Synthesis and Electrochemical Investigations of the [FeFe]‐Hydrogenase H‐Cluster Mimics Mediated by Bicyclic Dithiols Derivative

Biomimic of the active site of [FeFe]‐hydrogenase containing bicyclic dithiols as bridging linker has been synthesized and characterized using different spectroscopic methods. The influence of this linker on the redox properties and the catalytic behavior of the resulted binuclear complex was investigated using cyclic voltammetry, showing that it can catalyze the reduction of protons to H2 in the presence of acetic acid (AcOH). Moreover, the results revealed that the bicyclic dithiolene linker has improved the chemical stability of the reduced species and caused a shift to less negative potential in comparison to the synthetic models that mimic the active site of [FeFe]‐hydrogenase reported in the literature. In addition, the structure of the resulted binuclear complex mediated by bicyclic dithiols as bridging linker was confirmed by X‐ray diffraction analysis.