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Journal of Nucleic Acids
Volume 2010 (2010), Article ID 794782, 7 pages
Review Article

The Roles of Several Residues of Escherichia coli DNA Photolyase in the Highly Efficient Photo-Repair of Cyclobutane Pyrimidine Dimers

1Institute of Molecular Biology and Biotechnology, Anhui Normal University, Wuhu 241000, China
2Department of Basic Medicine, Wannan Medical College, Wuhu, Anhui 241002, China

Received 14 March 2010; Revised 7 July 2010; Accepted 7 August 2010

Academic Editor: Shigenori Iwai

Copyright © 2010 Lei Xu and Guoping Zhu. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Escherichia coli DNA photolyase is an enzyme that repairs the major kind of UV-induced lesions, cyclobutane pyrimidine dimer (CPD) in DNA utilizing 350–450 nm light as energy source. The enzyme has very high photo-repair efficiency (the quantum yield of the reaction is ~0.85), which is significantly greater than many model compounds that mimic photolyase. This suggests that some residues of the protein play important roles in the photo-repair of CPD. In this paper, we have focused on several residues discussed their roles in catalysis by reviewing the existing literature and some hypotheses.