| KIZEK, René, Jan VACEK, Libuše TRNKOVÁ a František JELEN. Cyclic voltammetric study of the redox system of glutathione using the disulfide bond reductant tris(2-carboxyethyl)phosphine. Bioelectrochemistry. The Netherlands: Elsevier, 2004, roč. 2004, č. 63, s. 19-24. ISSN 1567-5394. |
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@article{555076,
author = {Kizek, René and Vacek, Jan and Trnková, Libuše and Jelen, František},
article_location = {The Netherlands},
article_number = {63},
keywords = {voltammetry; hanging mercury drop electrode (HMDE); glutathione (GSH; GSSG); redox state; sulfhydryl and disulfide groups; tris(2-carboxyethyl)phosphine (TCEP); hydrogen peroxide},
language = {eng},
issn = {1567-5394},
journal = {Bioelectrochemistry},
title = {Cyclic voltammetric study of the redox system of glutathione using the disulfide bond reductant tris(2-carboxyethyl)phosphine},
volume = {2004},
year = {2004}
}
TY - JOUR
ID - 555076
AU - Kizek, René - Vacek, Jan - Trnková, Libuše - Jelen, František
PY - 2004
TI - Cyclic voltammetric study of the redox system of glutathione using the disulfide bond reductant tris(2-carboxyethyl)phosphine
JF - Bioelectrochemistry
VL - 2004
IS - 63
SP - 19-24
EP - 19-24
PB - Elsevier
SN - 15675394
KW - voltammetry
KW - hanging mercury drop electrode (HMDE)
KW - glutathione (GSH
KW - GSSG)
KW - redox state
KW - sulfhydryl and disulfide groups
KW - tris(2-carboxyethyl)phosphine (TCEP)
KW - hydrogen peroxide
N2 - The stabilization of the reduction state of proteins and peptides is very important for the monitoring of protein-protein, protein-DNA and protein-xenobiotic interactions. The reductive state of protein or peptide is characterized by the reactive sulfhydryl group. Glutathione in the reduced (GSH) and oxidized (GSSG) forms was studied by cyclic voltammetry. Tris(2-carboxyethyl)phosphine (TCEP) as the disulfide bond reductant and/or hydrogen peroxide as the sulfhydryl group oxidant were used. Cyclic voltammetry measurements, following the redox stateus of glutathione, were performed on a hanging mercury drop electrode (HMDE) in borate buffer (pH 9.2). It was shown that in aqueous solutions TCEP was able to reduce disulfide groups smoothly and quantitatively. The TCEP response at -0.25 V vs. Ag/AgCl/3M KCl did not disturb the signals of the thiol/disulfide redox couple. The origin of cathodic and anodic signals of GSH (at -0 .44 V and -0.37 V) and GSSG (at -0.69 V and -0.40 V) glutathione forms is discussed. It was shown that the application of TCEP to the conservation of sulfhydryl groups in peptides and proteins can be useful instrument for the study of peptides and proteins redox behaviour.
ER -
KIZEK, René, Jan VACEK, Libuše TRNKOVÁ a František JELEN. Cyclic voltammetric study of the redox system of glutathione using the disulfide bond reductant tris(2-carboxyethyl)phosphine. \textit{Bioelectrochemistry}. The Netherlands: Elsevier, 2004, roč.~2004, č.~63, s.~19-24. ISSN~1567-5394.
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