Observation of the FeIVO stretching Raman band for a thiolate-ligated heme protein Compound I of chloroperoxidase

Tsuyoshi Egawa; Hideho Miki; Takashi Ogura; Ryu Makino; Yuzuru Ishimura; Teizo Kitagawa

doi:10.1016/0014-5793(92)80668-7

Observation of the Fe^IVO stretching Raman band for a thiolate-ligated heme protein Compound I of chloroperoxidase

Tsuyoshi Egawa, Hideho Miki, Takashi Ogura, Ryu Makino, Yuzuru Ishimura, Teizo Kitagawa

Research output: Contribution to journal › Article › peer-review

34 Scopus citations

Abstract

The Fe^IVO stretching vibration has never been identified for a cysteine-coordinated heme enzyme. In this study, resonance Raman and visible absorption spectra were observed simultaneously for transient species in the catalytic reaction of chloroperoxidase with hydrogen peroxide by using our original apparatus for mixed-flow and Raman/absorption simultaneous measurements. For the first intermediate, the Fe^IVO stretching Raman band was observed at 790 cm^-1, which shifted to 756 cm^-1 with the ¹⁸O derivative, but the ν₄ band was too weak to be identified. This suggested the formation of an oxoferryl porphyrin π cation radical. The second intermediate gave an intense ν₄ band at 1,372 cm^-1 but no oxygen isotope-sensitive Raman band, suggesting oxygen exchange with bulk water.

Original language	English (US)
Pages (from-to)	206-208
Number of pages	3
Journal	FEBS Letters
Volume	305
Issue number	3
DOIs	https://doi.org/10.1016/0014-5793(92)80668-7
State	Published - Jul 6 1992
Externally published	Yes

Keywords

Chloroperoxidase
Compound I
Compound II
Ferryl-oxo stretching mode
Resonance Raman
Thiolate-ligated heme

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

Access to Document

10.1016/0014-5793(92)80668-7

Cite this

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title = "Observation of the FeIVO stretching Raman band for a thiolate-ligated heme protein Compound I of chloroperoxidase",

abstract = "The FeIVO stretching vibration has never been identified for a cysteine-coordinated heme enzyme. In this study, resonance Raman and visible absorption spectra were observed simultaneously for transient species in the catalytic reaction of chloroperoxidase with hydrogen peroxide by using our original apparatus for mixed-flow and Raman/absorption simultaneous measurements. For the first intermediate, the FeIVO stretching Raman band was observed at 790 cm-1, which shifted to 756 cm-1 with the 18O derivative, but the ν4 band was too weak to be identified. This suggested the formation of an oxoferryl porphyrin π cation radical. The second intermediate gave an intense ν4 band at 1,372 cm-1 but no oxygen isotope-sensitive Raman band, suggesting oxygen exchange with bulk water.",

keywords = "Chloroperoxidase, Compound I, Compound II, Ferryl-oxo stretching mode, Resonance Raman, Thiolate-ligated heme",

author = "Tsuyoshi Egawa and Hideho Miki and Takashi Ogura and Ryu Makino and Yuzuru Ishimura and Teizo Kitagawa",

year = "1992",

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T1 - Observation of the FeIVO stretching Raman band for a thiolate-ligated heme protein Compound I of chloroperoxidase

AU - Egawa, Tsuyoshi

AU - Miki, Hideho

AU - Ogura, Takashi

AU - Makino, Ryu

AU - Ishimura, Yuzuru

AU - Kitagawa, Teizo

PY - 1992/7/6

Y1 - 1992/7/6

N2 - The FeIVO stretching vibration has never been identified for a cysteine-coordinated heme enzyme. In this study, resonance Raman and visible absorption spectra were observed simultaneously for transient species in the catalytic reaction of chloroperoxidase with hydrogen peroxide by using our original apparatus for mixed-flow and Raman/absorption simultaneous measurements. For the first intermediate, the FeIVO stretching Raman band was observed at 790 cm-1, which shifted to 756 cm-1 with the 18O derivative, but the ν4 band was too weak to be identified. This suggested the formation of an oxoferryl porphyrin π cation radical. The second intermediate gave an intense ν4 band at 1,372 cm-1 but no oxygen isotope-sensitive Raman band, suggesting oxygen exchange with bulk water.

AB - The FeIVO stretching vibration has never been identified for a cysteine-coordinated heme enzyme. In this study, resonance Raman and visible absorption spectra were observed simultaneously for transient species in the catalytic reaction of chloroperoxidase with hydrogen peroxide by using our original apparatus for mixed-flow and Raman/absorption simultaneous measurements. For the first intermediate, the FeIVO stretching Raman band was observed at 790 cm-1, which shifted to 756 cm-1 with the 18O derivative, but the ν4 band was too weak to be identified. This suggested the formation of an oxoferryl porphyrin π cation radical. The second intermediate gave an intense ν4 band at 1,372 cm-1 but no oxygen isotope-sensitive Raman band, suggesting oxygen exchange with bulk water.

KW - Chloroperoxidase

KW - Compound I

KW - Compound II

KW - Ferryl-oxo stretching mode

KW - Resonance Raman

KW - Thiolate-ligated heme

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