THE USE OF NONAQUEOUS MEDIA TO PROBE BIOCHEMICALLY SIGNIFICANT ENZYME INTERMEDIATES - THE GENERATION AND STABILIZATION OF HORSERADISH-PEROXIDASE COMPOUND-II IN NEAT BENZENE SOLUTION AT ROOM-TEMPERATURE

UV-visible spectral evidence is presented demonstrating that the mechanistically significant horseradish peroxidase compound II intermediate can be generated and stabilized for spectroscopic study in virtually anhydrous (<1% H2O) neat benzene solution at room temperature. In organic media, the intermediate exhibits remarkable photostability and thermostability in contrast to its well-known photolability and thermal lability in aqueous solution.