The catalytic pathway of horseradish peroxidase at high resolution

Gunnar I. Berglund, Gunilla H. Carlsson, Andrew T. Smith, Hanna Szöke, Anette Henriksen and Janos Hajdu ()
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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
Anette Henriksen: University of Copenhagen
Janos Hajdu: Uppsala University, Biomedical Center

Nature, 2002, vol. 417, issue 6887, 463-468

Abstract: 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.

Date: 2002
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DOI: 10.1038/417463a

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