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

Static and time-resolved absorption spectroscopy of the bacteriorhodopsin mutant Tyr-185-->Phe: evidence for an equilibrium between bR570 and an O-like species.

Biochemistry - 9 Mar 1993

Sonar S, Krebs M P, Khorana H G, Rothschild K J

Abstract excerpt

The light-dark adaptation, photocycle kinetics, and acid-induced blue formation of the bacteriorhodopsin (bR) mutant Tyr-185-->Phe (Y185F) expressed in Halobacterium halobium have been investigated by both static and time-resolved visible absorption spectroscopy. Evidence is presented that a pH-dependent equilibrium exists between a bR570-like form (bRY185F570) and a red-shifted species in the light-adapted form...

Read the complete abstract on PubMed

Topics

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

Share to Darkness
Share to Hydrogen-Ion Concentration

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

Share to Mutation

Share to Osmolar Concentration

Share to Phenylalanine

Share to Spectrophotometry, Ultraviolet

Share to Tyrosine

Source

Identifiers

PMID: 8443169
DOI: 10.1021/bi00060a019

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

Static and time-resolved absorption spectroscopy of the bacteriorhodopsin mutant Tyr-185-->Phe: evidence for an equilibrium between bR570 and an O-like species.PMID 8443169Read ↗

FTIR difference spectroscopy of the bacteriorhodopsin mutant Tyr-185-->Phe: detection of a stable O-like species and characterization of its photocycle at low temperature.Semantic proximity Read ↗

Fourier transform Raman spectroscopy of the bacteriorhodopsin mutant Tyr-185-->Phe: formation of a stable O-like species during light adaptation and detection of its transient N-like photoproduct.Semantic proximity Read ↗

Ultraviolet-visible transient spectroscopy of bacteriorhodopsin mutants. Evidence for two forms of tyrosine-185----phenylalanine.Semantic proximity Read ↗

Effect of genetic modification of tyrosine-185 on the proton pump and the blue-to-purple transition in bacteriorhodopsin.Semantic proximity Read ↗

On the heterogeneity of the M population in the photocycle of bacteriorhodopsin.Semantic proximity Read ↗

Late events in the photocycle of bacteriorhodopsin mutant L93A.Semantic proximity Read ↗

High-throughput screening of bacteriorhodopsin mutants in whole cell pastes.Semantic proximity Read ↗

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

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

Crystal structures of bR(D85S) favor a model of bacteriorhodopsin as a hydroxyl-ion pump.Semantic proximity Read ↗

Voltage dependence of proton pumping by bacteriorhodopsin mutants with altered lifetime of the M intermediate.Semantic proximity Read ↗

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