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Updated: Jun 26, 2026

EPR Monitored Redox Titration of the Cofactors of Saccharomyces cerevisiae Nar1
Published on: November 26, 2014
Electrochemical determination of thioredoxin redox states
Vlastimil Dorcák1, Emil Palecek
1Institute of Biophysics, Academy of Sciences of the Czech Republic, CZ-612 65 Brno, Czech Republic.
Abstract:
Thioredoxin (TRX) is a general protein disulfide reductase with a large number of biological functions, including its roles in human diseases. The TRX redox mechanism is based on reversible oxidation of two cysteine thiol groups to a disulfide, accompanied by the transfer of two protons. Using constant-current chronopotentiometric stripping analysis (CPSA) and the electrocatalytic TRX peak H, we have determined redox states of TRX at submicromolar TRX concentrations. A concentration of 1 nM TRX produces a well-developed peak H at moderate accumulation time without stirring. On the basis of this peak, interactions of 4-hydroxy-2-nonenal (HNE, product of lipid peroxidation) with TRX and the formation of TRX-HNE adducts were studied. CPSA of TRX at a carbon electrode is less sensitive and does not discriminate between reduced and oxidized forms of TRX.
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