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 |
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Pages (from-to) | 870-871 |
Number of pages | 2 |
Journal | Chemistry Letters |
Volume | 33 |
Issue number | 7 |
DOIs | |
Publication status | Published - 2004 Jul 5 |
ASJC Scopus subject areas
- Chemistry(all)