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.
Stanley, R. J. & van Galen, C. J. in Methods Enzymol. Vol. 620 New Approaches for Flavoenzyme Catalysis (ed Bruce A. Palfey) 215-250 (Elsevier, 2019).
Bialas, C. et al. Ultrafast flavin/tryptophan radical pair kinetics in a magnetically sensitive artificial protein. PCCP 21, 13453-13461, doi:10.1039/c9cp01916b (2019).
Rousseau, B. J. G., Shafei, S., Migliore, A., Stanley, R. J. & Beratan, D. N. Determinants of Photolyase's DNA Repair Mechanism in Mesophiles and Extremophiles. J. Am. Chem. Soc. 140, 2853-2861, doi:10.1021/jacs.7b11926 (2018).
Rohwer, E. J. et al. Dipole Moment and Polarizability of Tunable Intramolecular Charge Transfer States in Heterocyclic pi-Conjugated Molecular Dyads Determined by Computational and Stark Spectroscopic Study. Journal of Physical Chemistry C 122, 9346-9355, doi:10.1021/acs.jpcc.8b02268 (2018).
Munshi, S., Rajamoorthi, A. & Stanley, R. J. Characterization of a cold-adapted DNA photolyase from C-psychrerythraea 34H. Extremophiles 21, 919-932, doi:10.1007/s00792-017-0953-z (2017).