Peroxidase-like catalytic activity of Mn3+-octabromo-tetrakis(4-sulfophenyl)porphine on linoleate hydroperoxide and its analytical application

Masaki Mifune, Hidenori Kamiguchi, Taka aki Tai, Seigo Kuremoto, Makiko Yamamoto, Ikuko Tsukamoto, Madoka Saito, Youji Kitamura, Yutaka Saito

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)


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, Mn3+-OBPS allowed to produce the largest amount of dye. The optimal conditions of the coloring reaction catalyzed by Mn3+-OBPS for the determination of LOOH were determined. A good linear calibration curve was obtained in the concentration range of 0.025-0.4 μmole LOOH with good reproducibility (coefficient of variance = 1.23%), suggesting that Mn3+-OBPS is a good artificial mimesis of the peroxidase for LOOH. In addition, Mn3+-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 Mn3+-OBTP is attributable to the redox cycle of Mn3+ ↔ Mn4+.

Original languageEnglish
Pages (from-to)456-461
Number of pages6
Issue number1
Publication statusPublished - Jan 15 2007


  • Determination
  • Linoleate hydroperoxide
  • Metal-porphyrin
  • Peroxidase

ASJC Scopus subject areas

  • Analytical Chemistry


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