Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Intramolecular proton transfer in channelrhodopsins.

Biophysical journal - 19 Feb 2013

Sineshchekov Oleg A, Govorunova Elena G, Wang Jihong, Li Hai, Spudich John L

Abstract excerpt

Channelrhodopsins serve as photoreceptors that control the motility behavior of green flagellate algae and act as light-gated ion channels when heterologously expressed in animal cells. Here, we report direct measurements of proton transfer from the retinylidene Schiff base in several channelrhodopsin variants expressed in HEK293 cells. A fast outward-directed current precedes the passive channel current that has...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Archaea
Share to Aspartic Acid
Share to Chlorophyta

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Ion Channel Gating

Share to Ion Transport

Share to Membrane Potentials

Share to Protons

Share to Retinoids

Source

Open in PubMed Open full text

Identifiers

PMID: 23442959
DOI: 10.1016/j.bpj.2013.01.002
PMCID: PMC3576534

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Intramolecular proton transfer in channelrhodopsins.PMID 23442959Read ↗

Aspartate-histidine interaction in the retinal schiff base counterion of the light-driven proton pump of Exiguobacterium sibiricum.Semantic proximity Read ↗

Proton transfer reactions in the red light-activatable channelrhodopsin variant ReaChR and their relevance for its function.Semantic proximity Read ↗

Conductance mechanisms of rapidly desensitizing cation channelrhodopsins from cryptophyte algaeSemantic proximity Read ↗

Voltage- and pH-dependent changes in vectoriality of photocurrents mediated by wild-type and mutant proteorhodopsins upon expression in Xenopus oocytes.Semantic proximity Read ↗

A redirected proton pathway in the bacteriorhodopsin mutant Tyr-57-->Asp. Evidence for proton translocation without Schiff base deprotonation.Semantic proximity Read ↗

The retinal Schiff base-counterion complex of bacteriorhodopsin: changed geometry during the photocycle is a cause of proton transfer to aspartate 85.Semantic proximity Read ↗

Electrostatic Control of Photoisomerization in Channelrhodopsin 2.Semantic proximity Read ↗

Converting a light-driven proton pump into a light-gated proton channel.Semantic proximity Read ↗

Internal Proton Transfer in the Activation of Heliorhodopsin.Semantic proximity Read ↗

Structural guidance of the photocycle of channelrhodopsin-2 by an interhelical hydrogen bond.Semantic proximity Read ↗

Gloeobacter rhodopsin, limitation of proton pumping at high electrochemical load.Semantic proximity Read ↗

Proton transport by proteorhodopsin requires that the retinal Schiff base counterion Asp-97 be anionic.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.