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A time-dependent bacterial bioluminescence emission spectrum in an in vitro single turnover system : energy transfer alone cannot account for the yellow emission of Vibrio fischeri Y-1

A time-dependent bacterial bioluminescence emission spectrum in an in vitro single turnover system : energy transfer alone cannot account for the yellow emission of Vibrio fischeri Y-1

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ECKSTEIN, Jens W., Ki Woong CHO, Pio COLEPICOLO, Sandro GHISLA, John Woodland HASTINGS, Thérèse WILSON, 1990. A time-dependent bacterial bioluminescence emission spectrum in an in vitro single turnover system : energy transfer alone cannot account for the yellow emission of Vibrio fischeri Y-1. In: Proceedings of the National Academy of Sciences of the United States of America. 87(4), pp. 1466-1470

@article{Eckstein1990time--8503, title={A time-dependent bacterial bioluminescence emission spectrum in an in vitro single turnover system : energy transfer alone cannot account for the yellow emission of Vibrio fischeri Y-1}, year={1990}, number={4}, volume={87}, journal={Proceedings of the National Academy of Sciences of the United States of America}, pages={1466--1470}, author={Eckstein, Jens W. and Cho, Ki Woong and Colepicolo, Pio and Ghisla, Sandro and Hastings, John Woodland and Wilson, Thérèse} }

1990 Cho, Ki Woong Wilson, Thérèse Cho, Ki Woong Eckstein, Jens W. Colepicolo, Pio 2011-03-24T17:44:12Z Hastings, John Woodland Ghisla, Sandro eng Colepicolo, Pio deposit-license Wilson, Thérèse Hastings, John Woodland A time-dependent bacterial bioluminescence emission spectrum in an in vitro single turnover system : energy transfer alone cannot account for the yellow emission of Vibrio fischeri Y-1 First publ. in: Proceedings of the National Academy of Sciences of the United States of America ; 87 (1990), 4. - S. 1466-1470 2011-03-24T17:44:12Z Ghisla, Sandro Eckstein, Jens W. Yellow fluorescent protein (YFP), which has a bound FMN, was isolated from the marine bacterium Vibrio fischeri strain Y-1b. Its presence in a luciferase [alkanal monooxygenase (FMN-linked); alkanal, reduced-FMN:oxygen oxidoreductase (1-hydroxylating, luminescing), EC 1.14.14.3] reaction mixture causes a striking color change, and an increase in bioluminescence intensity, as well as a faster rate of intensity decay, so that the quantum yield is not changed. The emission spectrum shows two distinct color bands, one at 490 nm attributed to the unaltered emission of the luciferase system, the other peaking in the yellow around 540 nm due to YFP emission. The kinetics of the two color bands differ, so the spectrum changes with time. The yellow emission reaches its initial maximum intensity later than the blue, and then both blue and yellow emissions decay exponentially with nearly the same pseudo-first-order rate constants, linearly dependent on [YFP] (from 0.01 sec-1 with no YFP to a maximum of ≈0.1 sec-1 at 4°C) but exhibiting a saturation behavior. The data can be interpreted by assuming the interaction of YFP with the peroxyhemiacetal intermediate in the luciferase reaction to form an unstable new complex whose breakdown gives the yellow emitter in its excited state. This simple model fits well the data at [YFP] < 15 µM. The results indicate that a single primary excited state cannot be responsible for the blue and the yellow emissions. application/pdf

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