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The catalytic pathway of horseradish peroxidase at high resolution

Author

Listed:
  • Gunnar I. Berglund

    (Uppsala University, Biomedical Center)

  • Gunilla H. Carlsson

    (Uppsala University, Biomedical Center)

  • Andrew T. Smith

    (University of Sussex)

  • Hanna Szöke

    (Uppsala University, Biomedical Center
    Lawrence Livermore National Laboratory)

  • Anette Henriksen

    (University of Copenhagen
    Carlsberg Laboratory)

  • Janos Hajdu

    (Uppsala University, Biomedical Center)

Abstract

A molecular description of oxygen and peroxide activation in biological systems is difficult, because electrons liberated during X-ray data collection reduce the active centres of redox enzymes catalysing these reactions1,2,3,4,5. Here we describe an effective strategy to obtain crystal structures for high-valency redox intermediates and present a three-dimensional movie of the X-ray-driven catalytic reduction of a bound dioxygen species in horseradish peroxidase (HRP). We also describe separate experiments in which high-resolution structures could be obtained for all five oxidation states of HRP, showing such structures with preserved redox states for the first time.

Suggested Citation

  • Gunnar I. Berglund & Gunilla H. Carlsson & Andrew T. Smith & Hanna Szöke & Anette Henriksen & Janos Hajdu, 2002. "The catalytic pathway of horseradish peroxidase at high resolution," Nature, Nature, vol. 417(6887), pages 463-468, May.
    • Handle: RePEc:nat:nature:v:417:y:2002:i:6887:d:10.1038_417463a
    DOI: 10.1038/417463a
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