Dorčák, Vlastimil Paleček, Emil Electrochemical Determination of Thioredoxin Redox States 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. accumulation time;HNE;Thioredoxin Redox StatesThioredoxin;protein disulfide reductase;cysteine thiol groups;lipid peroxidation;peak H;submicromolar TRX concentrations;1 nM TRX;TRX redox mechanism;redox states;Electrochemical Determination;carbon electrode;electrocatalytic TRX peak H;CPSA 2009-02-15
    https://acs.figshare.com/articles/journal_contribution/Electrochemical_Determination_of_Thioredoxin_Redox_States/2878528
10.1021/ac802274p.s001