Enzyme-catalyzed polymerization of 8-hydroxyquinoline-5-sulfonate by in situ nuclear magnetic resonance spectroscopy

In this report, we describe the use of in situ NMR spectroscopy to elucidate the mechanism of horseradish peroxidase-catalyzed oxidative free-radical coupling of phenols. We demonstrate the potential of the technique for the polymerization of 8-hydroxyquinoline-5-sulfonate (HQS). Based on the structural changes, we establish the involvement of ortho- and para-position protons (to the hydroxyl group) in the oxidative free-radical coupling polymerization with their relative preferences. For example, in HQS, we establish that the positions 2, 4, and 7 are involved in the chemical bonding with the order of preference being 7 ≥ 2 > 4. Analyses of ¹³C-NMR data suggest the formation of C—C- and C—O—C-type coupling bonds during enzymatic polymerization. © 1998 John Wiley & Sons, Inc. J. Appl. Polym. Sci. 70: 1257–1264, 1998