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<dc:title xml:lang="fr">Étude des propriétés optiques de l’oxyluciférine et de ses analogues</dc:title>
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<dc:subject xml:lang="fr">Spectroscopie à l’état stationnaire</dc:subject>
<dc:subject xml:lang="fr">Résolue en temps</dc:subject>
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<dc:subject xml:lang="en">Oxyluciferin</dc:subject>
<dc:subject xml:lang="en">Luciferase</dc:subject>
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<dcterms:abstract xml:lang="fr">La bioluminescence est un phénomène naturel au cours duquel des organismes vivants convertissent de l’énergie chimique en lumière. Dans le cas de la luciole, la réaction implique une réaction d’oxydation de la luciférine, catalysée par la luciférase, produisant le photoproduit oxyluciférine dans son premier état excité. L’oxyluciférine peut ensuite émettre une lumière pouvant varier du jaune-vert au rouge par relaxation vers son état fondamental. Le photoproduit peut exister sous six formes chimiques différentes provenant d’une conversion kéto/enol et de déprotonations des groupes phénols ou énols. La première partie de la thèse consistera à étudier les propriétés optiques des différentes formes chimiques en solution aqueuse, ainsi qu’à résoudre la dynamique des transferts de proton existant à l’état excité à l’aide de la spectroscopie pompe-sonde. Dans la dernière partie nous avons déterminer la nature de l’espèce produisant la bioluminescence en formant des complexes avec les formes chimiques synthétisées et la luciférase.</dcterms:abstract>
<dcterms:abstract xml:lang="en">Bioluminescence is a natural phenomenon during which living organisms convert chemical energy into light. The light is emitted through luciferase-catalysed reaction of D-luciferin substrate resulting in the formation of oxyluciferin (OxyLH2) in its first singlet excited state, which later decays radiatively to the ground state. OxyLH2 emits visible light with an emission that can vary from green to red. It can exist under six different chemical forms resulting from keto/enol tautomerization and deprotonation of phenol and/or enol moieties. In the first part of this work, we characterized the optical properties of OxyLH2 and its derivatives in aqueous buffer and we deciphered its photoluminescence pathway by monitoring the excited state proton transfer using pump-probe spectroscopy. We finally characterized the absorption and emission of OxyLH2’s forms inside the protein. These results were compared to those obtained on the complex formed after the bioluminescence reaction with D-luciferin. The goal of this part is to determine the nature of the emitter which produce the bioluminescence.</dcterms:abstract>
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