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Creators/Authors contains: "Zhang, Wenkai"

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  1. ; ; ; ; ; ; ; (, The Journal of Physical Chemistry C)
    Free, publicly-accessible full text available November 13, 2025
  2. ; (, IEEE)
    Full Text Available 
  3. ; ; ; ; ; ; ; ; ; ; et al (, Proceedings of the National Academy of Sciences)
    Significance Light-driven rhodopsin proteins pump ions across cell membranes. They have applications in optogenetics and can potentially be used to develop solar energy–harvesting devices. A detailed understanding of rhodopsin dynamics and functions may therefore assist research in medicine, health, and clean energy. This time-resolved crystallography study carried out with X-ray free-electron lasers reveals detailed dynamics of chloride ion–pumping rhodopsin (ClR) within 100 ps of light activation. It shows the dissociation of Cl−from the Schiff base binding site upon light-triggered retinal isomerization. This Cl−dissociation is followed by diffusion toward the intracellular direction. The results hint at a common ion-pumping mechanism across rhodopsin families. 
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