Coenzyme models. 32. Catalytic activity of polymer-bound thiazolium ions as estimated by flavin trapping technique

Three thiazolium-containing polymers, Th-7, Th-33, and Th-18-Py [where Th-x and Py mean x mol % thiazolium unit and pyridinium unit (54 mol %), respectively], were synthesized from partially p-chloromethylated polystyrene. The catalytic activities of these polymer catalysts in acyloin condensation of aldehydes and decarboxylation of α-keto acids were estimated kinetically by oxidative trapping of the key intermediate by flavin (flavin-trapping technique). In aqueous solution at 30°C, the catalytic activity of Th-18-Py and Th-33 in condensation of p-chlorobenzaldehyde was comparable with that of the cationic-micelle-bound thiazolium ion, whereas Th-7 and a monomeric thiazolium compound (N-benzylthiazolium bromide) scarcely exhibited any catalytic activity. The catalysis of the polymer-bound thiazolium ions was sensitively suppressed by increased ionic strength. These results suggest that the pendent thiazolium ion is activated by the relatively high charge density along the polymer chain: the cationic environment is able to facilitate dissociation of the thiazolium ion to the ylid form and deprotonation of the thiazolium-aldehyde adduct to the key intermediate.