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. 1972 Aug;69(8):2086-9.
doi: 10.1073/pnas.69.8.2086.

Reactions Involved in Bioluminescence Systems of Limpet (Latia Neritoides) and Luminous Bacteria

Free PMC article

Reactions Involved in Bioluminescence Systems of Limpet (Latia Neritoides) and Luminous Bacteria

O Shimomura et al. Proc Natl Acad Sci U S A. .
Free PMC article

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.

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