The oxidative dehydrogenation of phenol compounds, as well as polymer forma
tion from these monomers, was studied by UV-vis and Mossbauer spectroscopy
using a novel biological catalyst hematin. The mechanism of the polymerizat
ion reaction was also followed in various pH environments. Phenol radicals
were formed by a two-step electron transfer reaction catalyzed by hematin i
n the presence of peroxide, and polymer was formed from phenol radicals by
a noncatalytic reaction. This mechanism partially explains the analogous ca
talytic polymerization activity of horseradish peroxidase.