Configurational fluctuations and flavin-substrate interactions in the flavoenzyme ThyX studied by time- and spectrally resolved fluorescence - École polytechnique Access content directly
Journal Articles EPJ Web of Conferences Year : 2013

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

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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Dates and versions

hal-00943019 , version 1 (06-02-2014)

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Sergey P. Laptenok, Latifa Bouzhir-Sima, Hannu Myllykallio, Ursula Liebl, Marten H. Vos. Configurational fluctuations and flavin-substrate interactions in the flavoenzyme ThyX studied by time- and spectrally resolved fluorescence. EPJ Web of Conferences, 2013, 41, pp.07011. ⟨10.1051/epjconf/20134107011⟩. ⟨hal-00943019⟩
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