Abstract
The interaction of hemin with reduced glutathione (GSH) was studied using cyclic and linear sweep voltammetry with stationary and rotating disc electrodes and UV-VIS spectroelectrochemical experiments. A 1:1 global stoichiometry and similar values for the hemin - GSH binding constant were obtained in aqueous media in the presence of sodium dodecyl sulfate (SDS) with those in dimethylsulphoxide (DMSO). A comparison between the family of curves obtained during the electrochemical reduction of hemin with that recorded at the hemin - GSH interaction points to different absorption bands, leading to the idea of a complexation of the FeIII by GSH, rather than a Fe III → Fe II reduction. The biochemical relevance of the hemin-glutathione interaction is related to the presence of GSH in normal erythrocytes in high concentrations (1 - 4 mM), being involved as an agent in the trapping of free hemin from the cell cytosol.
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