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Biotechnology Letters, Vol.24, No.19, 1535-1538, 2002
Oxidation of dibenzothiophene catalyzed by immobilized hemoproteins in water-immiscible organic solvents
In various water-immiscible organic solvents, hemoglobin, myoglobin and cytochrome c deposited on Celite catalyzed the oxidation of dibenzothiophene when peroxides having nonpolar substituents, such as t-butyl hydroperoxide and cumene hydroperoxide (alpha, alpha-dimethylbenzyl hydroperoxide), were used as oxidants. In hexadecane, oxidation of dibenzothiophene by immobilized cytochrome c, with a K-m value of 0.15 mM for dibenzothiophene, was inhibited by cumene hydroperoxide above 0.5 mM.