ArticleBiochemistry2014
Light-driven Na(+) pump from Gillisia limnaea: a high-affinity Na(+) binding site is formed transiently in the photocycle.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 88 citations in OpenAlex.
- The Conformational Switches of a Bacterial Light-Driven Sodium Pump Characterized by Time-Resolved Resonance Raman Spectroscopy.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026Article
- Mechanistic insights into NaThe Journal of biological chemistry · 2026Article
- Light-Driven Sodium Pump as a Potential Tool for the Control of Seizures in Epilepsy.Molecular neurobiology · 2024Article
- A subgroup of light-driven sodium pumps with an additional Schiff base counterion.Nature communications · 2024Article
- NaMolecules (Basel, Switzerland) · 2023Review
- KInternational journal of molecular sciences · 2023Article
- Structural and functional consequences of the H180A mutation of the light-driven sodium pump KR2.Biophysical journal · 2023Article
- Potassium-selective channelrhodopsins.Biophysics and physicobiology · 2023Article
- Convergent evolution of animal and microbial rhodopsins.RSC advances · 2023Review
- Reisomerization of retinal represents a molecular switch mediating NaThe Journal of biological chemistry · 2022Article
- Application of direct electrometry in studies of microbial rhodopsins reconstituted in proteoliposomes.Biophysical reviews · 2022Review
- Microbial Rhodopsins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Probing the photointermediates of light-driven sodium ion pump KR2 by DNP-enhanced solid-state NMR.Science advances · 2021Article
- Article
- Diversity, Mechanism, and Optogenetic Application of Light-Driven Ion Pump Rhodopsins.Advances in experimental medicine and biology · 2021Review
- Article
- Molecular mechanism of light-driven sodium pumping.Nature communications · 2020Article
- Engineered Passive Potassium Conductance in the KR2 Sodium Pump.Biophysical journal · 2019Article
- Electrical properties, substrate specificity and optogenetic potential of the engineered light-driven sodium pump eKR2.Scientific reports · 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
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
A group of microbial retinal proteins most closely related to the proton pump xanthorhodopsin has a novel sequence motif and a novel function. Instead of, or in addition to, proton transport, they perform light-driven sodium ion transport, as reported for one representative of this group (KR2) from Krokinobacter. In this paper, we examine a similar protein, GLR from Gillisia limnaea, expressed in Escherichia coli, which shares some properties with KR2 but transports only Na(+). The absorption spectrum of GLR is insensitive to Na(+) at concentrations of ≤3 M. However, very low concentrations of Na(+) cause profound differences in the decay and rise time of photocycle intermediates, consistent with a switch from a "Na(+)-independent" to a "Na(+)-dependent" photocycle (or photocycle branch) at ∼60 μM Na(+). The rates of photocycle steps in the latter, but not the former, are linearly dependent on Na(+) concentration. This suggests that a high-affinity Na(+) binding site is created transiently after photoexcitation, and entry of Na(+) from the bulk to this site redirects the course of events in the remainder of the cycle. A greater concentration of Na(+) is needed for switching the reaction path at lower pH. The data suggest therefore competition between H(+) and Na(+) to determine the two alternative pathways. The idea that a Na(+) binding site can be created at the Schiff base counterion is supported by the finding that upon perturbation of this region in the D251E mutant, Na(+) binds without photoexcitation. Binding of Na(+) to the mutant shifts the chromophore maximum to the red like that of H(+), which occurs in the photocycle of the wild type.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.