1hch | pdb_00001hch
STRUCTURE OF HORSERADISH PEROXIDASE C1A COMPOUND I
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| 1hch, resolution 1.57Å | |||||||||||||
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| Sites: | CAA | ||||||||||||
| Ligands: | ACT, CA, HEM, O | ||||||||||||
| Activity: | Peroxidase, with EC number 1.11.1.7 | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Overview
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 Structure
1HCH is a Single protein structure of sequence from Armoracia rusticana. Full crystallographic information is available from OCA.
Reference
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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