Paper
5 February 1999 Comparative spectrochronography of different types of luciferases
E. Yu. Cherednikova, Andrey Yuri Chikishev, E. I. Dement'eva, O. V. Kosobokova
Author Affiliations +
Proceedings Volume 3732, ICONO '98: Laser Spectroscopy and Optical Diagnostics: Novel Trends and Applications in Laser Chemistry, Biophysics, and Biomedicine; (1999) https://doi.org/10.1117/12.340013
Event: ICONO '98: Laser Spectroscopy and Optical Diagnostics: Novel Trends and Applications in Laser Chemistry, Biophysics, and Biomedicine, 1998, Moscow, Russian Federation
Abstract
We investigated the dynamic properties of two firefly luciferases: Luciola Mingrelica, that contains the only tryptophan residue and Photinus Pyralis, that contains two tryptophan residues by means of fluorescence spectrochronography method. Relaxation time of protein matrix for Luciola mingrelica is estimated to be 2 ns. The dynamic properties of luciferases differ in spite of similar composition. We investigated also the influence of microenvironment on spectral and kinetic properties of luciferin. Fluorescence decay curves and stationary spectra were measured in 7 different solvents and in complex with luciferase. The closest coincidence of decay curves in the solvents with the decay curve in the complex with luciferase was obtained in water. It means that microenvironment of luciferase is not hydrophobic, as it had been determined earlier.
© (1999) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
E. Yu. Cherednikova, Andrey Yuri Chikishev, E. I. Dement'eva, and O. V. Kosobokova "Comparative spectrochronography of different types of luciferases", Proc. SPIE 3732, ICONO '98: Laser Spectroscopy and Optical Diagnostics: Novel Trends and Applications in Laser Chemistry, Biophysics, and Biomedicine, (5 February 1999); https://doi.org/10.1117/12.340013
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KEYWORDS
Luminescence

Bioluminescence

Proteins

Bioalcohols

Absorption

Molecules

Polarizability

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