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. 1972 Aug;69(8):2086–2089. doi: 10.1073/pnas.69.8.2086

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

Osamu Shimomura 1, Frank H Johnson 1, Yasuhiro Kohama 1
PMCID: PMC426874  PMID: 4506078

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 O2 molecules, in the presence of a “purple protein” cofactor, yielding a ketone, HCOOH, CO2, 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.

Keywords: Achromobacter fischeri, aldehyde, luciferin, luciferase, flavin, quantum yield

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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