1h5d: Difference between revisions
No edit summary |
No edit summary |
||
| Line 31: | Line 31: | ||
[[Category: x-ray induced reduction]] | [[Category: x-ray induced reduction]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:29:19 2007'' | ||
Revision as of 16:24, 30 October 2007
|
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] with ACT, CA and HEM as [ligands]. Active as [Peroxidase], with EC number [1.11.1.7]. Structure known Active Site: HEM. 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
Page seeded by OCA on Tue Oct 30 15:29:19 2007