Oxidative activation of 2-aminofluorene by human red blood cell cytosol.

ABSTRACT

Purified red blood cell cytosol is able to activate 2-aminofluorene (2AF) to N-hydroxy-2-aminofluorene. Apparent kinetic parameters are determined with and without methylene blue. The latter, which maintains haemoglobin in the reduced form and stimulates NADPH production, increases the affinity of the enzyme for the 2AF. This activity is inhibited by carbon monoxide while cyanide is without effect. The involvement of a peroxidative reaction or a one-electron oxidative mechanism involving free radicals may be excluded.