Meso-unsubstituted iron corrole in hemoproteins: Remarkable differences in effects on peroxidase activities between myoglobin and horseradish peroxidase

Takashi Matsuo, Akihiro Hayashi, Masato Abe, Takaaki Matsuda, Yoshio Hisaeda, Takashi Hayashi

Research output: Contribution to journalArticle

45 Citations (Scopus)

Abstract

(Figure Presented) Myoglobin (Mb) and horseradish peroxidase (HRP) were both reconstituted with a meso-unsubstituted iron corrole and their electronic configurations and peroxidase activities were investigated. The appearance of the 540 nm band upon incorporation of the iron corrole into apoMb indicates axial coordination by the proximal histidine imidazole in the Mb heme pocket. Based on 1H NMR measurements using the Evans method, the total magnetic susceptibility of the iron corrole reconstituted Mb was evaluated to be S = 3/2. In contrast, although a band does not appear in the vicinity of 540 nm during reconstitution of the iron corrole into the matrix of HRP, a spectrum similar to that of the iron corrole reconstituted Mb is observed upon the addition of dithionite. This observation suggests that the oxidation state of the corrole iron in the reconstituted HRP can be assigned as +4. The catalytic activities of both proteins toward guaiacol oxidation are quite different; the iron corrole reconstituted HRP decelerates H2O2-dependent oxidation of guaiacol, while the same reaction catalyzed by iron corrole reconstituted Mb has the opposite effect and accelerates the reaction. This finding can be attributed to the difference in the oxidation states of the corrole iron when these proteins are in the resting state.

Original languageEnglish
Pages (from-to)15124-15125
Number of pages2
JournalJournal of the American Chemical Society
Volume131
Issue number42
DOIs
Publication statusPublished - Oct 28 2009

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Myoglobin
Horseradish Peroxidase
Peroxidase
Iron
Guaiacol
Oxidation
Dithionite
Proteins
iron corrole
Magnetic susceptibility
Heme
Histidine
Catalyst activity
Nuclear magnetic resonance

All Science Journal Classification (ASJC) codes

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

Cite this

Meso-unsubstituted iron corrole in hemoproteins : Remarkable differences in effects on peroxidase activities between myoglobin and horseradish peroxidase. / Matsuo, Takashi; Hayashi, Akihiro; Abe, Masato; Matsuda, Takaaki; Hisaeda, Yoshio; Hayashi, Takashi.

In: Journal of the American Chemical Society, Vol. 131, No. 42, 28.10.2009, p. 15124-15125.

Research output: Contribution to journalArticle

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AB - (Figure Presented) Myoglobin (Mb) and horseradish peroxidase (HRP) were both reconstituted with a meso-unsubstituted iron corrole and their electronic configurations and peroxidase activities were investigated. The appearance of the 540 nm band upon incorporation of the iron corrole into apoMb indicates axial coordination by the proximal histidine imidazole in the Mb heme pocket. Based on 1H NMR measurements using the Evans method, the total magnetic susceptibility of the iron corrole reconstituted Mb was evaluated to be S = 3/2. In contrast, although a band does not appear in the vicinity of 540 nm during reconstitution of the iron corrole into the matrix of HRP, a spectrum similar to that of the iron corrole reconstituted Mb is observed upon the addition of dithionite. This observation suggests that the oxidation state of the corrole iron in the reconstituted HRP can be assigned as +4. The catalytic activities of both proteins toward guaiacol oxidation are quite different; the iron corrole reconstituted HRP decelerates H2O2-dependent oxidation of guaiacol, while the same reaction catalyzed by iron corrole reconstituted Mb has the opposite effect and accelerates the reaction. This finding can be attributed to the difference in the oxidation states of the corrole iron when these proteins are in the resting state.

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