Characteristics of endogenous flavin fluorescence of Photobacterium leiognathi luciferase and Vibrio fisheri NAD(P)H:FMN-oxidoreductase

E.V. Vetrova, N.S. Kudryasheva, A.J.W.G. Visser, A. van Hoek

Research output: Contribution to journalArticleAcademicpeer-review

18 Citations (Scopus)

Abstract

The bioluminescent bacterial enzyme system NAD(P)H:FMN-oxidoreductase-luciferase has been used as a test system for ecological monitoring. One of the modes to quench bioluminescence is the interaction of xenobiotics with the enzymes, which inhibit their activity. The use of endogenous flavin fluorescence for investigation of the interactions of non-fluorescent compounds with the bacterial luciferase from Photobacterium leiognathi and NAD(P)H:FMN-oxidoreductase from Vibrio fischeri has been proposed. Fluorescence spectroscopy methods have been used to study characteristics of endogenous flavin fluorescence (fluorophore lifetime, the rotational correlation time). The fluorescence anisotropy behaviour of FMN has been analysed and compared to that of the enzyme-bound flavin. The fluorescence characteristics of endogenous flavin of luciferase and NAD(P)H:FMN-oxidoreductase have been shown to be applicable in studying enzymes' interactions with non-fluorescent compounds
Original languageEnglish
Pages (from-to)205-209
JournalLuminescence
Volume20
Issue number3
DOIs
Publication statusPublished - 2005

Keywords

  • flavodoxin
  • anisotropy
  • reductase
  • dynamics
  • system

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