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
Complete list of metadatas

https://hal-polytechnique.archives-ouvertes.fr/hal-00943019
Contributor : Denis Roura <>
Submitted on : Thursday, February 6, 2014 - 8:53:09 PM
Last modification on : Thursday, November 14, 2019 - 2:32:24 PM
Long-term archiving on : Wednesday, May 7, 2014 - 4:40:17 AM

File

epjconf_up2012_07011.pdf
Publisher files allowed on an open archive

Identifiers

Collections

Citation

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⟩

Share

Metrics

Record views

295

Files downloads

169