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)

1 LOB - Laboratoire d'optique et biosciences

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

Domains: Life Sciences [q-bio]; Biochemistry, Molecular Biology; Physics [physics]; Physics [physics]; Biological Physics [physics.bio-ph]

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⟩