The oxidation of metallic mercury in vitro by red blood cells of normal, hypocatalasemia and acatalasemia human subjects is not always in proportion to catalase activity. Methemoglobin-hydrogen peroxide compounds and glutathione peroxidase in red blood cells appeared to accelerate mercury oxidation. The oxidation of metallic mercury in vivo in the lungs and blood of normal, hypocatalasemia and acatalasemia mice exposed to metallic mercury vapor was roughly proportional to the decrease in catalase activity.
Six ferric compounds, catalase, cytochrome C, methemoglobin, lactoperoxidase, ferritin and ferric ion, had the ability to oxidize metallic mercury in the presence of hydrogen peroxide. The oxidation of metallic mercury by catalase extracts prepared from mushrooms, hay bacillus and spinach was also observed.