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Interrogating the molecular details of the peroxiredoxin activity of the Escherichia coli bacterioferritin comigratory protein using high-resolution mass spectrometry

Authors :
Clarke, David J.
Mackay, C. Logan
Campopiano, Dominic J.
Langridge-Smith, Pat
Brown, Alan R.
Source :
Biochemistry. May 12, 2009, Vol. 48 Issue 18, 3904-3914
Publication Year :
2009

Abstract

Combination of high-resolution Fourier transform ion cyclotron resonance mass spectrometry and top-down fragmentation techniques were used to analyze the mechanistic details of hydrogen peroxide reduction by Escherichia coli bacterioferritin comigratory protein (BCP). The mutant BCP enzyme adopted a different and novel mechanistic pathway and reacted with peroxide to form a sulfenic acid on Cys-45 and is also a substrate for reduction by thioredoxin.

Details

Language :
English
ISSN :
00062960
Volume :
48
Issue :
18
Database :
Gale General OneFile
Journal :
Biochemistry
Publication Type :
Academic Journal
Accession number :
edsgcl.201456883