Biophysical Chemistry

Temple University Department of Chemistry

DNA photolyase binds its substrate by base flipping. We explore this process using fluorescent base analogs like 2-aminopurine. 1789-1793 (2004)

 

Research Projects

* 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 flavoprotein 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 and biochemical techniques to unravel this mechanism. We also explore the details of substrate binding using state of the art fluorescence reporter, two photon excitation techniques, and single molecule microscopy.

* 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.

* Fluorescent base analogs are widely used in biotechnology. We are exploring the excited state electronic properties of these analogs to be able to develop design motifs to improve and control their properties.

Robert J Stanley, Ph.D.

250B Beury Hall

Department of Chemistry

1901 N. 13th St.

Philadelphia PA 19122

To contact us:

Phone: 215-204-2027

Fax: 215-204-1532

E-mail: rstanley@temple.edu

Mees et al, Science v. 306, pp 1789-1793 (2004)

FAD binding site showing highly conserved Leu, Asn, Arg, Ala, and Asp residues within about 5 Å of the FAD