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Glutaredoxins (GRXs) are widespread proteins catalyzing deglutathionylation or glutathionylation reactions or serving for iron-sulfur (Fe-S) protein maturation. Previous studies highlighted a role of the <i>Arabidopsis thaliana</i> mitochondrial class II GRXS15 in Fe-S cluster assembly, whereas only a weak glutathione-dependent oxidation activity was detected with the non-physiological roGFP2 substrate in vitro. Still, the protein must exist in a reduced form for both redox and Fe-S cluster binding functions. Therefore, this study aimed at examining the redox properties of <i>At</i>GRXS15. The acidic pKa of the sole cysteine present in <i>At</i>GRXS15 indicates that it should be almost totally under a thiolate form at mitochondrial pH and thus possibly subject to oxidation. Oxidizing treatments revealed that this cysteine reacts with H₂O₂ or with oxidized glutathione forms. This leads to the formation of disulfide-bridge dimers and glutathionylated monomers which have redox midpoint potentials of −304 mV and −280 mV, respectively. Both oxidized forms are reduced by glutathione and mitochondrial thioredoxins. In conclusion, it appears that <i>At</i>GRXS15 is prone to oxidation, forming reversible oxidation forms that may be seen either as a catalytic intermediate of the oxidoreductase activity and/or as a protective mechanism preventing irreversible oxidation and allowing Fe-S cluster binding upon reduction.