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… 
Crystal Structures of the Lumazine Protein from Photobacterium kishitanii in Complexes with the Authentic Chromophore, 6,7-Dimethyl- 8-(1′-d-Ribityl) Lumazine, and Its Analogues, Riboflavin and Flavin Mononucleotide, at High Resolution
TLDR
The crystal structures of LumP from Photobacterium kishitanii in complexes with DMRL and its analogues, riboflavin (RBF) and flavin mononucleotide (FMN) are determined and it is suggested that the chromophore is located close enough for direct energy transfer to occur.
Lumazine proteins from photobacteria: localization of the single ligand binding site to the N-terminal domain
TLDR
It is shown that the N-terminal domain is the unique site for ligand binding in lumazine protein, which is believed to serve as an optical transponder in bioluminescence emission by certain marine bacteria.
Domain structure of riboflavin synthase.
TLDR
The data show that a single domain comprises the intact binding site for one substrate molecule in the enzyme-catalyzed dismutation of riboflavin, and each active site of the enzyme appears to be located at the interface of an N- terminal and C-terminal domain.
Structure of lumazine protein, an optical transponder of luminescent bacteria.
TLDR
An extensive crystallization screen was performed using numerous single-site mutants of the lumazine protein from Photobacterium leiognathi in complex with its fluorophore and with riboflavin, respectively, yielding suitable crystals.
Genetic Control of Biosynthesis and Transport of Riboflavin and Flavin Nucleotides and Construction of Robust Biotechnological Producers
TLDR
Whereas earlier RF overproducers were isolated by classical selection, current producers of riboflavin and flavin nucleotides have been developed using modern approaches of metabolic engineering that involve overexpression of structural and regulatory genes of the RF biosynthetic pathway as well as genes involved in the overproduction of the purine precursor of rib oflavin, GTP.
Biochemistry and genetics of bacterial bioluminescence.
  • P. Dunlap
  • Chemistry, Medicine
    Advances in biochemical engineering/biotechnology
  • 2014
TLDR
The evolutionary origins and physiological function of bioluminescence in bacteria are not well understood but are thought to relate to utilization of oxygen as a substrate in the luminescence reaction.
Investigation of recombinant protein production by Escherichia coli : expression of Green fluorescent protein and a co-factor dependent flavinated enzyme
This thesis summarises work done on the Escherichia coli strain MG1655 expressing a Green Fluorescent Protein (GFP) and the flavo-protein N-methyl-L-tryptophan oxidase (MTOX) product and examining
Biosynthesis of Vitamin B2
TLDR
Acid quenching of reaction mixtures of riboflavin synthase of Methanococcus jannaschii afforded a compound whose optical absorption and NMR spectra resemble that of the pentacyclic E. coli rib oflavin synthesis intermediate, whereas the circular dichroism spectra of the two compounds have similar envelopes but opposite signs.
Activities of the Bimodal Fluorescent Protein Produced by Photobacterium phosphoreum Strain bmFP in the Luciferase Reaction In Vitro
TLDR
After bmFP was used in luciferase reactions initiated either chemically or electrochemically, it was still capable of emitting bimodal fluorescence.
Biosynthesis of vitamin B2: Structure and mechanism of riboflavin synthase.
TLDR
The structures and reaction mechanisms of riboflavin synthases and related proteins up to 2007 are reviewed and 122 references are cited.
...
1
2
3
...

References

SHOWING 1-10 OF 28 REFERENCES
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.
Spectroscopic investigations of the single tryptophan residue and of riboflavin and 7-oxolumazine bound to lumazine apoprotein from Photobacterium leiognathi.
TLDR
A new method is designed for evaluation of the rate constant of energy transfer by measuring the (picosecond) rise time of the acceptor fluorescence, which indicates no change in secondary structure on binding to the apoprotein.
Two active forms of the accessory yellow fluorescence protein of the luminous bacterium Vibrio fischeri strain Y1
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.
Free and membrane-bound forms of bacterial cytochrome c4.
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.
...
1
2
3
...