Peroxidase-like catalytic activity of Mn(3+)-octabromo-tetrakis(4-sulfophenyl)porphine on linoleate hydroperoxide and its analytical application.
To reveal an enzyme-like catalytic activity of metal-octabromo-tetrakis(sulfophenyl)porphines (M-OBPSs), their peroxidease-like catalytic activity on linoleate hydroperoxide (LOOH) were evaluated on the basis of dye-formation in the coloring reaction between N,N-diethylaniline and 4-aminoantipyrine that yields a quinoid-type dye. Among M-OBPSs tested, Mn(3+)-OBPS allowed to produce the largest amount of dye. The optimal conditions of the coloring reaction catalyzed by Mn(3+)-OBPS for the determination of LOOH were determined. A good linear calibration curve was obtained in the concentration range of 0.025-0.4mumole LOOH with good reproducibility (coefficient of variance=1.23%), suggesting that Mn(3+)-OBPS is a good artificial mimesis of the peroxidase for LOOH. In addition, Mn(3+)-OBPS was highly specific for LOOH even in the presence of cumene hydroxyperoxide or hydrogen peroxide. It was revealed that the peroxidase-like activity of Mn(3+)-OBTP is attributable to the redox cycle of Mn(3+)<-->Mn(4+).
Mifune
Masaki
M
Department of Pharmaceutical Sciences, Graduate School of Medicine and Dentistry and Pharmaceutical Sciences, Okayama University, Tsushima-Naka, Okayama 700-8530, Japan.
Kamiguchi
Hidenori
H
Tai
Taka-Aki
TA
Kuremoto
Seigo
S
Yamamoto
Makiko
M
Tsukamoto
Ikuko
I
Saito
Madoka
M
Kitamura
Youji
Y
Saito
Yutaka
Y