Robert J. Stanley


Robert Stanley

Associate Professor

A.B. ('78), University of California - Berkeley
M.Sc. ('83) University of Colorado - Boulder
Ph.D. ('91) Pennsylvania State University - University Park

Beury Hall 250B


Department of Chemistry
Beury Hall 130
1901 N. 13th Street
Philadelphia, PA 19122


office: 215-204-2027
fax: 215-204-0478
lab: 215-204-7114, -6320




Biological / Photonics / Physical

Research Interests

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 (flavo)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 and biochemical techniques to unravel this mechanism. We also explore the details of substrate binding using state of the art fluorescence reporter and two photon excitation techniques.

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.



Selected Publications

Yu, X.; Eymur, S.; Singh, V.; Yang, B. Q.; Tonga, M.; Bheemaraju, A.; Cooke, G.; Subramani, C.; Venkataraman, D.; Stanley, R. J.; Rotello, V. M. "Flavin as a photo-active acceptor for efficient energy and charge transfer in a model donor-acceptor system." Physical Chemistry Chemical Physics (2012), 14 (19), 6749-6754.

Kodali, G.; Narayanan, M.; Stanley, R. J. "The Excited State Electronic Properties of 6-Methylisoxanthopterin (6-MI): An Experimental and Theoretical Study." The Journal of Physical Chemistry B (2012), 116 (9), 2981-2989.  


Narayanan, M.; Kodali, G.; Xing, Y.; Stanley, R. J. "Photoinduced electron transfer occurs between 2-aminopurine and the DNA nucleic acid monophosphates: results from cyclic voltammetry and fluorescence quenching." Journal of Physical Chemistry B (2010), 114 (32), 10573-10580.


Narayanan, M.; Kodali, G.; Xing, Y.; Hawkins, M. E.; Stanley, R. J. "Differential Fluorescence Quenching of Fluorescent Nucleic Acid Base Analogues by Native Nucleic Acid Monophosphates." The Journal of Physical Chemistry B (2010), 114 (17), 5953-5963.


Kodali, G.; Siddiqui, S. U.; Stanley, R. J. "Charge Redistribution in Oxidized and Semiquinone E. coli DNA Photolyase upon Photoexcitation: Stark Spectroscopy Reveals a Rationale for the Position of Trp382." J. Am. Chem. Soc. (2009), 131 (13), 4795-4807.


Yang, K.; Matsika, S.; Stanley, R. J. "6MAP, a fluorescent adenine analogue, is a probe of base flipping by DNA photolyase." Journal of Physical Chemistry, B (2007), 111 (35), 10615-10625.


Stanley, R. J.; Hou, Z.; Yang, A.; Hawkins, M. E. "The Two-Photon Excitation Cross Section of 6MAP, a Fluorescent Adenine Analogue." Journal of Physical Chemistry B (2005), 109 (8), 3690-3695.

MacFarlane IV, A. W.; Stanley, R. J. "Cis-Syn Thymidine Dimer Repair by DNA Photolyase in Real Time." Biochemistry (2003), 42 (28), 8558-8568.

Hopkins, N.; Stanley, R. J. "Measurement of the Electronic Properties of the Flavoprotein Old Yellow Enzyme (OYE) and the OYE:p-Cl Phenol Charge-Transfer Complex Using Stark Spectroscopy." Biochemistry (2003), 42 (4), 991-999.


Christine, K. S.; MacFarlane IV, A. W.; Yang, K.; Stanley, R. J. "Cyclobutylpyrimidine Dimer Base Flipping by DNA Photolyase." Journal of Biological Chemistry (2002), 277 (41), 38339-38344.

Stanley, R. J.; Siddiqui, M. S. "A Stark Spectroscopic Study of N(3)-Methyl, N(10)-Isobutyl-7,8-Dimethylisoalloxazine in Nonpolar Low-Temperature Glasses: Experiment and Comparison with Calculations." Journal of Physical Chemistry A (2001), 105 (49), 11001-11008.

MacFarlane IV, A. W.; Stanley, R. J., "Evidence of Powerful Substrate Electric Fields in DNA Photolyase: Implications for Thymidine Dimer Repair." Biochemistry (2001), 40 (50), 15203-15214.