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Characteristics of endogenous flavin fluorescence of Photobacterium leiognathi luciferase and Vibrio fischeri NAD(P)H:FMN‐oxidoreductase
Author(s) -
Vetrova E. V.,
Kudryasheva N. S.,
Visser A. J. W. G.,
van Hoek A.
Publication year - 2005
Publication title -
luminescence
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.428
H-Index - 45
eISSN - 1522-7243
pISSN - 1522-7235
DOI - 10.1002/bio.815
Subject(s) - flavin group , luciferase , nad+ kinase , luciferases , chemistry , photobacterium , bioluminescence , oxidoreductase , fluorescence , enzyme , fluorophore , biochemistry , stereochemistry , vibrio , biology , bacteria , physics , transfection , genetics , quantum mechanics , gene
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. Copyright © 2005 John Wiley & Sons, Ltd.