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Configurational fluctuations and flavin-substrate interactions in the flavoenzyme ThyX studied by time- and spectrally resolved fluorescence
Journal article   Open access  Peer reviewed

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

Sergey Laptenok, Latifa Bouzhir-Sima, Hannu Myllykallio, Ursula Liebl and Marten Vos
EPJ Web of conferences, Vol.41, pp.07011-np
01/01/2013
DOI: https://doi.org/10.1051/epjconf/20134107011

Abstract

Biochemistry, Molecular Biology Biological Physics Life Sciences Physics
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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https://doi.org/10.1051/epjconf/20134107011View
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