Purification of the yellow fluorescent protein from vibrio fischeri and identity of the flavin chromophore
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A low molecular weight protein (~ 25,000 D) exhibiting a yellow fluorescence emission peaking at ~ 540 nm was isolated from Vibrio fischeri (strain Y-1) and purified to apparent homogeneity. FMN is the chromophore, but it exhibits marked red shifts in both the absorption (λmax = 380, 460 nm) and the fluorescence emission. When added to purified luciferase from the same strain, which itself catalyzes an emission of blue-green light (λmax ~ 495 nm), this protein induces a bright yellow luminescence (λmax ~ 540 nm); this corresponds to the emission of the Y-1 strain in vivo. This yellow bioluminescence emission is thus ascribed to the interaction of these two proteins, and to the excitation of the singlet FMN bound to this fluorescent protein.
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MACHEROUX, Peter, K. U. SCHMIDT, Petra STEINERSTAUCH, Sandro GHISLA, Pio COLEPICOLO, Rudolf BUNTIC, J. Woodland HASTINGS, 1987. Purification of the yellow fluorescent protein from vibrio fischeri and identity of the flavin chromophore. In: Biochemical and Biophysical Research Communications. 1987, 146(1), pp. 101-106. ISSN 0006-291XBibTex
@article{Macheroux1987Purif-7105, year={1987}, title={Purification of the yellow fluorescent protein from vibrio fischeri and identity of the flavin chromophore}, number={1}, volume={146}, issn={0006-291X}, journal={Biochemical and Biophysical Research Communications}, pages={101--106}, author={Macheroux, Peter and Schmidt, K. U. and Steinerstauch, Petra and Ghisla, Sandro and Colepicolo, Pio and Buntic, Rudolf and Hastings, J. Woodland} }
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