Cyclic voltammetric study of the redox system of glutathione using the disulfide bond reductant tris(2-carboxyethyl)phosphine

KIZEK, René, Jan VACEK, Libuše TRNKOVÁ and 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, vol. 2004, No 63, p. 19-24. ISSN 1567-5394.

Basic information

• Original name: Cyclic voltammetric study of the redox system of glutathione using the disulfide bond reductant tris(2-carboxyethyl)phosphine
• Name in Czech: Cyklicko-voltametrická studie redox systému glutathione pomocí tris(2-carboxyethyl)phosphinu jako redukčního činidla disulfidických vazeb
• Authors: KIZEK, René (203 Czech Republic), Jan VACEK (203 Czech Republic), Libuše TRNKOVÁ (203 Czech Republic, guarantor) and František JELEN (203 Czech Republic).
• Edition: Bioelectrochemistry, The Netherlands, Elsevier, 2004, 1567-5394.

Other information

• Original language: English
• Type of outcome: Article in a journal
• Field of Study: 10405 Electrochemistry
• Country of publisher: Netherlands
• Confidentiality degree: is not subject to a state or trade secret
• Impact factor: Impact factor: 2.261
• RIV identification code: RIV/00216224:14310/04:00011179
• Organization unit: Faculty of Science
• UT WoS: 000221786900005
• Keywords in English: voltammetry; hanging mercury drop electrode (HMDE); glutathione (GSH; GSSG); redox state; sulfhydryl and disulfide groups; tris(2-carboxyethyl)phosphine (TCEP); hydrogen peroxide
• Tags: glutathione (GSH, GSSG), hydrogen peroxide, redox state, sulfhydryl and disulfide groups, tris(2-carboxyethyl)phosphine (TCEP), Voltammetry

Abstract

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.

Abstract (in Czech)

Cyklicko-voltametrická studie redox systému glutathione pomocí tris(2-carboxyethyl)phosphinu jako redukčního činidla disulfidických vazeb

Links

• GA203/02/0422, research and development project: Name: Nové směry v elektrochemii nukleových kyselin a jejich aplikace v chemii životního prostředí

Investor: Czech Science Foundation, New trends in electrochemistry of nucleic acids and their applications in enviromental chemistry

• IAA1163201, research and development project: Name: Využití adsorptivní přenosové a eliminační techniky pro elektrochemickou analýzu oligonukleotidů a nukleových kyselin

Investor: Academy of Sciences of the Czech Republic, Application of adsorptive transfer and elemination techniques in oligonucleotides and nucleic acids analysis.