Reactions involved in bioluminescence systems of limpet (Latia neritoides) and luminous bacteria

Proc Natl Acad Sci U S A. 1972 Aug;69(8):2086-9. doi: 10.1073/pnas.69.8.2086.

Abstract

Luminescence in Latia involves a specific flavoprotein enzyme ("luciferase"), which has a tightly bound flavin group constituting the light-emitter. The overall reaction includes oxidation of a specific substrate ("luciferin," an enol formate derivative of an aliphatic aldehyde), by 2 O(2) molecules, in the presence of a "purple protein" cofactor, yielding a ketone, HCOOH, CO(2), and light. In Achromobacter, a required aliphatic aldehyde, which is functionally equivalent to Latia luciferin, is oxidized to an acid containing the same hydrocarbon chain as the aldehyde; this reaction proceeds in the presence of bacterial luciferase and reduced flavin mononucleotide with a quantum yield of 0.17 + 0.1 photons per aldehyde molecule that is independent of aldehyde chain length from 9 to at least 14 carbons.

MeSH terms

  • Alcaligenes / enzymology
  • Alcaligenes / metabolism*
  • Aldehydes / metabolism*
  • Animals
  • Cyanides / metabolism
  • Firefly Luciferin / metabolism*
  • Fishes / metabolism*
  • Flavin-Adenine Dinucleotide / metabolism
  • Fluorescence
  • Hydrocarbons / metabolism
  • Luciferases / metabolism*
  • Luminescent Measurements*
  • Mass Spectrometry
  • Methods
  • Mollusca / enzymology
  • Spectrophotometry

Substances

  • Aldehydes
  • Cyanides
  • Hydrocarbons
  • Flavin-Adenine Dinucleotide
  • Firefly Luciferin
  • Luciferases