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1 February 2000 Activities of the Bimodal Fluorescent Protein Produced by Photobacterium phosphoreum Strain bmFP in the Luciferase Reaction In Vitro
Hajime Karatani, Taku Konaka
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Abstract

The activity of the bimodal fluorescent protein (bmFP) (λmax, 488 and 517 nm) in the in vitro luciferase reaction has been studied. The bmFP that is produced by Photobacterium phosphoreum strain bmFP is a dimer of two homologous subunits binding four riboflavin 5′-phosphate (FMN)-myristate chromophores. The addition of bmFP to the luciferase reaction in the presence of the lumazine protein prevented the lumazine protein-induced blue shift in the emission band. The bmFP reduced electrochemically serves as a substrate in the luciferase reaction in the absence of added FMN, resulting in light emission with a single maximum at about 487 nm. The bmFP was also active in lieu of FMN in the NADH/FMN oxidoreductase (flavin reductase)–luciferase coupled bioluminescence reaction in the absence of added FMN. In the coupled reaction, bioluminescence with the isolated bmFP chromophore was weaker than that with the holo-bmFP. After bmFP was used in luciferase reactions initiated either chemically or electrochemically, it was still capable of emitting bimodal fluorescence.

Hajime Karatani and Taku Konaka "Activities of the Bimodal Fluorescent Protein Produced by Photobacterium phosphoreum Strain bmFP in the Luciferase Reaction In Vitro," Photochemistry and Photobiology 71(2), 237-242, (1 February 2000). https://doi.org/10.1562/0031-8655(2000)071<0237:AOTBFP>2.0.CO;2
Received: 27 August 1999; Accepted: 1 November 1999; Published: 1 February 2000
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KEYWORDS
bimodal fluorescence
coupled bioluminescence
flavin reductase
fluorescent protein
luciferase
LuxF protein
Photobacterium phosphoreum
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