ArticleCommunications biology2020
Collective exchange processes reveal an active site proton cage in bacteriorhodopsin.
Article in Communications biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 20 citations in OpenAlex.
- Revealing the glutamate switch: Insights into proton translocation in plant HBiophysical journal · 2025Article
- Ultrafast Magic Angle Spinning Solid-State NMR Spectroscopy: Advances in Methodology and Applications.Chemical reviews · 2023Review
- QuasAr Odyssey: the origin of fluorescence and its voltage sensitivity in microbial rhodopsins.Nature communications · 2022Article
- Review
- Robust Photoelectric Biomolecular Switch at a Microcavity-Supported Lipid Bilayer.ACS applied materials & interfaces · 2021Article
- MAS NMR detection of hydrogen bonds for protein secondary structure characterization.Journal of biomolecular NMR · 2020Article
Corrections and comments
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Authors and funding
6 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proton translocation across membranes is vital to all kingdoms of life. Mechanistically, it relies on characteristic proton flows and modifications of hydrogen bonding patterns, termed protonation dynamics, which can be directly observed by fast magic angle spinning (MAS) NMR. Here, we demonstrate that reversible proton displacement in the active site of bacteriorhodopsin already takes place in its equilibrated dark-state, providing new information on the underlying hydrogen exchange processes. In particular, MAS NMR reveals proton exchange at D85 and the retinal Schiff base, suggesting a tautomeric equilibrium and thus partial ionization of D85. We provide evidence for a proton cage and detect a preformed proton path between D85 and the proton shuttle R82. The protons at D96 and D85 exchange with water, in line with ab initio molecular dynamics simulations. We propose that retinal isomerization makes the observed proton exchange processes irreversible and delivers a proton towards the extracellular release site.
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Registered trials
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