EPJ Web of Conferences 41, 07011 (2013)
https://doi.org/10.1051/epjconf/20134107011
https://doi.org/10.1051/epjconf/20134107011
Configurational fluctuations and flavin-substrate interactions in the flavoenzyme ThyX studied by time- and spectrally resolved fluorescence
Laboratory for Optics and Biosciences, CNRS UMR7645, INSERM U696, Ecole Polytechnique, 91128 Palaiseau, France
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
This is an Open Access article distributed under the terms of the Creative Commons Attribution License 2.0, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
