Sulfur oxidation in Paracoccus pantotrophus: interaction of the sulfur-binding protein SoxYZ with the dimanganese SoxB protein

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Item Type:	Article
Title:	Sulfur oxidation in Paracoccus pantotrophus: interaction of the sulfur-binding protein SoxYZ with the dimanganese SoxB protein
Creators Name:	Quentmeier, A., Hellwig, P., Bardischewsky, F., Grelle, G., Kraft, R. and Friedrich, C.G.
Abstract:	The central protein of the sulfur-oxidizing enzyme system of Paracoccus pantotrophus, SoxYZ, formed complexes with subunits associated and covalently bound. In denaturing SDS-polyacrylamide gel electrophoresis (PAGE) SoxY migrated at 12 and SoxZ at 16kDa. SDS-PAGE of homogeneous SoxYZ without reductant separated dimeric complexes of 25, 29, and 32kDa identified by the N-terminal amino acid sequences as SoxY-Y, SoxY-Z, and SoxZ-Z, and subunit cleavage by reduction suggested their linkage via protein disulfide bonds. SoxYZ was reversibly redox active between -0.25 and 0.2V, as monitored by a combined electrochemical and FTIR spectroscopic approach. The dimanganese SoxB protein (58.611Da) converted the covalently linked heterodimer SoxY-Z to SoxYZ with associated subunits which in turn aggregated to the heterotetramer Sox(YZ)2. This reaction depended on time and the SoxB concentration, and demonstrated the interaction of these two Sox proteins.
Keywords:	FTIR Spectroscopy, Paracoccus Pantrotrophus, Protein Disulfide, Redox Properties, SoxYZ Protein
Source:	Biochemical and Biophysical Research Communications
ISSN:	0006-291X
Publisher:	Academic Press
Volume:	312
Number:	4
Page Range:	1011-1018
Date:	1 January 2003
Official Publication:	https://doi.org/10.1016/j.bbrc.2003.11.021
PubMed:	View item in PubMed

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