Purification and characterization of flavoproteins and cytochromes from the yellow bioluminescence marine bacterium Vibrio fischeri strain Y1.

@article{Petushkov1997PurificationAC,
  title={Purification and characterization of flavoproteins and cytochromes from the yellow bioluminescence marine bacterium Vibrio fischeri strain Y1.},
  author={Valentin N Petushkov and Jinhyuk Lee},
  journal={European journal of biochemistry},
  year={1997},
  volume={245 3},
  pages={
          790-6
        }
}
Several flavoproteins and cytochromes that occur as major components in extracts of the yellow bioluminescence Y1 strain of the marine bacterium Vibrio fischeri have been purified and characterized with respect to their mass (SDS/PAGE and matrix-assisted laser-desorption/ionization MS), chromatographic properties, N-terminal sequence, and spectroscopy (absorption, fluorescence emission and anisotropy decay). The investigated proteins were as follows: yellow fluorescence protein (YFP) with bound… 
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References

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Yellow light emission of Vibrio fischeri strain Y-1: purification and characterization of the energy-accepting yellow fluorescent protein.
TLDR
Addition of purified YFP to a reaction in which luciferase was supplied with FMNH2 (reduced FMN) by a NADH:FMN oxidoreductase resulted in a dramatic enhancement in the intensity of bioluminescence and an additional peak in the emission spectrum at about 534 nm.
Purification of the yellow fluorescent protein from Vibrio fischeri and identity of the flavin chromophore.
TLDR
A low molecular weight protein exhibiting a yellow fluorescence emission peaking at approximately 540 nm was isolated from Vibrio fischeri and purified to apparent homogeneity, and this emission is ascribed to the interaction of these two proteins, and to the excitation of the singlet FMN bound to this fluorescent protein.
Properties of recombinant fluorescent proteins from Photobacterium leiognathi and their interaction with luciferase intermediates.
TLDR
Fluorescence emission anisotropy decay was used to establish that none of these holoproteins complexed with native luciferase and that the lumazine protein alone formed a 1:1 complex with theLuciferase hydroxyflavin fluorescent transient and the Luciferase peroxyflavin intermediates.
Interaction of Photobacterium leiognathi and Vibrio fischeri Y1 luciferases with fluorescent (antenna) proteins: bioluminescence effects of the aliphatic additive.
The kinetics of the bacterial bioluminescence reaction is altered in the presence of the fluorescent (antenna) proteins, lumazine protein (LumP) from Photobacterium or the yellow fluorescence…
The yellow bioluminescence bacterium, Vibrio fischeri Y1, contains a bioluminescence active riboflavin protein in addition to the yellow fluorescence FMN protein.
TLDR
The yellow bioluminescence Y1 strain of Vibrio fischeri can produce a 22 kDa protein with either FMN or riboflavin as a bound fluorophore, and the in vivo emission appears to be an equal mixture of the two.
Expression and properties of the recombinant lumazine (riboflavin) protein from Photobacterium leiognathi.
TLDR
The absorption and fluorescence spectra, fluorescence yield, and bioluminescence properties of this rebound protein identify it as authentic lumazine protein.
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TLDR
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TLDR
In addition to the typical blue luminescence, the light emission of the luminous bacterium Vibrio fischeri strain Y1 has a yellow component, attributable to an accessory “yellow fluorescence protein” (YFP), which acts in conjunction with the enzyme luciferase and possesses a flavin chromophore.
Direct measurement of excitation transfer in the protein complex of bacterial luciferase hydroxyflavin and the associated yellow fluorescence proteins from Vibrio fischeri Y1.
TLDR
Time-resolved fluorescence was used to directly measure the energy transfer rate constant in the protein-protein complex involved in the yellow bioluminescence of Vibrio fischeri, strain Y1, and it was concluded that the topology of the protein complexes in both cases, must be very similar.
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TLDR
The behaviour of the holocytochromes in SDS was atypical, but removal of the haem groups resulted in a normal migration, and a model is proposed for the process of solubilization.
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