FACILE OXIDATION OF THIOPHENOL BY A FLAVIN IMMOBILIZED IN CATIONIC POLYELECTROLYTES: A FLOVOENZYME MODEL.

This paper is concerned with the flavin oxidation of thiols to disulfides which has been of special in3erest in connection with the action of flavoenzymes. The mechanisms by which the flavoenzymes catalyze oxidoreduction reactions have been studied in nonenzymatic systems. In the conventional nonenzymatic systems, however, the reactivity of flavin is incomparably suppressed relative to that observed in enzymatic systems. In this short communication results of a study are presented which show that a flavin immobilized in cationic polyelectrolytes readily oxidizes thiopehnol to diphenyl disulfide at ambient conditions. It is concluded that the facilitation of flavin-mediated oxidation of thiophenol is achieved by an environmental effect. Preliminary experiments similarly indicate that glutathione and 1,4-butanedithiol are readily oxidized by flavin immobilized in cationic polyelectrolytes.