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

Division of Organic- and Biomaterials Research

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

3 Citations (Scopus)

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.

Original language	English
Pages (from-to)	870-871
Number of pages	2
Journal	Chemistry Letters
Volume	33
Issue number	7
DOIs	https://doi.org/10.1246/cl.2004.870
Publication status	Published - 2004 Jul 5

ASJC Scopus subject areas

Chemistry(all)

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

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