Time-resolved fluorescence spectroscopy of lumazine protein from Photobacterium phosphoreum using synchrotron radiation

  title={Time-resolved fluorescence spectroscopy of lumazine protein from Photobacterium phosphoreum using synchrotron radiation},
  author={Antonie J.W.G. Visser and Arie van Hoek and Dennis J. O'Kane and J-Y. Lee},
  journal={European Biophysics Journal},
Time-resolved fluorescence on lumazine protein from Photobacterium phosphoreum was performed with synchrotron radiation as a source of continuously tunable excitation. The experiments yielded structural and dynamic details from which two aspects became apparent. From fluorescence anisotropy decay monitoring of lumazine fluorescence with different excitation wavelengths, the average correlation times were shown to change, which must indicate the presence of anisotropic motion of the protein. A… 
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Time‐Resolved Fluorescence Study of the Dissociation of FMN from the Yellow Fluorescence Protein from Vibrio fischeri
Time-resolved fluorescence spectroscopy of the flavin mononucleotide (FMN) prosthetic group of the yellow fluorescence protein (YFP) from Vibrio @hen has provided quantitative, thermodynamic
Lumazine protein and the excitation mechanism in bacterial bioluminescence.
  • J. Lee
  • Chemistry, Medicine
    Biophysical chemistry
  • 1993
From measurements of the decay of fluorescence anisotropy of lumazine protein alone and in mixtures with theLuciferase fluorescent transient, it is shown that a protein-protein complex is formed and that there is rapid energy transfer between the flavin on the luciferase and the lumazine derivative bound to its protein.
Fluorescence anisotropy decay study of self-association of bacterial luciferase intermediates
The fluorescence dynamics parameters of the fluorescent transient flavin-luciferase species from the typesVibrio fischeri andPhotobacterium leiognathi are presented and it is proposed that the self-association competes with the lumazine protein interaction in the bioluminescence reaction.
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Purification of lumazine proteins from Photobacterium leiognathi and Photobacterium phosphoreum: bioluminescence properties.
Bright strains of the marine bioluminescent bacterium Photobacterium leiognathi produce a "lumazine protein" in amounts comparable to that previously found in Photobacteria phosphoreum, but in dimmer strains the amounts of lumazine protein in extracts are less, and also there is an accompanying shift of the biolumscence spectral maximum to longer wavelength.
Spectral properties and function of two lumazine proteins from Photobacterium.
The spectral properties are compared for two 6,7-dimethyl-8-ribityllumazine proteins from marine bioluminescent bacteria, one from a psychrophile, Photobacterium phosphoreum, and the other from a
Determination of rotational correlation times from deconvoluted fluorescence anisotropy decay curves. Demonstration with 6,7-dimethyl-8-ribityllumazine and lumazine protein from Photobacterium leiognathi as fluorescent indicators.
The experimental and analytical protocols required for obtaining rotational correlation times of biological macromolecules from fluorescence anisotropy decay measurements are described and the unbound 6,7-dimethyl-8-ribityllumazine protein was used as a model compound for determining correlation times in the picosecond time range.
Physical characterization of lumazine proteins from Photobacterium.
The physicochemical properties of Photobacterium lumazine proteins have been investigated, and there is insufficient area on the exterior surface to accommodate hydration when the lumzine proteins are considered as smooth-surfaced ellipsoids.
Spectroscopic investigations of the single tryptophan residue and of riboflavin and 7-oxolumazine bound to lumazine apoprotein from Photobacterium leiognathi.
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Dynamic fluorescence properties of bacterial luciferase intermediates.
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Chemical characterization of lumazine protein from Photobacterium leiognathi: comparison with lumazine protein from Photobacterium phosphoreum.
The UV and visible absorption spectra of both lumazine proteins denatured in 6 M guanidine hydrochloride can be accurately modeled by using the number of equivalents of the lumazine derivative and blocked aromatic amino acid model compounds determined by chemical and spectrophotometric analyses for Trp, Tyr, and Phe.
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