Some Oxygen-18 Studies on the Mechanism of Myo-inositol Oxygenase

摘要

Myo-inositol oxygenase is known to catalyze the cleavage of myo-inositol to D-glucuronic acid in the presence of O2. Several mechanisms for this cleavage have been proposed. The present research was concerned with determining the number and location of oxygen atoms incorporated from O2, thereby limiting the number of possible mechanisms. This was accomplished by a series of oxygen-18 labeling studies with analysis of trimethyl-silylated compounds by GC/MS techniques.