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

  title={Purification and characterization of flavoproteins and cytochromes from the yellow bioluminescence marine bacterium Vibrio fischeri strain Y1.},
  author={Valentin N Petushkov and J. Lee},
  journal={European journal of biochemistry},
  volume={245 3},
  • V. PetushkovJ. Lee
  • Published 1 May 1997
  • Biology, Chemistry
  • European journal of biochemistry
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

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

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.

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.

Genetic Control of Biosynthesis and Transport of Riboflavin and Flavin Nucleotides and Construction of Robust Biotechnological Producers

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
  • Biology
    Advances in biochemical engineering/biotechnology
  • 2014
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 and the flavo-protein N-methyl-L-tryptophan oxidase (MTOX) product and examines the effect foreign protein production has on cell growth parameters, comparable to that seen in E.coli fermentations.

Activities of the Bimodal Fluorescent Protein Produced by Photobacterium phosphoreum Strain bmFP in the Luciferase Reaction In Vitro

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.

The Sensitized Bioluminescence Mechanism of Bacterial Luciferase

After more than one‐half century of investigations, the mechanism of bioluminescence from the FMNH2 assisted oxygen oxidation of an aliphatic aldehyde on bacterial luciferase continues to resist

Biosynthesis of flavocoenzymes.

The biosynthesis of one riboflavin molecule requires one molecule of GTP and two molecules of ribulose 5-phosphate to produce 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione, which is recycled in the biosynthetic pathway.



Yellow light emission of Vibrio fischeri strain Y-1: purification and characterization of the energy-accepting yellow fluorescent protein.

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.

Properties of recombinant fluorescent proteins from Photobacterium leiognathi and their interaction with luciferase intermediates.

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.

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Spectroscopic investigations of the single tryptophan residue and of riboflavin and 7-oxolumazine bound to lumazine apoprotein from Photobacterium leiognathi.

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.

Direct measurement of excitation transfer in the protein complex of bacterial luciferase hydroxyflavin and the associated yellow fluorescence proteins from Vibrio fischeri Y1.

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.

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