both show a quasi-reversible electron reduction at E-1/2 = -1.81 V and -1.56 V respectively with IR SEC showing that it is Fe-2-based (ca. 50 cm(-1) hypsochromic shift) and leads to a significant structural rearrangement with formation of a bridging carbonyl being at ca. 1715 cm(-1). They also show reversible one-electron oxidation with a small (ca. 15 cm(-1)) hypsochromic nu(CO) shift, showing it is ferrocene-based, while oxidation of the Fe-2 centre occurs outside of the potential window. DFT calculations on 1 show that the HOMO is ferrocene-based, and the LUMO Fe-2-based, both in accord with the IR SEC results. However, the radical anion [1](-) is calculated to have an elongated metal-metal vector rather than a bridging carbonyl, although a complex with an open structure [1(mu-CO)](-) in which one thiolate group moves from a bridging to a terminal position is energetically similar. For 2 , DFT shows the HOMO is Fe-2-based, which is not supported experimentally. Complexes 1-2 are proton-reduction catalysts at their first reduction potential in the presence of trifluoroacetic acid. DFT suggests two competing pathways for H-2 generation catalysed by 1 , occurring upon protonation of either [1](-) or [1(mu-CO)](-) to give bridging and terminal hydride complexes respectively. For 2 , DFT suggests that [2(mu-CO)](-) is only slightly higher in energy than [2](-), probably a result of the weaker Fe-Se vs Fe-S bond, and thus proton-reduction likely proceeds (primarily) through the open-structure isomer. (c) 2022 The Authors. Published by Elsevier B.V. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/)