DNA is often damaged by UV radiation penetrating the ozone layer. The Stanley group uses ultrafast laser spectroscopy and biochemistry to understand the mechanism of DNA repair by DNA photolyase. Photolyase is a flavoprotein that uses light to drive an photoinduced electron transfer reaction repairing the bound DNA lesion. We are using ultrafast laser and biochemical techniques to unravel the substrate binding and repair mechanism.
We are also interested in how the redox properties of flavoenzymes are tuned by the protein binding site. We are studying these interactions quantitatively using Stark spectroscopy.
Overlapping Electronic States with Nearly Parallel Transition Dipole Moments in Reduced Anionic Flavin Can Distort Photobiological Dynamics
Pauszek, R. F., G. Kodali, M. S. U. Siddiqui and R. J. Stanley
J. Am. Chem. Soc. 138, 14880-14889 (2016).
The Missing Electrostatic Interactions Between DNA Substrate and Sulfolobus solfataricus DNA Photolyase: What is the Role of Charged Amino Acids in Thermophilic DNA Binding Proteins?
Gindt, Y. M., B. H. Edani, A. Olejnikova, A. N. Roberts, S. Munshi and R. J. Stanley
J. Phys. Chem. B 120, 10234-10242 (2016).
Excited State Charge Redistribution and Dynamics in the Donor-pi-Acceptor Flavin Derivative ABFL
Pauszek, R. F., G. Kodali, S. T. Caldwell, B. Fitzpatrick, N. Y. Zainalabdeen, G. Cooke, V. M. Rotello and R. J. Stanley
J. Phys. Chem. B 117, 15684-15694 (2013).