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In the present study we have shown that erythrocyte-catalyzed 1,8-dinitropyrene reduction occurs via formation of reactive intermediate species, which bind covalently to haemoglobin and other erythrocyte proteins. In fact after mild-acid hydrolysis of lysate proteins exposed to DNP, the reduced metabolites, 1-amino-8-nitropyrene and 1,8-diaminopyrene, were released, thus indicating the formation of sulphinamide adducts to proteins. These results suggest that haemoglobin adduct biomonitoring would be a useful method of controlling exposure to nitroarene in persons at risk.

Nitroarenes are environmental contaminants produced during incomplete combustion processes. It has been reported that nitroreduction, the most important pathway of nitroarene toxification, occurs mainly in the liver and intestine. In the present study we have shown that red cells also possess the metabolic competence to reduce nitroarenes. In particular, 1,8-dinitropyrene, the nitroarene chosen as model compound, was reduced to the corresponding mono- and diamino-derivatives, 1-amino-8-nitropyrene and 1,8-diaminopyrene, by human lysate supplemented with cofactors.