An examination of the oxidation of mercury vapor by rat brain homogenate

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Abstract
The oxidation of mercury vapor (Hg°) to divalent inorganic mercury (Hg2+) was studied in rat brain homogenates. By using a “degassing” method, it was possible to speciate the mercury present in the homogenate and, for the first time, to measure the rate of oxidation as a function of the substrate (Hg°) concentration. Mercury oxidation was first-order with respect to substrate concentration at all concentrations tested, and the first-order rate constant for the oxidation process was proportional to homogenate concentration. The role of catalase compound I in mercury vapor oxidation by brain homogenate was examined by observing the effects of two inhibitors of catalase (catalase compound I) on homogenate mercury-oxidizing activity and catalase activity. Sodium azide (50 mM) completely inhibited both mercury-oxidizing activity and catalase activity. Aminotriazole (3-amino-1H-1,2,4-triazole) (50 mM) completely inhibited only mercury-oxidizing activity; some residual catalase activity was found in the aminotriazole-treated homogenate. It was concluded that catalase compound I plays a major role in the oxidation of Hg°, but the possibility that catalase-independent pathways make a minor contribution cannot be excluded.