1h5d
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| , resolution 1.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , and | ||||||
| Activity: | Peroxidase, with EC number 1.11.1.7 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
X-RAY INDUCED REDUCTION OF HORSERADISH PEROXIDASE C1A COMPOUND III (0-11% DOSE)
OverviewOverview
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.
About this StructureAbout this Structure
1H5D is a Single protein structure of sequence from Armoracia rusticana. Full crystallographic information is available from OCA.
ReferenceReference
The catalytic pathway of horseradish peroxidase at high resolution., Berglund GI, Carlsson GH, Smith AT, Szoke H, Henriksen A, Hajdu J, Nature. 2002 May 23;417(6887):463-8. PMID:12024218
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