The nature of the bridging dithiolate has an important role on tuning the physical and electrochemical properties of the synthetic H-cluster mimics of [FeFe]-hydrogenase and still of significant concern to scientists. In this report we describe the synthetic models of the active site of [FeFe]-hydrogenase containing perylene monoimide of peri-substituted disulfides as bridging linker. The resulting complexes were characterized by 1H and 13C­{1H} NMR and IR spectroscopic techniques, mass spectrometry, and elemental analysis as well as X-ray analysis of complex 2a. The purpose of this work was to investigate the influence of the perylene-linker on the redox potentials of the complexes and their catalytic ability in the presence of acetic acid (AcOH) by applying cyclic voltammetry. Moreover, we compare these results with different diiron hexacarbonyl complexes previously reported in the literature. As a result, we have found that the presence of the rylene-linker provides further stability for the reduced species and shifted its reduction potentials to more positive values.