12th International Symposium on Bioluminescence & Chemiluminescence

Symposium abstracts:

Protein structure and bioluminescent spectra for firefly bioluminescence

Ugarova, Nataliya N.¹, Brovko Lubov Yu.²

1. Dept of Chemistry, Lomonosov Moscow State University, Moscow 117899, Russia
Email: unn@enz.chem.msu.ru

2. Department of Food Science, University of Guelph, Guelph, Ontario N1G 2W1, Canada

Modern theory on general and specific effects of microenvironment on emission spectra was used for explanation of spectral differences for both natural and mutant forms of beetle luciferases as well as for bioluminescence emitter oxyluciferin in model systems. For the analysis both authors’ and other published data were used. It was shown that active site mutations that resulted in spectral shifts of bioluminescence as a rule caused substantial decrease in catalytic activity of the enzyme. At the same time mutations in the conservative regions of the protein amino acid sequence that were in the periphery of the protein globe resulted in the red shift of bioluminescence spectra without affecting catalytic activity. Correlation was observed between the value of spectral shift and polarizability of the introduced amino acid residue: the higher was the polarizability the larger was red shift of bioluminescence.

This is a preprint of an article accepted for publication in Luminescence: Copyright 2001 John
Wiley & Sons, Ltd (Wiley website)