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.
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