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

Sergey Laptenok 1 Latifa Bouzhir-Sima 1 Hannu Myllykallio 1 Ursula Liebl 1 Marten Vos 1, *
* Corresponding author
1 LOB - Laboratoire d'optique et biosciences
Abstract : 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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Sergey Laptenok, Latifa Bouzhir-Sima, Hannu Myllykallio, Ursula Liebl, Marten Vos. Configurational fluctuations and flavin-substrate interactions in the flavoenzyme ThyX studied by time- and spectrally resolved fluorescence. EPJ Web of Conferences, EDP Sciences, 2013, 41, pp.07011. ⟨10.1051/epjconf/20134107011⟩. ⟨hal-00943019⟩

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