2j18

From Proteopedia

Revision as of 16:17, 5 November 2007

CHLOROPEROXIDASE MIXTURE OF FERRIC AND FERROUS STATES (LOW DOSE DATA SET)

Overview

The X-ray crystallographic analysis of redox-active systems may be, complicated by photoreduction. Although radiolytic reduction by the, probing X-ray beam may be exploited to generate otherwise short-lived, reaction intermediates of metalloproteins, it is generally an undesired, feature. Here, the X-ray-induced reduction of the three heme proteins, myoglobin, cytochrome P450cam and chloroperoxidase has been followed by, on-line UV-Vis absorption spectroscopy. All three systems showed a very, rapid reduction of the heme iron. In chloroperoxidase the change of the, ionization state from ferric to ferrous heme is associated with a movement, of the heme-coordinating water molecule. The influence of the energy of, the incident X-ray photons and of the presence of scavengers on the, apparent reduction rate of ferric myoglobin crystals was analyzed.

About this Structure

2J18 is a Single protein structure of sequence from Leptoxyphium fumago with NAG, MAN, MN, BR and HEM as ligands. Active as Chloride peroxidase, with EC number 1.11.1.10 Structure known Active Site: AC1. Full crystallographic information is available from OCA.

Reference

Cryoradiolytic reduction of crystalline heme proteins: analysis by UV-Vis spectroscopy and X-ray crystallography., Beitlich T, Kuhnel K, Schulze-Briese C, Shoeman RL, Schlichting I, J Synchrotron Radiat. 2007 Jan;14(Pt 1):11-23. Epub 2006 Dec 15. PMID:17211068

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