1h5a

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{{STRUCTURE_1h5a| PDB=1h5a | SCENE= }}
{{STRUCTURE_1h5a| PDB=1h5a | SCENE= }}
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'''STRUCTURE OF FERRIC HORSERADISH PEROXIDASE C1A IN COMPLEX WITH ACETATE'''
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===STRUCTURE OF FERRIC HORSERADISH PEROXIDASE C1A IN COMPLEX WITH ACETATE===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_12024218}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 12024218 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12024218}}
==About this Structure==
==About this Structure==
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[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Peroxidase]]
[[Category: Peroxidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:27:04 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:38:49 2008''

Revision as of 03:38, 1 July 2008

Image:1h5a.png

Template:STRUCTURE 1h5a

STRUCTURE OF FERRIC HORSERADISH PEROXIDASE C1A IN COMPLEX WITH ACETATE

Template:ABSTRACT PUBMED 12024218

About this Structure

1H5A 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

Page seeded by OCA on Tue Jul 1 06:38:49 2008

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