The catalytic pathway of horseradish peroxidase at high resolution

Nature. 2002 May 23;417(6887):463-8. doi: 10.1038/417463a.


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 reactions. 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Catalysis / radiation effects
  • Crystallization
  • Crystallography, X-Ray
  • Horseradish Peroxidase / chemistry*
  • Horseradish Peroxidase / metabolism*
  • Iron / chemistry
  • Iron / metabolism
  • Models, Molecular
  • Oxidation-Reduction / radiation effects
  • Oxygen / metabolism*
  • Protein Conformation / radiation effects
  • X-Rays


  • Iron
  • Horseradish Peroxidase
  • Oxygen

Associated data

  • PDB/1H55
  • PDB/1H57
  • PDB/1H58
  • PDB/1H5A
  • PDB/1H5C
  • PDB/1H5D
  • PDB/1H5E
  • PDB/1H5F
  • PDB/1H5G
  • PDB/1H5H
  • PDB/1H5I
  • PDB/1H5J
  • PDB/1H5L
  • PDB/1H5M
  • PDB/1HCH