Firefly luciferase produces hydrogen peroxide as a coproduct in dehydroluciferyl adenylate formation

Chembiochem. 2006 Jun;7(6):929-35. doi: 10.1002/cbic.200500443.

Abstract

Firefly luciferase catalyzes the synthesis of H2O2 from the same substrates as the bioluminescence reaction: ATP and luciferin (D-LH2). About 80% of the enzyme-bound intermediate D-luciferyl adenylate (D-LH2-AMP) is oxidized into oxyluciferin, and a photon is emitted during this reaction. The enzyme pathway responsible for the generation of H2O2 is a side reaction in which D-LH2-AMP is oxidized into dehydroluciferyl adenylate (L-AMP). Like the bioluminescence reaction, the luciferase-catalyzed synthesis of H2O2 and L-AMP is a stereospecific process, involving only the natural D enantiomer. However, the intramolecular electron transfer postulated as essential to the light emission process is not involved in this side reaction.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Animals
  • Chromatography, High Pressure Liquid
  • Firefly Luciferin / metabolism*
  • Hydrogen Peroxide / analysis
  • Hydrogen Peroxide / metabolism*
  • Luciferases, Firefly / metabolism*
  • Models, Biological
  • Molecular Structure
  • Oxidation-Reduction
  • Oxygen / metabolism

Substances

  • dehydroluciferin
  • Firefly Luciferin
  • Adenosine Triphosphate
  • Hydrogen Peroxide
  • Luciferases, Firefly
  • Oxygen