Fluorescence spectra of Trp53Phe and Trp110Ile mutants of a heme-regulated phosphodiesterase from Escherichia coli

Satoshi Hirata; Hirofumi Kurokawa; Ikuko Sagami; Toru Shimizu

doi:10.1246/cl.2004.870

Fluorescence spectra of Trp53Phe and Trp110Ile mutants of a heme-regulated phosphodiesterase from Escherichia coli

Satoshi Hirata, Hirofumi Kurokawa, Ikuko Sagami, Toru Shimizu

多元物質科学研究所・有機・生命科学研究部門

研究成果: Article › 査読

3 被引用数 (Scopus)

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Fluorescence bands of a Trp110Ile mutant of the isolated heme domain of a heme-regulated phosphodiesterase (Ec DOS) from Escherichia coli and its complex with 8-anilino-1-naphthalenesulfonic acid (ANS) were very weak, compared to the wild-type protein, suggesting that the fluorescence of the remaining Trp53 residue is quenched by interactions with heme, and that the Trp110 residue is exposed to the solvent.

本文言語	English
ページ（範囲）	870-871
ページ数	2
ジャーナル	Chemistry Letters
巻	33
号	7
DOI	https://doi.org/10.1246/cl.2004.870
出版ステータス	Published - 2004 7 5

ASJC Scopus subject areas

化学 (全般)

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10.1246/cl.2004.870

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title = "Fluorescence spectra of Trp53Phe and Trp110Ile mutants of a heme-regulated phosphodiesterase from Escherichia coli",

abstract = "Fluorescence bands of a Trp110Ile mutant of the isolated heme domain of a heme-regulated phosphodiesterase (Ec DOS) from Escherichia coli and its complex with 8-anilino-1-naphthalenesulfonic acid (ANS) were very weak, compared to the wild-type protein, suggesting that the fluorescence of the remaining Trp53 residue is quenched by interactions with heme, and that the Trp110 residue is exposed to the solvent.",

author = "Satoshi Hirata and Hirofumi Kurokawa and Ikuko Sagami and Toru Shimizu",

year = "2004",

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doi = "10.1246/cl.2004.870",

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journal = "Chemistry Letters",

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T1 - Fluorescence spectra of Trp53Phe and Trp110Ile mutants of a heme-regulated phosphodiesterase from Escherichia coli

AU - Hirata, Satoshi

AU - Kurokawa, Hirofumi

AU - Sagami, Ikuko

AU - Shimizu, Toru

PY - 2004/7/5

Y1 - 2004/7/5

N2 - Fluorescence bands of a Trp110Ile mutant of the isolated heme domain of a heme-regulated phosphodiesterase (Ec DOS) from Escherichia coli and its complex with 8-anilino-1-naphthalenesulfonic acid (ANS) were very weak, compared to the wild-type protein, suggesting that the fluorescence of the remaining Trp53 residue is quenched by interactions with heme, and that the Trp110 residue is exposed to the solvent.

AB - Fluorescence bands of a Trp110Ile mutant of the isolated heme domain of a heme-regulated phosphodiesterase (Ec DOS) from Escherichia coli and its complex with 8-anilino-1-naphthalenesulfonic acid (ANS) were very weak, compared to the wild-type protein, suggesting that the fluorescence of the remaining Trp53 residue is quenched by interactions with heme, and that the Trp110 residue is exposed to the solvent.

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JO - Chemistry Letters

JF - Chemistry Letters

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Fluorescence spectra of Trp53Phe and Trp110Ile mutants of a heme-regulated phosphodiesterase from Escherichia coli

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