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

Protein-bound water as the determinant of asymmetric functional conversion between light-driven proton and chloride pumps.

Biochemistry - 12 Jun 2012

Muroda Kosuke, Nakashima Keisuke, Shibata Mikihiro, Demura Makoto, Kandori Hideki

Abstract excerpt

Bacteriorhodopsin (BR) and halorhodopsin (HR) are light-driven outward proton and inward chloride pumps, respectively. They have similar protein architecture, being composed of seven-transmembrane helices that bind an all-trans-retinal. BR can be converted into a chloride pump by a single amino acid replacement at position 85, suggesting that BR and HR share a common transport mechanism, and the ionic specificity...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Substitution
Share to Bacteriorhodopsins

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

Share to Chlorides

Share to Gene Expression Regulation, Bacterial

Share to Proton Pumps

Share to Spectroscopy, Fourier Transform Infrared

Source

Identifiers

PMID: 22583333
DOI: 10.1021/bi300485r

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

Protein-bound water as the determinant of asymmetric functional conversion between light-driven proton and chloride pumps.PMID 22583333Read ↗

The crystal structures of a chloride-pumping microbial rhodopsin and its proton-pumping mutant illuminate proton transfer determinants.Semantic proximity Read ↗

Halide binding by the D212N mutant of Bacteriorhodopsin affects hydrogen bonding of water in the active site.Semantic proximity Read ↗

FTIR studies of internal water molecules in the Schiff base region of bacteriorhodopsin.Semantic proximity Read ↗

O to bR transition in bacteriorhodopsin occurs through a proton hole mechanism.Semantic proximity Read ↗

Structure of an Inward Proton-Transporting Anabaena Sensory Rhodopsin Mutant: Mechanistic Insights.Semantic proximity Read ↗

The Schiff base counterion of bacteriorhodopsin is protonated in sensory rhodopsin I: spectroscopic and functional characterization of the mutated proteins D76N and D76A.Semantic proximity Read ↗

Water-containing hydrogen-bonding network in the active center of channelrhodopsin.Semantic proximity Read ↗

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

Electrostatic interactions and hydrogen bond dynamics in chloride pumping by halorhodopsin.Semantic proximity Read ↗

Water and peptide backbone structure in the active center of bovine rhodopsin.Semantic proximity Read ↗

Spectral Tuning Mechanism of Primate Blue-sensitive Visual Pigment Elucidated by FTIR Spectroscopy.Semantic proximity Read ↗

Trp86 --> Phe replacement in bacteriorhodopsin affects a water molecule near Asp85 and light adaptation.Semantic proximity Read ↗

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