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

Coupling between the retinal thermal isomerization and the Glu194 residue of bacteriorhodopsin.

Photochemistry and photobiology - 1 Jan 2000

Lazarova Tzvetana, Querol Enric, Padrós Esteve

Abstract excerpt

Glu194 is a residue located at the end of F helix on the extracellular side of the light-induced proton pump bacteriorhodopsin (BR). Currently, it is well recognized that Glu194 and Glu204 residues, along with water clusters, constitute the proton release group of BR. Here we report that the replacement of Glu194 for Gln affects not only the photocycle of the protein but also has tremendous effect on the...

Read the complete abstract on PubMed

Topics

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

Share to Adaptation, Biological
Share to Bacteriorhodopsins
Share to Glutamic Acid

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

Share to Halobacterium salinarum

Share to Isomerism

Share to Sensory Receptor Cells

Share to Spectrophotometry

Source

Identifiers

PMID: 19267876
DOI: 10.1111/j.1751-1097.2008.00534.x

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

Coupling between the retinal thermal isomerization and the Glu194 residue of bacteriorhodopsin.PMID 19267876Read ↗

Coupling photoisomerization of retinal to directional transport in bacteriorhodopsin.Semantic proximity Read ↗

Schiff Base Proton Acceptor Assists Photoisomerization of Retinal Chromophores in Bacteriorhodopsin.Semantic proximity Read ↗

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

A color-determining amino acid residue of proteorhodopsin.Semantic proximity Read ↗

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

Contribution of glutamic acid in the conserved E/DRY triad to the functional properties of rhodopsin.Semantic proximity Read ↗

Effects of mutations of Lys41 and Asp102 of bacteriorhodopsin.Semantic proximity Read ↗

Photocycle of Exiguobacterium sibiricum rhodopsin characterized by low-temperature trapping in the IR and time-resolved studies in the visible.Semantic proximity Read ↗

Tuning the primary reaction of channelrhodopsin-2 by imidazole, pH, and site-specific mutations.Semantic proximity Read ↗

The role of water in the extracellular half channel of bacteriorhodopsin.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 ↗

Redox potentials of the oriented film of the wild-type, the E194Q-, E204Q- and D96N-mutated bacteriorhodopsins.Semantic proximity Read ↗

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