1hch
STRUCTURE OF HORSERADISH PEROXIDASE C1A COMPOUND I
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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
1HCH is a [Single protein] structure of sequence from [Armoracia rusticana] with ACT, CA, HEM and O as [ligands]. Active as [Peroxidase], with EC number [1.11.1.7]. Structure known Active Site: CAA. 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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