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Journal articles

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

Sergey P. Laptenok 1 Latifa Bouzhir-Sima 1 Hannu Myllykallio 1 Ursula Liebl 1 Marten H. 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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Submitted on : Thursday, February 6, 2014 - 8:53:09 PM
Last modification on : Tuesday, October 19, 2021 - 5:12:18 PM
Long-term archiving on: : Wednesday, May 7, 2014 - 4:40:17 AM

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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, EDP Sciences, 2013, 41, pp.07011. ⟨10.1051/epjconf/20134107011⟩. ⟨hal-00943019⟩

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