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

Satoshi Hirata, Hirofumi Kurokawa, Ikuko Sagami, Toru Shimizu

Research output: Contribution to journalArticlepeer-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 languageEnglish
Pages (from-to)870-871
Number of pages2
JournalChemistry Letters
Volume33
Issue number7
DOIs
Publication statusPublished - 2004 Jul 5

ASJC Scopus subject areas

  • Chemistry(all)

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