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1h5h

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[[Category: x-ray induced reduction]]
[[Category: x-ray induced reduction]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:22:17 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 16:29:35 2007''

Revision as of 14:24, 5 November 2007


1h5h, resolution 1.60Å

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X-RAY INDUCED REDUCTION OF HORSERADISH PEROXIDASE C1A COMPOUND III (44-56% DOSE)

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

1H5H is a Single protein structure of sequence from Armoracia rusticana with ACT, CA, HEM and PEO as ligands. Active as Peroxidase, with EC number 1.11.1.7 Structure known Active Site: CAA. 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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