Time‐Resolved Fluorescence Study of the Dissociation of FMN from the Yellow Fluorescence Protein from Vibrio fischeri

  title={Time‐Resolved Fluorescence Study of the Dissociation of FMN from the Yellow Fluorescence Protein from Vibrio fischeri},
  author={Antonie J.W.G. Visser and Arie van Hoek and Nina V. Visser and Yongho Lee and Sandro Ghisla},
  journal={Photochemistry and Photobiology},
Time-resolved fluorescence spectroscopy of the flavin mononucleotide (FMN) prosthetic group of the yellow fluorescence protein (YFP) from Vibrio @hen has provided quantitative, thermodynamic information on the FMN-apoYFP equilibrium in aqueous buffer. In diluted aqueous solution two fluorescent species could be identified by distinct fluorescence lifetimes and rotational correlation times originating from free- and protein-bound FMN. Quantitation of the amounts of free and bound FMN in… 
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  • J. Lee
  • Biology, Chemistry
    Biophysical chemistry
  • 1993
A bacterial luciferase reaction with a negative temperature coefficient attributable to protein-protein interaction.
A yellow fluorescent protein (YFP) present in a strain of bioluminescent bacteria is shown here not only to modify the color and intensity of the emission, as already known and attributed to the
  • A. Visser
  • Chemistry, Physics
    Photochemistry and photobiology
  • 1984
The time dependence of the fluorescence of flavin adenine dinucleotide (FAD) was measured with a subnanosecond‐resolving fluorometer and the decay of FAD was proved to be nonexponential.