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Coelenterazine-dependent luciferases.

S V Markova1, E S Vysotski

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Summary

Bioluminescence involves diverse light-emitting mechanisms across species, even when using similar substrates like coelenterazine or Cypridina luciferin. This review examines luciferases and their engineered variants for enhanced bioluminescence imaging applications.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Marine Biology

Background:

  • Bioluminescence is a natural light emission process found across diverse taxa, including bacteria, fungi, invertebrates, and fish.
  • Despite a common outcome, the biochemical mechanisms of light production vary significantly between different luminous organisms.
  • Key substrates for bioluminescent reactions in marine organisms include imidazopyrazinone derivatives like coelenterazine and Cypridina luciferin.

Purpose of the Study:

  • To review luciferases from various luminous organisms that utilize coelenterazine or Cypridina luciferin.
  • To discuss modifications of these luciferases aimed at improving their properties for in vivo bioluminescence imaging.

Main Methods:

  • Comparative analysis of bioluminescent systems across different taxa.
  • Examination of the structural and sequence diversity of luciferases.
  • Review of protein engineering strategies applied to luciferases.

Main Results:

  • Luciferases employing the same substrate (coelenterazine or Cypridina luciferin) exhibit significant divergence in amino acid sequences and spatial structures.
  • Despite structural differences, these luciferases catalyze light emission through related biochemical pathways.
  • Engineered luciferases demonstrate enhanced physicochemical and bioluminescent properties.

Conclusions:

  • The diversity of luciferase structures highlights convergent evolution in bioluminescence.
  • Modified luciferases offer improved tools for advanced bioluminescence imaging techniques.
  • Understanding luciferase diversity is crucial for developing novel bioimaging applications.