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.

Keywords

ChromophoreFlavin groupVibrioFluorescenceChemistryFluorescent proteinRiboflavinBiochemistryPhotochemistryBiologyGreen fluorescent proteinGeneticsBacteriaGeneEnzymePhysics

MeSH Terms

Flavin MononucleotideFluorescenceMolecular WeightSpectrometryFluorescenceVibrioViral Proteins

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Publication Info

Year
1987
Type
article
Volume
146
Issue
1
Pages
101-106
Citations
55
Access
Closed

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Cite This

Peter Macheroux, Katrin Schmidt, P. Steinerstauch et al. (1987). Purification of the yellow fluorescent protein from vibrio fischeri and identity of the flavin chromophore. Biochemical and Biophysical Research Communications , 146 (1) , 101-106. https://doi.org/10.1016/0006-291x(87)90696-6

Identifiers

DOI
10.1016/0006-291x(87)90696-6
PMID
3606610

Data Quality

Data completeness: 86%