The active site of the [FeFe]-hydrogenase enzyme (found in the anaerobic bacteria Clostridium pasteurianum (Cpl) and Desulfovibrio desulfuricans (Ddh)) reversibly catalyzes the activation of hydrogen according to the equation: H2 ↔ 2H+ + 2e-. Structural and functional models of the general formula (μ-Rdt)[FeL3]2 are showing great promise as iron-based catalysts and could potentially replace platinum analogs, thereby making proposed hydrogen fuel cells an economically feasible, renewable energy source. Our research is focused on investigating the wavelength dependent role of light, which is required to drive the Hydrogen Evolution Reaction (HER) in [FeFe]-hydrogenase models. It is hypothesized that wavelength dependent photolysis of (μ-pdt)[Fe(CO)2(PMe3)]2 in the presence of H2 will remove a CO ligand. Using FTIR and Uv-vis spectroscopy, results will be presented demonstrating the photochemical activity of (μ-pdt)[Fe(CO)2(PMe3)]2, which is wavelength and solvent dependent; additionally, properties of the possible photoproducts will be explored, which will help us elucidate a mechanism of hydrogen activation.

Photo-activation of hydrogen by an [FeFe]-hydrogenase model complex

251st National Meeting (2016)

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