Dynamics and mechanism of repair of ultraviolet-induced (6–4) photoproduct by photolyase

Jiang Li, Zheyun Liu, Chuang Tan, Xunmin Guo, Lijuan Wang, Aziz Sancar and Dongping Zhong ()
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Jiang Li: Chemistry and Biochemistry, Programs of Biophysics, Chemical Physics and Biochemistry, 191 West Woodruff Avenue, The Ohio State University
Zheyun Liu: Chemistry and Biochemistry, Programs of Biophysics, Chemical Physics and Biochemistry, 191 West Woodruff Avenue, The Ohio State University
Chuang Tan: Chemistry and Biochemistry, Programs of Biophysics, Chemical Physics and Biochemistry, 191 West Woodruff Avenue, The Ohio State University
Xunmin Guo: Chemistry and Biochemistry, Programs of Biophysics, Chemical Physics and Biochemistry, 191 West Woodruff Avenue, The Ohio State University
Lijuan Wang: Chemistry and Biochemistry, Programs of Biophysics, Chemical Physics and Biochemistry, 191 West Woodruff Avenue, The Ohio State University
Aziz Sancar: University of North Carolina School of Medicine
Dongping Zhong: Chemistry and Biochemistry, Programs of Biophysics, Chemical Physics and Biochemistry, 191 West Woodruff Avenue, The Ohio State University

Nature, 2010, vol. 466, issue 7308, 887-890

Abstract: DNA repair: key histidine residue The enzyme (6-4) photolyase utilizes blue-light energy to repair DNA damage by cleaving the ultraviolet-induced bond between pyrimidine dimers. Ultrafast spectroscopy has now been used to examine the detailed electron and proton movements during the repair photocycle. Histidine 364 is identified as the crucial residue involved in the rate-limiting step.

Date: 2010
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DOI: 10.1038/nature09192

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