Biomimetics of the [FeFe]-H2ase enzyme active site (EAS)
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In this project funded by the Chemical Synthesis Program of the Chemistry Division, Professor Marcetta Y. Darensbourg of the Department of Chemistry at Texas A & M University will develop synthetic analogues of the iron- and nickel-containing active sites of hydrogen-processing biocatalysts known as Hydrogenases. The PI''s group reproduces almost precise structural models of the unique and illusive "rotated" structure found in the diiron hydrogenase, and displayed in the as-isolated, mixed-valent FeIIFeI state of the enzyme. In depth analysis of the electronic structure of the models by MÃ¶ssbauer, EPR (ENDOR), and computational chemistry stimulates the design of advanced biomimetics, and its ability to serve as hydrogen-evolving electrocatalysts will be screened by cyclic voltammetry. Through continued collaborations, such catalysts will be analyzed for electronic structures and for applications to dye-sensitized photocatalysis. The PI''s group is diverse and contributes to the annual Chemistry Open House, the Expanding Your Horizons program for 6th grade girls, and other outreach programs, such as NOBCChE. In a broad scope, this work addresses the role of hydrogen as an energy vector--in energy storage applications, and the need for sustainable catalysts in both the production and utilization of hydrogen. The sustainable energy-related research area impacts society as a whole and represents cross-disciplinary and collaborative training opportunities for students. The research inspires coworkers to gain a broad scientific knowledge base in chemistry, biology, spectroscopy, theory, etc., and to be ever alert for the universal language of science, chemistry in particular, for the solving of problems.