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| Robert J. Stanley, Ph.D. Associate Professor Physical/Biophysical Chemistry 248 Beury Hall (215) 204-2027 |  |
| - A principal focus of our group is to understand the mechanism of DNA repair by the light-driven enzyme, DNA photolyase. DNA is often damaged by UV radiation that is not otherwise absorbed by the ozone layer. Photolyase is a FAD-containing protein that uses light to drive an ultrafast electron transfer reaction between the protein and the bound DNA lesion. The transferred electron repairs the damaged DNA by an unknown mechanism. We are using ultrafast laser techniques to unravel this mechanism.
DNA Photolyase crystal structure from Kim et al (Science, 268, pp. 1866-72 (1995)) - A second area of interest centers around the electronic properties of flavins in flavoproteins. The redox properties of flavoenzymes are known to be sensitive to electronic interactions between the flavin cofactor and the protein host. We are studying these interactions quantitatively using Stark spectroscopy.
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updated 04/25/04 |