Thesis presented on September 28, 2006
Abstract:
Hydrogenase enzymes reversibly catalyze the oxidation and production of hydrogen in a range close to the thermodynamic potential. The [NiFe] hydrogenase active site contains an iron-cyano-carbonyl moiety linked to a nickel atom which is in an all sulphur environment. Both the active site originality and the potential development of an hydrogen economy make the synthesis of functional and structural models worthy. To take up this challenge, we have synthesized mononuclear ruthenium models and more importantly, nickel-ruthenium complexes, mimicking some structural features of the [NiFe] hydrogenase active site. Ruthenium is indeed isoelectronic to iron and some of its complexes are well-known to bear hydrides. The compounds described in this study have been well characterized and their activity in proton reduction has been successfully tested. Most of them are able to catalyze this reaction though their electrocatalytic potentials remain much more negative compared to which of platinum. The studied parameters point out the importance of the complexes electron richness, especially of the nickel environment. Furthermore, the proton reduction activity is stable for several hours at good rates. The ruthenium environment seems important for this stability. Altogether, these compounds represent the very first catalytically active [NiFe] hydrogenase models. Important additional results of this study are the synergetic behavior of the two metals in protons reduction and the evidence of a protonation step as the limitating step of the catalytic cycle. We have also shown that a basic site close to ruthenium improves the electrocatalytic potential of the complexes.
Keywords:
Hydrogenases, bio-inspired chemistry, proton reduction, dihydrogen, nickel, ruthénium
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