INOR 83 |
| To be able to understand and eventually reproduce the function of multielectron redox enzymes is one of the most challenging goals of modern chemistry. We have developed a method to mimic and study the function of redox enzymes by covalently attaching synthetic models of enzyme active sites onto self-assembled monolayer coated electrodes. This method has been used to study a model of the active-site of cytochrome c oxidase, the terminal respiratory enzyme in aerobic organisms. A key function of this enzyme is its ability to reduce oxygen to water without the release of toxic partially reduced oxygen species. Our synthetic model mimics the coordination environments and relative locations of hemea3, CuB, and tyrosine-244 which are the key redox groups known to participate in the oxygen reduction reaction. We have studied the complete model as well as analogs lacking copper and phenol and have found that under the physiologically relevant condition of turnover limiting electr transfer all three redox groups are required to give enhanced selectivity for on the four electron reduction of oxygen to water.
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Young Investigator Symposium
1:30 PM-5:30 PM, Sunday, August 19, 2007 BCEC -- 206 A/B, Oral
Division of Inorganic Chemistry |
