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

Photovoltage evidence that Glu-204 is the intermediate proton donor rather than the terminal proton release group in bacteriorhodopsin.

FEBS letters - 28 Aug 1998

Kalaidzidis I V, Belevich I N, Kaulen A D

Abstract excerpt

Electrogenic events in the E204Q bacteriorhodopsin mutant have been studied. A two-fold decrease in the magnitude of microsecond photovoltage generation coupled to M intermediate formation in the E204Q mutant is shown. This means that deprotonation of E204 is an electrogenic process and its elect...

Topics

Bacteriorhodopsins
Energy Metabolism
Halobacterium salinarum
Hydrogen-Ion Concentration
Mutation
Protons

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 9738477
DOI: 10.1016/s0014-5793(98)00980-6

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9738477-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Photovoltage evidence that Glu-204 is the intermediate proton donor rather than the terminal proton release group in bacteriorhodopsin.PMID 9738477Read ↗

Substitution of amino acids Asp-85, Asp-212, and Arg-82 in bacteriorhodopsin affects the proton release phase of the pump and the pK of the Schiff base.Semantic proximity Read ↗

Membrane potential stabilizes the O intermediate in liposomes containing bacteriorhodopsin.Semantic proximity Read ↗

Proton transport by a bacteriorhodopsin mutant, aspartic acid-85-->asparagine, initiated in the unprotonated Schiff base state.Semantic proximity Read ↗

Formation of the M(N) (M(open)) intermediate in the wild-type bacteriorhodopsin photocycle is accompanied by an absorption spectrum shift to shorter wavelength, like that in the mutant D96N bacteriorhodopsin photocycle.Semantic proximity Read ↗

Photocycle in the M-form in bacteriorhodopsin mutants devoid of primary proton acceptor Asp-85.Semantic proximity Read ↗

Formation of M-Like Intermediates in Proteorhodopsin in Alkali Solutions (pH ≥ ∼8.5) Where the Proton Release Occurs First in Contrast to the Sequence at Lower pH.Semantic proximity Read ↗

Properties of Asp212----Asn bacteriorhodopsin suggest that Asp212 and Asp85 both participate in a counterion and proton acceptor complex near the Schiff base.Semantic 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 ↗

Glutamate-194 to cysteine mutation inhibits fast light-induced proton release in bacteriorhodopsin.Semantic proximity Read ↗

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

Intramolecular proton transfer in channelrhodopsins.Semantic proximity Read ↗

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

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