2j5m

From Proteopedia

Revision as of 17:39, 18 December 2007 by OCA (Talk | contribs)
Jump to: navigation, search

2j5m, resolution 1.75Å

Drag the structure with the mouse to rotate

STRUCTURE OF CHLOROPEROXIDASE COMPOUND 0

Overview

We have determined the crystal structure of the chloroperoxidase (CPO), hydroperoxo reaction intermediate (CPO compound 0) at 1.75-A resolution., The intermediate was generated through controlled photoreduction of the, CPO oxygen complex during x-ray data collection, which was monitored by, recording of the crystal absorption spectra. Initially, the peroxo-anion, species was formed and then protonated to yield compound 0. Quantum, chemical calculations indicate that the peroxo-anion species is not stable, and collapses instantaneously to compound 0. Compound 0 is present in the, ferric low-spin doublet ground state and is characterized by a long O O, bond length of 1.5 A and a Fe O bond distance of 1.8 A, which is also, observed in the crystal structure.

About this Structure

2J5M is a Single protein structure of sequence from Leptoxyphium fumago with NAG, MAN, MN, ACT, HEM, PEO and EDO as ligands. Active as Chloride peroxidase, with EC number 1.11.1.10 Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Structure and quantum chemical characterization of chloroperoxidase compound 0, a common reaction intermediate of diverse heme enzymes., Kuhnel K, Derat E, Terner J, Shaik S, Schlichting I, Proc Natl Acad Sci U S A. 2007 Jan 2;104(1):99-104. Epub 2006 Dec 26. PMID:17190816

Page seeded by OCA on Tue Dec 18 19:49:46 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools