ArticleStructure (London, England : 1993)2013
Deprotonation of D96 in bacteriorhodopsin opens the proton uptake pathway.
Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Time-resolved x-ray solution scattering from detergent solubilized visual rhodopsin.Biophysical journal · 2026Article
- Conformational Flexibility of Transmembrane Helices: How it Works and Where it Matters.Chemical reviews · 2026Review
- Revealing the glutamate switch: Insights into proton translocation in plant HBiophysical journal · 2025Article
- Rhodopsin from Haloquadratum walsbyi is a light-driven magnesium transporter.Nature communications · 2025Article
- Long-Time Scale Simulations Reveal Key Dynamics That Drive the Onset of the N State in the Proteorhodopsin Photocycle.The journal of physical chemistry. B · 2024Article
- Transient water wires mediate selective proton transport in designed channel proteins.Nature chemistry · 2023Article
- Potassium-selective channelrhodopsins.Biophysics and physicobiology · 2023Article
- Archaeal Lipids Regulating the Trimeric Structure Dynamics of Bacteriorhodopsin for Efficient Proton Release and Uptake.International journal of molecular sciences · 2022Article
- Dynamic Coupling of Tyrosine 185 with the Bacteriorhodopsin Photocycle, as Revealed by Chemical Shifts, Assisted AF-QM/MM Calculations and Molecular Dynamic Simulations.International journal of molecular sciences · 2021Article
- Cryo-EM structure and dynamics of the green-light absorbing proteorhodopsin.Nature communications · 2021Article
- Multiscale Simulations of Biological Membranes: The Challenge To Understand Biological Phenomena in a Living Substance.Chemical reviews · 2019Article
- Allosteric Effects of the Proton Donor on the Microbial Proton Pump Proteorhodopsin.Biophysical journal · 2018Article
- Bacteriorhodopsin-like channelrhodopsins: Alternative mechanism for control of cation conductance.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Stable closure of the cytoplasmic half-channel is required for efficient proton transport at physiological membrane potentials in the bacteriorhodopsin catalytic cycle.Biochemistry · 2014Article
- Crystal structure of Escherichia coli-expressed Haloarcula marismortui bacteriorhodopsin I in the trimeric form.PloS one · 2014Article
- Structural insights into the proton pumping by unusual proteorhodopsin from nonmarine bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Photocycle of Exiguobacterium sibiricum rhodopsin characterized by low-temperature trapping in the IR and time-resolved studies in the visible.The journal of physical chemistry. B · 2013Article
- Schiff base switch II precedes the retinal thermal isomerization in the photocycle of bacteriorhodopsin.PloS one · 2013Article
- Microcompartments and protein machines in prokaryotes.Journal of molecular microbiology and biotechnology · 2013Review
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7 authors.
Funding
Abstract
Despite extensive investigation, the precise mechanism controlling the opening of the cytoplasmic proton uptake pathway in bacteriorhodopsin (bR) has remained a mystery. From an analysis of the X-ray structure of the D96G/F171C/F219L triple mutant of bR and 60 independent molecular dynamics simulations of bR photointermediates, we report that the deprotonation of D96, a key residue in proton transfer reactions, serves two roles that occur sequentially. First, D96 donates a proton to the Schiff base. Subsequently, the deprotonation of D96 serves to "unlatch" the cytoplasmic side. The latching function of D96 appears to be remarkably robust, functioning to open hydration channels in all photointermediate structures. These results suggest that the protonation state of D96 may be the critical biophysical cue controlling the opening and closing of the cytoplasmic half-channel in bR. We suspect that this protonation-switch mechanism could also be utilized in other proton pumps to minimize backflow and reinforce directionality.
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