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Updated: May 29, 2026

A Rhodopsin Transport Assay by High-Content Imaging Analysis
Published on: January 16, 2019
Photoisomerization detected in a fully wavelength-tunable rhodopsin mimic system
Nona Ehyaei1, Courtney Bingham1, Katelyn Silva1
1Department of Chemistry, Michigan State University, East Lansing, MI 48824, USA.
None:
We describe the photoisomerization of the retinylidene protonated Schiff base in human retinol-binding protein II (hCRBPII) and the role of water molecules in this process. We characterize the photoisomerization of the 15-cis/all-trans retinylidene protonated Schiff base in this system using UV-visible spectroscopy and atomic-resolution X-ray crystallography. We further demonstrate a process where the pKa of the protonated Schiff base is substantially altered by light-induced dehydration of the binding pocket, suggesting novel pathways of photoswitching that rely not on isomerization or conformational change of the chromophore but rather on light-induced reorganization of the protein environment.
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