Review Article

Protein structure and bioluminescent spectra for firefly bioluminescence

  1. N. N. Ugarova1,*,
  2. L. Y. Brovko2

Article first published online: 23 SEP 2002

DOI: 10.1002/bio.688

Issue

Luminescence

Luminescence

Volume 17, Issue 5, pages 321–330, September/October 2002

Additional Information

How to Cite

Ugarova, N. N. and Brovko, L. Y. (2002), Protein structure and bioluminescent spectra for firefly bioluminescence. Luminescence, 17: 321–330. doi: 10.1002/bio.688

Author Information

  1. 1

    Chemical Department, Lomonosov Moscow State University, Moscow 117899, Russian Federation

  2. 2

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

*Chemical Department, Lomonosov Moscow State University, Moscow 117899, Russian Federation

Publication History

  1. Issue published online: 23 SEP 2002
  2. Article first published online: 23 SEP 2002
  3. Manuscript Accepted: 20 DEC 2002
  4. Manuscript Received: 7 SEP 2002

Funded by

  • Russian Foundation of Fundamental Investigations (RFFI). Grant Number: 99-04-49-219

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Keywords:

  • bioluminescence;
  • luciferase;
  • luciferin;
  • ATP;
  • fireflies;
  • bioluminescence spectra;
  • protein structure;
  • mutation of amino acid residues

Abstract

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 the 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 red shift of the 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 the polarizability, the larger was the red shift of bioluminescence. Copyright © 2002 John Wiley & Sons, Ltd.

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