title: Purification of the yellow fluorescent protein from Vibrio fischeri and identity of the flavin chromophore.
abstract: A low molecular weight protein (approximately 25,000 D) exhibiting a yellow fluorescence emission peaking at approximately 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 (lambda max = 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 (lambda max approximately 495 nm), this protein induces a bright yellow luminescence (lambda max approximately 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.
mesh_terms: D005486:Flavin Mononucleotide; D005453:Fluorescence; D008970:Molecular Weight; D013050:Spectrometry, Fluorescence; D014733:Vibrio / Q000032:analysis*; D014764:Viral Proteins / Q000302:isolation & purification*
chemical_list: D014764:Viral Proteins; D005486:Flavin Mononucleotide