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

Author

Listed:
  • 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)

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.

Suggested Citation

  • Jiang Li & Zheyun Liu & Chuang Tan & Xunmin Guo & Lijuan Wang & Aziz Sancar & Dongping Zhong, 2010. "Dynamics and mechanism of repair of ultraviolet-induced (6–4) photoproduct by photolyase," Nature, Nature, vol. 466(7308), pages 887-890, August.
    • Handle: RePEc:nat:nature:v:466:y:2010:i:7308:d:10.1038_nature09192
    DOI: 10.1038/nature09192
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