Abstract
Thioredoxin is a major oxido-reductase which intervenes in the redox-controlled cellular signalization pathways. Its active site is a thiol-disulfide function. The study of the one-electron reduction of the oxidized protein by gamma radiolysis shows that its behaviour is markedly different from that of other protein disulfides, like those of lysozyme. In order to understand this difference, we have prepared by site-directed mutagenesis two mutant forms ofthioredoxin. We observe that the redox properties of the protein are modulated by the amino acids Asp30 and Trp35.
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