Glutathione (GSH) protects proteins from oxidative damage by forming reversible mixed disulfides with cysteine residues, a phenomenon knows as protein glutathionylation. Glutaredoxins are involved in this process: they regulate protein redox state through deglutathionylate GSH-protein mixed dissulfides. Acute cadmium exposure of mammal cells leads to inhibition of the cytosolic glutaredoxin (Grx1).  Cadmium is a mutagen that acts by inhibiting mismatch repair, while its toxic effect seems to be related to an indirect oxidative stress. Saccharomyces cerevisiae, a model organism to study the mechanisms of metal homeostasis and tolerance, possess two cytosolic glutaredoxins, Grx1 and Grx2. In this work, we show that yeast cells deficient in GRX2, growing in 80 mM of cadmium, demonstrated high mitochondrial mutagenic rate, determined by frequency of mutants that had lost mitochondrial function (petite mutants), high tolerance and lower apoptosis induction. The mutant strain also showed decreased levels of GSH-protein after cadmium exposure, which might difficult the signaling to apoptosis, leading to mutagenic increased rates. Taken together, these results suggest that the mutagenic action of Cd⁺² seems to involve glutaredoxin, which seems to affect the process of apoptosis.