Resonance Raman spectroscopic characterization of α-hydroxyheme and verdoheme complexes of heme oxygenase

Satoshi Takahashi, Kathryn Mansfield Matera, Hiroshi Fujii, Hong Zhou, Kazunobu Ishikawa, Tadashi Yoshida, Masao Ikeda-Saito, Denis L. Rousseau

Research output: Contribution to journalArticle

37 Citations (Scopus)

Abstract

Heme oxygenase (HO) is the microsomal enzyme that catalyzes the oxidative degradation of protoheme (iron protoporphyrin IX) and the generation of carbon monoxide. The enzyme converts protoheme into biliverdin through two known heme derivatives, α-hydroxyheme and verdoheme. To gain insight into the degradation mechanisms of the two intermediates, the resonance Raman spectra were observed for α-hydroxyheme and verdoheme complexes of HO and compared with those of apomyoglobin (apo-Mb) complexes. The ferrous α-hydroxyheme complexed with both HO and apo-Mb shows a resonance Raman spectral pattern similar to that of the protoheme complexes. On the contrary, the ferric α-hydroxyheme and ferrous verdoheme complexes of HO and apo-Mb show atypical Raman patterns, which are interpreted as the result of the symmetry lowering of the porphyrin-conjugated π-electron system. The comparison of the resonance Raman spectra of the verdoheme complexed with HO and apo-Mb with those of the five- and six-coordinate model complexes of verdoheme shows that the ferrous forms of the verdoheme-protein complexes are six-coordinate. The Fe-CO and Fe-CN stretching frequencies of ferrous verdoheme compounds are distinct froth those of ferrous heme compounds. It is inferred that the positive charge of the verdoheme ring possesses some of the charge density on the iron atom, causing unique characteristics of the iron ligand stretching vibrations and altered ligand binding properties.

Original languageEnglish (US)
Pages (from-to)1402-1410
Number of pages9
JournalBiochemistry
Volume36
Issue number6
DOIs
StatePublished - Feb 11 1997

Fingerprint

Heme Oxygenase (Decyclizing)
Heme
Ferrous Compounds
Carbon Monoxide
Stretching
Raman scattering
Iron
Biliverdine
Ligands
Degradation
verdoheme
Porphyrins
Enzymes
Vibration
Charge density
Electrons
Derivatives
Atoms
apomyoglobin

ASJC Scopus subject areas

  • Biochemistry

Cite this

Resonance Raman spectroscopic characterization of α-hydroxyheme and verdoheme complexes of heme oxygenase. / Takahashi, Satoshi; Matera, Kathryn Mansfield; Fujii, Hiroshi; Zhou, Hong; Ishikawa, Kazunobu; Yoshida, Tadashi; Ikeda-Saito, Masao; Rousseau, Denis L.

In: Biochemistry, Vol. 36, No. 6, 11.02.1997, p. 1402-1410.

Research output: Contribution to journalArticle

Takahashi, S, Matera, KM, Fujii, H, Zhou, H, Ishikawa, K, Yoshida, T, Ikeda-Saito, M & Rousseau, DL 1997, 'Resonance Raman spectroscopic characterization of α-hydroxyheme and verdoheme complexes of heme oxygenase', Biochemistry, vol. 36, no. 6, pp. 1402-1410. https://doi.org/10.1021/bi962361q
Takahashi S, Matera KM, Fujii H, Zhou H, Ishikawa K, Yoshida T et al. Resonance Raman spectroscopic characterization of α-hydroxyheme and verdoheme complexes of heme oxygenase. Biochemistry. 1997 Feb 11;36(6):1402-1410. https://doi.org/10.1021/bi962361q
Takahashi, Satoshi ; Matera, Kathryn Mansfield ; Fujii, Hiroshi ; Zhou, Hong ; Ishikawa, Kazunobu ; Yoshida, Tadashi ; Ikeda-Saito, Masao ; Rousseau, Denis L. / Resonance Raman spectroscopic characterization of α-hydroxyheme and verdoheme complexes of heme oxygenase. In: Biochemistry. 1997 ; Vol. 36, No. 6. pp. 1402-1410.
@article{d11ebfcbec034c4b91feaf66b0da8dc0,
title = "Resonance Raman spectroscopic characterization of α-hydroxyheme and verdoheme complexes of heme oxygenase",
abstract = "Heme oxygenase (HO) is the microsomal enzyme that catalyzes the oxidative degradation of protoheme (iron protoporphyrin IX) and the generation of carbon monoxide. The enzyme converts protoheme into biliverdin through two known heme derivatives, α-hydroxyheme and verdoheme. To gain insight into the degradation mechanisms of the two intermediates, the resonance Raman spectra were observed for α-hydroxyheme and verdoheme complexes of HO and compared with those of apomyoglobin (apo-Mb) complexes. The ferrous α-hydroxyheme complexed with both HO and apo-Mb shows a resonance Raman spectral pattern similar to that of the protoheme complexes. On the contrary, the ferric α-hydroxyheme and ferrous verdoheme complexes of HO and apo-Mb show atypical Raman patterns, which are interpreted as the result of the symmetry lowering of the porphyrin-conjugated π-electron system. The comparison of the resonance Raman spectra of the verdoheme complexed with HO and apo-Mb with those of the five- and six-coordinate model complexes of verdoheme shows that the ferrous forms of the verdoheme-protein complexes are six-coordinate. The Fe-CO and Fe-CN stretching frequencies of ferrous verdoheme compounds are distinct froth those of ferrous heme compounds. It is inferred that the positive charge of the verdoheme ring possesses some of the charge density on the iron atom, causing unique characteristics of the iron ligand stretching vibrations and altered ligand binding properties.",
author = "Satoshi Takahashi and Matera, {Kathryn Mansfield} and Hiroshi Fujii and Hong Zhou and Kazunobu Ishikawa and Tadashi Yoshida and Masao Ikeda-Saito and Rousseau, {Denis L.}",
year = "1997",
month = "2",
day = "11",
doi = "10.1021/bi962361q",
language = "English (US)",
volume = "36",
pages = "1402--1410",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "6",

}

TY - JOUR

T1 - Resonance Raman spectroscopic characterization of α-hydroxyheme and verdoheme complexes of heme oxygenase

AU - Takahashi, Satoshi

AU - Matera, Kathryn Mansfield

AU - Fujii, Hiroshi

AU - Zhou, Hong

AU - Ishikawa, Kazunobu

AU - Yoshida, Tadashi

AU - Ikeda-Saito, Masao

AU - Rousseau, Denis L.

PY - 1997/2/11

Y1 - 1997/2/11

N2 - Heme oxygenase (HO) is the microsomal enzyme that catalyzes the oxidative degradation of protoheme (iron protoporphyrin IX) and the generation of carbon monoxide. The enzyme converts protoheme into biliverdin through two known heme derivatives, α-hydroxyheme and verdoheme. To gain insight into the degradation mechanisms of the two intermediates, the resonance Raman spectra were observed for α-hydroxyheme and verdoheme complexes of HO and compared with those of apomyoglobin (apo-Mb) complexes. The ferrous α-hydroxyheme complexed with both HO and apo-Mb shows a resonance Raman spectral pattern similar to that of the protoheme complexes. On the contrary, the ferric α-hydroxyheme and ferrous verdoheme complexes of HO and apo-Mb show atypical Raman patterns, which are interpreted as the result of the symmetry lowering of the porphyrin-conjugated π-electron system. The comparison of the resonance Raman spectra of the verdoheme complexed with HO and apo-Mb with those of the five- and six-coordinate model complexes of verdoheme shows that the ferrous forms of the verdoheme-protein complexes are six-coordinate. The Fe-CO and Fe-CN stretching frequencies of ferrous verdoheme compounds are distinct froth those of ferrous heme compounds. It is inferred that the positive charge of the verdoheme ring possesses some of the charge density on the iron atom, causing unique characteristics of the iron ligand stretching vibrations and altered ligand binding properties.

AB - Heme oxygenase (HO) is the microsomal enzyme that catalyzes the oxidative degradation of protoheme (iron protoporphyrin IX) and the generation of carbon monoxide. The enzyme converts protoheme into biliverdin through two known heme derivatives, α-hydroxyheme and verdoheme. To gain insight into the degradation mechanisms of the two intermediates, the resonance Raman spectra were observed for α-hydroxyheme and verdoheme complexes of HO and compared with those of apomyoglobin (apo-Mb) complexes. The ferrous α-hydroxyheme complexed with both HO and apo-Mb shows a resonance Raman spectral pattern similar to that of the protoheme complexes. On the contrary, the ferric α-hydroxyheme and ferrous verdoheme complexes of HO and apo-Mb show atypical Raman patterns, which are interpreted as the result of the symmetry lowering of the porphyrin-conjugated π-electron system. The comparison of the resonance Raman spectra of the verdoheme complexed with HO and apo-Mb with those of the five- and six-coordinate model complexes of verdoheme shows that the ferrous forms of the verdoheme-protein complexes are six-coordinate. The Fe-CO and Fe-CN stretching frequencies of ferrous verdoheme compounds are distinct froth those of ferrous heme compounds. It is inferred that the positive charge of the verdoheme ring possesses some of the charge density on the iron atom, causing unique characteristics of the iron ligand stretching vibrations and altered ligand binding properties.

UR - http://www.scopus.com/inward/record.url?scp=0031033674&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0031033674&partnerID=8YFLogxK

U2 - 10.1021/bi962361q

DO - 10.1021/bi962361q

M3 - Article

VL - 36

SP - 1402

EP - 1410

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 6

ER -