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

Satoshi Hirata, Hirofumi Kurokawa, Ikuko Sagami, Toru Shimizu

研究成果: Article査読

3 被引用数 (Scopus)

抄録

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
33
7
DOI
出版ステータスPublished - 2004 7 5

ASJC Scopus subject areas

  • 化学 (全般)

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