[FeFe] hydrogenase is a responsible for the reversible catalytic oxidation of H2 in anaerobic organisms. Many synthetic models of the active site of [FeFe] hydrogenase have been reported. However, these models generally reduce at potentials over an order of magnitude more negative than the metalloenzyme (�0.4 V vs. NHE). We therefore hypothesize the protein environment must be important for tuning the redox potential of the active site. Enveloping the metal center in an environment comparable to that afforded by the enzyme's polypeptide should permit the model complex to reduce at milder potentials and achieve a turn-over frequency for H2 production similar to [FeFe] Hydrogenase. We report here the preparation and characterization of various reversibly collapsible polymer-bound diiron cluster model complexes. X-ray crystallography, 1H NMR and IR spectroscopy were used to verify the structure of the diiron center. Polymer molecular weight distribution and conformation (chain/nanoparticle) were determined by GPC.

Design and synthesis of polymer-bound azadithiodiiron clusters to model [FeFe] hydrogenase

248th National Meeting (2014)

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