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Iron-catalysed oxidation intermediates captured in a DNA repair dioxygenase

Author

Listed:
  • Chengqi Yi

    (The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA)

  • Guifang Jia

    (The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA)

  • Guanhua Hou

    (University of Wisconsin, 1101 University Avenue)

  • Qing Dai

    (The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA)

  • Wen Zhang

    (The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA)

  • Guanqun Zheng

    (The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA)

  • Xing Jian

    (The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA)

  • Cai-Guang Yang

    (The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA
    Shanghai Institute of Materia Medica, Chinese Academy of Sciences, 555 Zuchongzhi Road, Shanghai 201203, China)

  • Qiang Cui

    (University of Wisconsin, 1101 University Avenue)

  • Chuan He

    (The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA)

Abstract

Oxidation intermediates in a DNA repair dioxygenase The AlkB type proteins are demethylases that are thought to play a part in DNA repair by oxidatively removing methyl adducts on DNA, RNA and histones. Yi et al. have determined the structure of AlkB oxygenase crystallized in complex with various modified DNAs. By growing the crystals under anaerobic conditions and then exposing them to dioxygen to initiate oxidation, two different intermediates were trapped. A third type of intermediate was determined using additional computational analysis. These structures provide detailed mechanistic insight into how these enzymes perform oxidative demethylation.

Suggested Citation

  • Chengqi Yi & Guifang Jia & Guanhua Hou & Qing Dai & Wen Zhang & Guanqun Zheng & Xing Jian & Cai-Guang Yang & Qiang Cui & Chuan He, 2010. "Iron-catalysed oxidation intermediates captured in a DNA repair dioxygenase," Nature, Nature, vol. 468(7321), pages 330-333, November.
    • Handle: RePEc:nat:nature:v:468:y:2010:i:7321:d:10.1038_nature09497
    DOI: 10.1038/nature09497
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