In vitro oxidation of metallic mercury by catalase and hydrogen peroxide generated by the glucose-glucose oxidase system, D-alanine-D-amino acid oxidase system and xanthine-xanthine oxidase-superoxide dismutase system was investigated. In vitro oxidation of metallic mercury by catalase and hydrogen peroxide generated by the reaction with glucose and glucose oxidase was observed in erythrocytes and crystalline beef liver catalase solution. The uptake depended on the concentration of glucose oxidase and nearly logarithmically increased with the increasing concentration of glucose oxidase. Similar oxidation of metallic mercury was observed in the solution of catalase, D-amino acid oxidase and D-alanine. The uptake also nearly logarithmically increased with increasing concentration of D-amino acid oxidase. In vitro oxidation of metallic mercury by catalase and hydrogen peroxide generated by the reaction system xanthine, xanthine oxidase and superoxide dismutase was observed. Oxidation of metallic mercury similar to that in the xanthine-xanthine oxidase system was observed in the solution of human plasma, hemolysate and erythrocytes containing superoxide dismutase and catalase. These results suggest that hydrogen peroxidase generated by oxidase has an important role in the uptake of metallic mercury vapor.
oxidation of mercury by catalase