1ebe
From Proteopedia
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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 [[1]] with HEM and O as [ligands]. Active as [[2]], with EC number [1.11.1.5]. 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
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