A current goal of catalysis is to develop first-row transition metals that by virtue of fortunate molecular combinations might perform small molecule transformations that typically require the 2-electron redox conversions of heavier metals such as palladium or platinum.  To illicit such reactivity in iron or nickel, nature has assembled two metals in close proximity as in the [NiFe]- and [FeFe]-hydrogenases, [NiNi]-ACS (acetyl-co-A synthase) or [NiFex]-CODH (carbon monoxide dehydrogenase).  Such catalytic sites, isolated in evolutionarily designed pockets within protein folds, and characterized by crystallography and various spectroscopies, compel computational chemists to explore their mechanism of action.  Thus a synergy between theory and experiment has developed for the hydrogen-producing /hydrogen-oxidation hydrogenase enzymes.  By defining the requirements for catalysis made more or less clear by the structure of the enzyme, biomimetics may be designed to merge synthetic chemical possibilities with the biochemical or natural design.   We synthesize thiolate-S bridged diiron complexes that are inspired by the [FeFe]- and [NiFe]-H2ase active sites  and submit them to functional, electrochemical and spectroscopic studies with tuning of properties as suggested by computations from the M.B. Hall group.

Synthesis of biomimetics of hydrogenases:  Synergy with computational modeling

248th National Meeting (2014)

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