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 |
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ページ(範囲) | 870-871 |
ページ数 | 2 |
ジャーナル | Chemistry Letters |
巻 | 33 |
号 | 7 |
DOI | |
出版ステータス | Published - 2004 7月 5 |
ASJC Scopus subject areas
- 化学 (全般)