CATALASE DEGRADES DIPEROXOVANADATE AND RELEASES OXYGEN

On incubation with catalase diperoxovanadate was found to be degraded, showing a decrease in its absorbance at 356 nm and a loss of its peak with a chemical shift at -706 ppm in its V-51 NMR spectrum. The produ cts of the reaction had an absorption peak at 266 nm and chemical shif ts at -569 and -578 ppm in NMR spectra assigned to dimer and tetramer of vanadate, respectively, Catalase released half the molecular equiva lent of oxygen during this degradation of diperoxovanadate with a rate two orders of magnitude lower than that seen with H2O2. By substituti ng for and not releasing H2O2, diperoxovanadate supported scopoletin o xidation by horseradish peroxidase, as indicated by the reaction being not sensitive to catalase, unlike that seen with H2O2. Catalase-depen dent oxygen release was sensitive to azide with both H2O2 and diperoxo vanadate as substrates, whereas EDTA selectively inhibited this reacti on with diperoxovanadate. The results bring out the potential of catal ase in degrading diperoxovanadate and suggest caution in the use of th is enzyme to destroy excess H2O2 during preparation of this compound. (C) 1995 Academic Press, Inc.