ArticleNature communications2024
Retinal photoisomerization versus counterion protonation in light and dark-adapted bacteriorhodopsin and its primary photoproduct.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- Natural and engineered charge-transfer and diradical state mixing and retinal chromophore dynamics.Physical chemistry chemical physics : PCCP · 2026Review
- Active pixel power control for crosstalk-free all-optical neural interrogation.Nature communications · 2026Article
- Consistent and Generalizable Effective Model Hamiltonian Framework for Studying Nonadiabatic Dynamics in the Condensed Phase.Journal of chemical theory and computation · 2025Review
- A Multiscale Simulation Framework for Elucidating Photochemical Structure-Activity Relationships of Photoswitchable Ligands in Complex Biomolecular Environments.Journal of chemical information and modeling · 2025Article
- Structural and spectroscopic basis of excitation energy transfer in microbial rhodopsins binding xanthophylls.Chemical science · 2025Article
- Multistep 11-Journal of the American Chemical Society · 2025Article
- Retinal to Retinal Energy Transfer in a Bistable Microbial Rhodopsin Dimer.Journal of the American Chemical Society · 2025Article
- A Detailed View on the (Re)isomerization Dynamics in Microbial Rhodopsins Using Complementary Near-UV and IR Readouts.Angewandte Chemie (International ed. in English) · 2025Article
- Reversible Photochromic Reactions of Bacteriorhodopsin fromMolecules (Basel, Switzerland) · 2024Article
- Retinal photoisomerization versus counterion protonation in light and dark-adapted bacteriorhodopsin and its primary photoproduct.Nature communications · 2024Article
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Authors and funding
7 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Discovered over 50 years ago, bacteriorhodopsin is the first recognized and most widely studied microbial retinal protein. Serving as a light-activated proton pump, it represents the archetypal ion-pumping system. Here we compare the photochemical dynamics of bacteriorhodopsin light and dark-adapted forms with that of the first metastable photocycle intermediate known as "K". We observe that following thermal double isomerization of retinal in the dark from bio-active all-trans 15-anti to 13-cis, 15-syn, photochemistry proceeds even faster than the ~0.5 ps decay of the former, exhibiting ballistic wave packet curve crossing to the ground state. In contrast, photoexcitation of K containing a 13-cis, 15-anti chromophore leads to markedly multi-exponential excited state decay including much slower stages. QM/MM calculations, aimed to interpret these results, highlight the crucial role of protonation, showing that the classic quadrupole counterion model poorly reproduces spectral data and dynamics. Single protonation of ASP212 rectifies discrepancies and predicts triple ground state structural heterogeneity aligning with experimental observations. These findings prompt a reevaluation of counter ion protonation in bacteriorhodopsin and contribute to the broader understanding of its photochemical dynamics.
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