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 journalArticle

43 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

Fingerprint

Horseradish Peroxidase
Iron
Proteins
Oxidation
Hydrogen peroxide
Heme
Hydrogen Peroxide
Guaiacol
Propionates
Reaction rates
Positive ions
porphycene
ferryl iron
Cations
Kinetics
Substrates

All Science Journal Classification (ASJC) codes

  • Chemistry(all)

Cite this

Porphyrinoid chemistry in hemoprotein matrix : Detection and reactivities of iron(IV)-oxo species of porphycene incorporated into horseradish peroxidase. / Matsuo, Takashi; Murata, Dai; Hisaeda, Yoshio; Hori, Hiroshi; Hayashi, Takashi.

In: Journal of the American Chemical Society, Vol. 129, No. 43, 31.10.2007, p. 12906-12907.

Research output: Contribution to journalArticle

@article{42a2d868d0bc487daba6c2863a7749c1,
title = "Porphyrinoid chemistry in hemoprotein matrix: Detection and reactivities of iron(IV)-oxo species of porphycene incorporated into horseradish peroxidase",
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.",
author = "Takashi Matsuo and Dai Murata and Yoshio Hisaeda and Hiroshi Hori and Takashi Hayashi",
year = "2007",
month = "10",
day = "31",
doi = "10.1021/ja074685f",
language = "English",
volume = "129",
pages = "12906--12907",
journal = "Journal of the American Chemical Society",
issn = "0002-7863",
publisher = "American Chemical Society",
number = "43",

}

TY - JOUR

T1 - Porphyrinoid chemistry in hemoprotein matrix

T2 - Detection and reactivities of iron(IV)-oxo species of porphycene incorporated into horseradish peroxidase

AU - Matsuo, Takashi

AU - Murata, Dai

AU - Hisaeda, Yoshio

AU - Hori, Hiroshi

AU - Hayashi, Takashi

PY - 2007/10/31

Y1 - 2007/10/31

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=35848930137&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=35848930137&partnerID=8YFLogxK

U2 - 10.1021/ja074685f

DO - 10.1021/ja074685f

M3 - Article

VL - 129

SP - 12906

EP - 12907

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 0002-7863

IS - 43

ER -