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1e93

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{{STRUCTURE_1e93| PDB=1e93 | SCENE= }}
{{STRUCTURE_1e93| PDB=1e93 | SCENE= }}
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'''HIGH RESOLUTION STRUCTURE AND BIOCHEMICAL PROPERTIES OF A RECOMBINANT CATALASE DEPLETED IN IRON'''
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===HIGH RESOLUTION STRUCTURE AND BIOCHEMICAL PROPERTIES OF A RECOMBINANT CATALASE DEPLETED IN IRON===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 8901874 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8901874}}
==About this Structure==
==About this Structure==
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[[Category: Nadp]]
[[Category: Nadp]]
[[Category: Peroxidase]]
[[Category: Peroxidase]]
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Revision as of 21:20, 30 June 2008

Image:1e93.png

Template:STRUCTURE 1e93

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

Template:ABSTRACT PUBMED 8901874

About this Structure

1E93 is a Single protein structure of sequence from Proteus mirabilis. 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

Page seeded by OCA on Tue Jul 1 00:20:44 2008

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