Specialties
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Biography
InterestsDNA 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. Select PublicationsNarayanan, M., Singh, V.R., Kodali, G., Moravcevic, K. & Stanley, R.J. An Ethenoadenine FAD Analog Accelerates UV Dimer Repair by DNA Photolyase. Photochemistry and Photobiology 93, 343-354 (2017).
Munshi, S., Rajamoorthi, A. & Stanley, R.J. Characterization of a cold-adapted DNA photolyase from C. psychrerythraea 34H. Extremophiles (2017). Pauszek, R.F., Kodali, G., Siddiqui, M.S. & Stanley, R.J. Overlapping Electronic States with Nearly Parallel Transition Dipole Moments in Reduced Anionic Flavin Can Distort Photobiological Dynamics. Jour. of the Amer. Chem. Soc. 138, 14880-14889 (2016). Lee, W., Kodali, G., Stanley, R.J. & Matsika, S. Coexistence of different electron transfer mechanisms in the DNA repair process by photolyase. Chemistry - A European Journal 22, 11371-11381 (2016). Gindt, Y.M. et al. 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? Journal of Physical Chemistry B 120, 10234-10242 (2016). Pauszek, R.F. & Stanley, R.J. A "How-To" Guide to the Stark Spectroscopy of Flavins and Flavoproteins. in Flavins and Flavoproteins: Methods and Protocols, Vol. 1146 (eds. Weber, S. & Schleicher, E.) 443-466 (2014). |
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