%0 Journal Article %A Mathes, Tilo %A Heilmann, Monika %A Pandit, Anjali %A Zhu, Jingyi %A Ravensbergen, Janneke %A Kloz, Miroslav %A Fu, Yinan %A Smith, Brian O. %A Christie, John M. %A Jenkins, Gareth I. %A T. M. Kennis, John %D 2015 %T Proton-Coupled Electron Transfer Constitutes the Photoactivation Mechanism of the Plant Photoreceptor UVR8 %U https://acs.figshare.com/articles/journal_contribution/Proton_Coupled_Electron_Transfer_Constitutes_the_Photoactivation_Mechanism_of_the_Plant_Photoreceptor_UVR8/2057460 %R 10.1021/jacs.5b01177.s001 %2 https://acs.figshare.com/ndownloader/files/3635496 %K Plant Photoreceptor UVR 8UVR %K absorption %K UVR 8 %K mechanism %K electron transfer reactions %K monomerization %K tryptophan side chains %K homodimeric UVR 8 %X UVR8 is a novel UV-B photoreceptor that regulates a range of plant responses and is already used as a versatile optogenetic tool. Instead of an exogenous chromophore, UVR8 uniquely employs tryptophan side chains to accomplish UV-B photoreception. UV-B absorption by homodimeric UVR8 induces monomerization and hence signaling, but the underlying photodynamic mechanisms are not known. Here, by using a combination of time-resolved fluorescence and absorption spectroscopy from femto- to microseconds, we provide the first experimental evidence for the UVR8 molecular signaling mechanism. The results indicate that tryptophan residues at the dimer interface engage in photoinduced proton coupled electron transfer reactions that induce monomerization. %I ACS Publications