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Separation and structure of the prosthetic group of the blue fluorescence protein from the bioluminescent bacterium Photobacterium phosphoreum.
  • P. Koka, J. Lee
  • Chemistry, Medicine
    Proceedings of the National Academy of Sciences…
  • 1 July 1979
The highly fluorescent prosthetic group of the blue fluorescence protein purified from the bioluminescent bacterium Photobacterium phosphoreum has been dissociated and separated from its apoprotein by affinity chromatography on Cibacron Blue-Sepharose and was readily transformed into riboflavin by rib oflavin synthetase.
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
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.
Raman spectra of flavin bound in flavodoxins and in other flavoproteins. Evidence for structural variations in the flavin-binding region.
The resonance coherent anti-Stokes Raman scattering (CARS) spectra for a number of flavoproteins are found to be fingerprints for the particular type of flavofiltration, based on tentative assignment of the vibrational modes in flavin models.
Bacterial bioluminescence: equilibrium association measurements, quantum yields, reaction kinetics, and overall reaction scheme.
Even when the aldehyde concentration limits the rate of the light reaction, the quantum yield of the long-lived intermediate is unchanged, and together these data mean that, under the optimal conditions chosen for quantum yield measurements, no dark side reactions effectively compete with the main reaction leading to light emission.
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
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.
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.