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Electrochemical Determination of Thioredoxin Redox States

2009; American Chemical Society; Volume: 81; Issue: 4 Linguagem: Inglês

10.1021/ac802274p

1520-6882

Vlastimil Dorčák, Emil Paleček,

Electrochemical Analysis and Applications

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.