The superoxide-generating reaction of adrenaline autoxidation in an alkaline medium, used in vitro to identify the antioxidant properties of various compounds, simulates the complex multistep process of quinoid oxidation of catecholamines (CA) in the body. Sulfur-containing cysteine (Cys) and reduced glutathione (GSH), as well as oxidized glutathione (GSSG), have been shown to inhibit this process. The studied substances were considered as inhibitors of quinoid oxidation and are evaluated as antioxidants. The IC50 values for Cys and GSH were close to 7.5 mM. Inhibition by GSSG was weaker; represented approximately 50-70% of Cys and GSH. Other sulfur-containing compounds that differ in chemical structure, the amino acids taurine and methionine were ineffective. The interest in this model and the search for effective compounds acting on this reaction is associated with one of the mechanisms of the etiopathogenesis of Parkinson's disease (PD) discussed in the literature, which occurs when the biochemical transformations of dopamine CA and its quinoid oxidation process are violated. Cys, GSH and GSSG in the model system inhibit quinoid oxidation of adrenaline, as a result of which the formation of superoxide (O2 ·-) is also inhibited. Experiments with the superoxide-generating enzymatic reaction xanthine xanthioxidase, the chemistry of which is different and not related to formation of quinoid metabolites, showed that the studied substances did not inhibit O2 ·- formation in this model. Thus, it was established that the biologically active sulfur-containing compounds Cys, GSH and GSSG are specific inhibitors of quinoid oxidation of CA, and are likely to be able to play the role of a neuroprotector. It is proposed to use these compounds in the treatment and prevention of PD by activating their biosynthesis in the body.