[FeFe]-hydrogenases are capable of reversibly catalyzing the reduction of protons to hydrogen gas, 2H+ + 2e- ↔ H2, in a reaction that occurs under mild conditions. A variety of functional mimics of the hydrogenase active site have been successfully designed and synthesized in this rapidly growing field of study. These functional mimics are an attractive target to link to artificial photosynthetic systems for the development of new photocatalytic biohybrid complexes. In this work, diiron complexes, mimics of the [FeFe]-hydrogenase, were synthesized and characterized using electronic absorption and IR spectroscopies in combination with NMR and mass spectrometry. The complexes Fe2(μ-S2)(CO)6 and Fe2(μ-pdt)(CO)6 (pdt = SCH2CH2CH2S) were then investigated for their ability to interact with select peptides to provide a better understanding of how the protein environment may tune [FeFe] hydrogenase active sites.

Synthesis and characterization of diiron complexes: Structural mimics of [FeFe]-hydrogenase

2019 Spring National Meeting

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