Porphyrinoid chemistry in hemoprotein matrix: Detection and reactivities of iron(IV)-oxo species of porphycene incorporated into horseradish peroxidase

Takashi Matsuo, Dai Murata, Yoshio Hisaeda, Hiroshi Hori, Takashi Hayashi

Research output: Contribution to journalArticlepeer-review

46 Citations (Scopus)

Abstract

The iron porphycene with two propionates at the peripheral positions of the framework was incorporated into the heme pocket of horseradish peroxidase. In the presence of hydrogen peroxide, the ferric iron porphycene was smoothly converted into the iron(IV)-oxo porphycene π-cation radical species, which was confirmed by the appearance of a band around 800 nm in the UV-vis spectrum. The protein with the iron porphycene showed a 10-fold higher reactivity for the thioanisole oxidation when compared to the native protein. In contrast, the guaiacol oxidation proceeded with similar reaction rates in both proteins. The kinetic analyses indicated that the ferric porphycene in the protein more slowly reacts with hydrogen peroxide than the native heme, whereas the high oxidation states show higher reactivities during oxidations of an organic substrate. The formation of the iron(IV)-oxo species of porphycene and its reactivities in the hemoprotein matrix are demonstrated.

Original languageEnglish
Pages (from-to)12906-12907
Number of pages2
JournalJournal of the American Chemical Society
Volume129
Issue number43
DOIs
Publication statusPublished - Oct 31 2007

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

Fingerprint Dive into the research topics of 'Porphyrinoid chemistry in hemoprotein matrix: Detection and reactivities of iron(IV)-oxo species of porphycene incorporated into horseradish peroxidase'. Together they form a unique fingerprint.

Cite this