期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1972
卷号：69
期号：8
页码：2086-2089
DOI：10.1073/pnas.69.8.2086
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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.
