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

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 O2molecule... Ausführliche Beschreibung

1. Person: Shimomura, Osamu
Weitere Personen: Johnson, Frank H. verfasserin; Kohama, Yasuhiro verfasserin
Quelle: in Proceedings of the National Academy of Sciences of the United States of America Vol. 69, No. 8 (1972), p. 2086-2089
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Format: Online-Artikel
Sprache: English
Veröffentlicht: 1972
Beschreibung: Online-Ressource
Schlagworte: research-article
Biochemistry
Achromobacter fischeri
Aldehyde
Luciferin
Luciferase
Flavin
Quantum yield
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Zusammenfassung: 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 O2molecules, 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.
ISSN: 0027-8424

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