1e93

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[[Category: peroxidase]]
[[Category: peroxidase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:50:23 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:08:32 2007''

Revision as of 13:03, 30 October 2007

Image:1e93.gif

1e93, resolution 2.00Å

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HIGH RESOLUTION STRUCTURE AND BIOCHEMICAL PROPERTIES OF A RECOMBINANT CATALASE DEPLETED IN IRON

Overview

Various enzymes use semi-stable ferryl intermediates and free radicals, during their catalytic cycle, amongst them haem catalases. Structures for, two transient intermediates (compounds I and II) of the NADPH-dependent, catalase from Proteus mirabilis (PMC) have been determined by, time-resolved X-ray crystallography and single crystal, microspectrophotometry. The results show the formation and transformation, of the ferryl group in the haem, and the unexpected binding of an anion, during this reaction at a site distant from the haem.

About this Structure

1E93 is a [Single protein] structure of sequence from [Proteus mirabilis] with ACT, SO4 and HEM as [ligands]. Active as [Catalase], with EC number [1.11.1.6]. Structure known Active Site: HEM. Full crystallographic information is available from [OCA].

Reference

Ferryl intermediates of catalase captured by time-resolved Weissenberg crystallography and UV-VIS spectroscopy., Gouet P, Jouve HM, Williams PA, Andersson I, Andreoletti P, Nussaume L, Hajdu J, Nat Struct Biol. 1996 Nov;3(11):951-6. PMID:8901874

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