This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1ebe
From Proteopedia
|
LAUE DIFFRACTION STUDY ON THE STRUCTURE OF CYTOCHROME C PEROXIDASE COMPOUND I
Overview
BACKGROUND: Cytochrome c peroxidase from yeast is a soluble, haem-containing protein found in the mitochondrial electron transport, chain where it probably protects against toxic peroxides. The aim of this, study was to obtain a reliable structure for the doubly oxidized transient, intermediate (termed compound I) in the reaction of cytochrome c, peroxidase with hydrogen peroxide. This intermediate contains a semistable, free radical on Trp191, and an oxyferryl haem group. RESULTS: Compound I, was produced in crystals of yeast cytochrome c peroxidase by reacting the, crystalline enzyme with hydrogen peroxide in a flow cell. The reaction was, monitored by microspectrophotometry and Laue crystallography in separate, experiments. A nearly complete conversion to compound I was achieved, ... [(full description)]
About this Structure
1EBE is a [Single protein] structure of sequence from [Saccharomyces cerevisiae] with HEM and O as [ligands]. Active as [Cytochrome-c peroxidase], with EC number [1.11.1.5]. Structure known Active Sites: HEM and OXO. Full crystallographic information is available from [OCA].
Reference
Laue diffraction study on the structure of cytochrome c peroxidase compound I., Fulop V, Phizackerley RP, Soltis SM, Clifton IJ, Wakatsuki S, Erman J, Hajdu J, Edwards SL, Structure. 1994 Mar 15;2(3):201-8. PMID:8069633
Page seeded by OCA on Tue Oct 30 15:10:15 2007
