Luciferin
Mostrando 1-12 de 77 artigos, teses e dissertações.
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1. Brazilian Bioluminescent Beetles: Reflections on Catching Glimpses of Light in the Atlantic Forest and Cerrado
ABSTRACT Bioluminescence - visible and cold light emission by living organisms - is a worldwide phenomenon, reported in terrestrial and marine environments since ancient times. Light emission from microorganisms, fungi, plants and animals may have arisen as an evolutionary response against oxygen toxicity and was appropriated for sexual attraction, predation
An. Acad. Bras. Ciênc.. Publicado em: 2018
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2. Mechanistic study on fungi bioluminescence / Estudo mecanístico da bioluminescência de fungos
Esta tese descreve como é possível obter emissão de luz in vitro enzimaticamente, a partir de extratos quente e frio de diferentes espécies de fungos bioluminescentes, o que indica também um mecanismo comum de bioluminescência em todos esses organismos. Dados cinéticos sugerem um mecanismo enzimático em duas etapas e corroboram a hipótese enzimátic
Publicado em: 2010
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3. Extraction of Renilla-type luciferin from the calcium-activated photoproteins aequorin, mnemiopsin, and berovin.
Photoproteins, which emit light in an oxygen-independent intramolecular reaction initiated by calcium ions, have been isolated from several bioluminescent organisms, including the hydrozoan jellyfish Aequorea and the ctenophore Mnemiopsis. The system of a related anthozoan coelenterate, the sea pansy Renilla reniformis, however, is oxygen dependent, requirin
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4. Structure of native Renilla reinformis luciferin
The structure of native luciferin from the bioluminescent coelenterate Renilla reniformis is shown to be 3,7-dihydro-2-(p-hydroxybenzyl)-6-(p-hydroxyphenyl)-8-benzylimidazo[1,2-a]pyrazin-3-one by mass spectral analysis of synthetic luciferin and the luciferin derived from a protein directly involved in the bioluminescent system. A previous report of the mole
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5. Can coelenterates make coelenterazine? Dietary requirement for luciferin in cnidarian bioluminescence
In the calcium-activated photoprotein aequorin, light is produced by the oxidation of coelenterazine, the luciferin used by at least seven marine phyla. However, despite extensive research on photoproteins, there has been no evidence to indicate the origin of coelenterazine within the phylum Cnidaria. Here we report that the hydromedusa Aequorea victori
The National Academy of Sciences.
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6. Circadian expression of the luciferin-binding protein correlates with the binding of a protein to the 3' untranslated region of its mRNA.
The circadian-expressed luciferin-binding protein from the dinoflagellate Gonyaulax polyedra is regulated at the translational level. We detected a protein, apparently a dimer, that binds specifically to the 3' untranslated region of its mRNA. Its binding site was localized within a 22-nt region in the 3' untranslated region containing seven UG repeats. The
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7. Source of oxygen in the CO2 produced in the bioluminescent oxidation of firefly luciferin
Incorporation of 18O into the CO2 produced in the bioluminescent oxidation of firefly luciferin was studied. In H216O medium with 18O2 gas, the product CO2 contained up to 75% C16O18O, showing that one O of the product CO2 arose from the O2 that oxidized luciferin. This result is consistent with a dioxetane mechanism. Analysis of the mass spectral data of th
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8. Isolation and expression of a cDNA encoding Renilla reniformis luciferase.
Renilla reniformis is an anthozoan coelenterate capable of exhibiting bioluminescence. Bioluminescence in Renilla results from the oxidation of coelenterate luciferin (coelenterazine) by luciferase [Renilla-luciferin:oxygen 2-oxidoreductase (decarboxylating), EC 1.13.12.5]. In vivo, the excited state luciferin-luciferase complex undergoes the process of nonr
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9. CRYSTALLINE LUCIFERIN FROM A LUMINESCENT FISH, PARAPRIACANTHUS BERYCIFORMES*
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10. Cloning and expression of cDNA for the luciferase from the marine ostracod Vargula hilgendorfii.
The marine ostracod Vargula hilgendorfii ejects luciferin and luciferase into seawater to produce a bright luminous cloud. The light is due to the oxidation of luciferin, an imidazopyrazine compound, by molecular oxygen, catalyzed by luciferase. The mechanism of the reaction has been studied extensively and the 60 kcal/mol required for the blue emission have
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11. PARTIAL PURIFICATION AND PROPERTIES OF BACTERIAL LUCIFERIN AND LUCIFERASE1
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12. Crossreactivity between the light-emitting systems of distantly related organisms: Novel type of light-emitting compound
Dinoflagellate luciferin has been found to crossreact and emit light with euphausid photoprotein; and euphausid fluorescent substance gives luminescence with dinoflagellate luciferase. Luciferin and the fluorescent substance, both highly unstable and fluorescent compounds, are biochemically similar but not identical. Preliminary spectral and chemical data su