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Activities of the Bimodal Fluorescent Protein Produced by Photobacterium phosphoreum Strain bmFP in the Luciferase Reaction In Vitro
Author(s) -
Karatani Hajime,
Konaka Taku
Publication year - 2000
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1562/0031-8655(2000)0710237aotbfp2.0.co2
Subject(s) - photobacterium phosphoreum , luciferase , strain (injury) , fluorescence , photobacterium , chemistry , in vitro , microbiology and biotechnology , biochemistry , biology , bacteria , organic chemistry , vibrio , gene , anatomy , toxicity , transfection , physics , genetics , quantum mechanics
The activity of the bimodal fluorescent protein (bmFP) ( λ max , 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.