CHED 846 |
| FeFe-hydrogenases manifest an exceptionally high catalytic rate of proton reduction. The metalloenzyme's active site (H-cluster) contains iron-sulfur clusters and biologically unusual cyanide and carbonyl ligands and a yet to be determined bridging ligand. Such chemical composition would be a desirable starting point for developing biomimetic compounds for hydrogen uptake and evolution reactions using inexpensive, iron-based complexes. The aim of our work is to contribute to the rationalized catalyst design employing in lumeno and in silico approaches. Exploiting the complementarity of the metalloprotein and biomimetic chemistry, as well as the synchrotron-based techniques and computational methods, we aim to define the catalytic wave function that is responsible for the high activity. Our recent results will be summarized on eliminating structural uncertainties, the role of the tetranuclear iron-sulfur cluster, and developing a 220 atom in silico model that looks and acts like the H-cluster.
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Exploring and Exploiting Nature with Biomimetics
1:30 PM-4:45 PM, Monday, March 26, 2007 McCormick Place North -- Room N230A, Level 2, Oral
Division of Chemical Education |
