Peroxidase-like catalytic activity of aqueous- and immobilized-Mn 3+-octabromo-porphyrins on ion-exchange resin supplied as mimetic of horseradish peroxidase

Youji Kitamura, Katsuya Mori, Makiko Yamamoto, Akira Nozaki, Madoka Saito, Ikuko Tsukamoto, Masaki Mifune, Yutaka Saito

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

In order to explore the capability of metal porphyrins as an alternative of horseradish peroxidase (HRP), HRP-like activity of three manganese-porphyrins (Mn-Ps) and three Mn-octabromo-porphyrins (Mn-OBPs) was examined in both aqueous and immobilized states. It was found that Mn3+ octabromotetrakis (1-methyl-pyridinium-4yl)porphine (Mn-OBTMPyP) has an activity of at least 90% of HRP in an aqueous solution. Mn-OBTMPyP exhibited a catalytic activity even in the presence of hydrogen peroxide without suicide reaction. In addition, Mn-OBTMPyP was revealed to function as an alternative to HRP in the quantitative determination of serum uric acid. These results are of great interest because they indicate that metal-octabromo-porphyrins possibly include promising candidates of artificial enzyme capable of substituting for HRP.

Original languageEnglish
Pages (from-to)1364-1366
Number of pages3
JournalChemical and Pharmaceutical Bulletin
Volume56
Issue number9
DOIs
Publication statusPublished - Sep 1 2008

Keywords

  • Bromination
  • Horseradish-peroxidase
  • Manganese-porphyrin
  • Mimetic

ASJC Scopus subject areas

  • Chemistry(all)
  • Drug Discovery

Fingerprint Dive into the research topics of 'Peroxidase-like catalytic activity of aqueous- and immobilized-Mn <sup>3+</sup>-octabromo-porphyrins on ion-exchange resin supplied as mimetic of horseradish peroxidase'. Together they form a unique fingerprint.

  • Cite this