1e93 | pdb_00001e93
HIGH RESOLUTION STRUCTURE AND BIOCHEMICAL PROPERTIES OF A RECOMBINANT CATALASE DEPLETED IN IRON
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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 Known structural/functional 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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