The kinetics of o-dianisidine oxidation by hydrogen peroxide catalyzed
by meso-tetrakis-phenylferrichloroporphyrin (TPP-1)(4), aminoethyl)am
inoethoxy]phenyl}ferrichloroporphyrin (TPP-2), l-meso[4(2-bromoethoxy)
phenyl]ferrichloroporphyrin (TPP-3), rakis-[4(2-bromoethoxy)phenyl]fer
richloroporphyrin (TPP-4), and their complexes with additional ligands
(aniline, imidazole, and pyridine) were studied in reversed micelles
of Aerosol OT (AOT) in octane. The TPP complexes incorporated in rever
sed micelles of AOT in octane mimicked characteristic features of the
active site of horseradish peroxidase, i.e., the high-spin state of he
me iron and its ability to bind hydrogen peroxide and generate the act
ive forms of hydrogen peroxide, thus initiating o-dianisidine oxidatio
n by a mechanism involving free radicals. The imidazole and pyridine c
omplexes of TPP-4 exhibited the maximum catalytic activity. Means for
regulating the activity of the peroxidase models in reversed micelles
of surfactants, such as selection and modification of surfactant, atta
chment of porphyrins to micelles by ''anchor'' groups, and an addition
al ligation of Fe ion, are discussed.