1e93

From Proteopedia

Revision as of 13:03, 30 October 2007 by OCA (Talk | contribs)
Jump to: navigation, search
Image:1e93.gif

1e93, resolution 2.00Å

Drag the structure with the mouse to rotate

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

Page seeded by OCA on Tue Oct 30 15:08:32 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1e93"
Personal tools