Configurational fluctuations and flavin-substrate interactions in the flavoenzyme ThyX studied by time- and spectrally resolved fluorescence

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Laptenok, Sergey, P. | Bouzhir-Sima, Latifa | Myllykallio, Hannu | Liebl, Ursula | Vos, Marten, H.

Edité par CCSD ; EDP Sciences -

International audience. Femtosecond-resolved fluorescence of bacterial thymidilate synthase using a Kerr-gate based setup identifies a close-by tyrosine involved in flavin fluorescence quenching, shows that the substrate dUMP acts as a strong quencher itself and highlights functional configurational flexibility. © Owned by the authors, published by EDP Sciences, 2013

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