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Proceedings Paper

Fluorescence dynamics measurement of energy transfer in the bacterial luciferase and lumazine protein interaction
Author(s): John W. Lee; Wang Yanyun; B. V. Gibson; Dennis J. O'Kane
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Paper Abstract

The enzyme bacterial luciferase is able to transform the chemical exergonicity from the oxidation of FMNH2 and tetradecanal by oxygen, into electronic excitation of an associated fluorophore. The naturally occurring fluorophore in Photobacterium is 6,7-dimethyl-8-ribityllumazine bound to a protein that interacts in some way with the luciferase. Lumazine protein is not only raised to its excited state during the reaction but its presence alters the bioluminescence kinetics, possibly by catalyzing the decomposition of a "chemically- charged" intermediate on the luciferase. The emitter of bioluminescence in the reaction of luciferase is a highly fluorescent reaction intermediate called the "Fluorescent Transient". Energy transfer between luciferase fluorophores and lumazine protein has been studied using time correlated fluorescence and anisotropy decay techniques. Results of these and previous studies show that the energy transformation process in bacterial bioluminescence does not involve these proteins in a resonance energy transfer process.

Paper Details

Date Published: 1 May 1990
PDF: 11 pages
Proc. SPIE 1204, Time-Resolved Laser Spectroscopy in Biochemistry II, (1 May 1990); doi: 10.1117/12.17717
Show Author Affiliations
John W. Lee, Univ. of Georgia (United States)
Wang Yanyun, Univ. of Georgia (United States)
B. V. Gibson, Univ. of Georgia (United States)
Dennis J. O'Kane, Univ. of Georgia (United States)


Published in SPIE Proceedings Vol. 1204:
Time-Resolved Laser Spectroscopy in Biochemistry II
Joseph R. Lakowicz, Editor(s)

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