Dynamics and mechanism of dimer dissociation of photoreceptor UVR8

Xiankun Li, Zheyun Liu, Haisheng Ren, Mainak Kundu, Frank W. Zhong, Lijuan Wang, Jiali Gao, Dongping Zhong

Research output: Contribution to journalArticlepeer-review

11 Scopus citations


Photoreceptors are a class of light-sensing proteins with critical biological functions. UVR8 is the only identified UV photoreceptor in plants and its dimer dissociation upon UV sensing activates UV-protective processes. However, the dissociation mechanism is still poorly understood. Here, by integrating extensive mutations, ultrafast spectroscopy, and computational calculations, we find that the funneled excitation energy in the interfacial tryptophan (Trp) pyramid center drives a directional Trp-Trp charge separation in 80 ps and produces a critical transient Trp anion, enabling its ultrafast charge neutralization with a nearby positive arginine residue in 17 ps to destroy a key salt bridge. A domino effect is then triggered to unzip the strong interfacial interactions, which is facilitated through flooding the interface by channel and interfacial water molecules. These detailed dynamics reveal a unique molecular mechanism of UV-induced dimer monomerization.

Original languageEnglish (US)
Article number93
JournalNature communications
Issue number1
StatePublished - Dec 2022

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