Thesis presented on September 24, 2009
Abstract:
NiFe hydrogenases are unique metalloenzymes that catalyze H+/H2 interconversion with remarkable efficiency close to the thermodynamic potential. Their active site consists of a heterobimetallic complex containing a nickel ion in a sulphur-rich environment connected by two thiolates bridges to an organometallic cyano-carbonyl iron moiety. In order to improve the understanding of the enzymatic mechanism and to obtain new base-metal electrocatalysts for H2 production, we synthesized a series of bio-inspired low molecular weight model complexes with the butterfly structure Ni(µ-S2)M (M= Ru, Mn and Fe). All these compounds displayed a catalytic activity of hydrogen production. Modulating the electronic and steric properties of the ruthenium center allowed optimizing the catalytic performances of these compounds in terms of stability, catalytic rate and overpotential. Mechanistic studies of the catalytic cycle of the Ni-Ru complexes have also been carried out. They allowed us to suggest a bio-relevant bridging hydride as the catalytic intermediate. Finally, we synthesized one of the first Ni-Fe complexes that is both a structural and a functional model of NiFe hydrogenase.
Keywords:
NiFe hydrogenases, H2 production, bioinspired chemistry, electrocatalysis, ruthenium, nickel, fer
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