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Article

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.

Proceedings of the National Academy of Sciences of the United States of America - 1 Feb 1990

Otto H, Marti T, Holz M, Mogi T, Stern L J, Engel F, Khorana H G, Heyn M P

Abstract excerpt

Photocycle and flash-induced proton release and uptake were investigated for bacteriorhodopsin mutants in which Asp-85 was replaced by Ala, Asn, or Glu; Asp-212 was replaced by Asn or Glu; Asp-115 was replaced by Ala, Asn, or Glu; Asp-96 was replaced by Ala, Asn, or Glu; and Arg-82 was replaced by Ala or Gln in dimyristoylphosphatidylcholine/3-[(3-cholamidopropyl)dimethylammonio]-1- propanesulfonate micelles at...

Topics

Arginine
Aspartic Acid
Bacteriorhodopsins
Cloning, Molecular
Escherichia coli
Genes, Bacterial
Halobacterium
Kinetics
Mutation
Protons
Schiff Bases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Spectrophotometry

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Identifiers

PMID: 2153966
DOI: 10.1073/pnas.87.3.1018
PMCID: PMC53401

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2153966-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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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.PMID 2153966Read ↗

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

Protonation state of Asp (Glu)-85 regulates the purple-to-blue transition in bacteriorhodopsin mutants Arg-82----Ala and Asp-85----Glu: the blue form is inactive in proton translocation.Semantic proximity Read ↗

Influence of the size and protonation state of acidic residue 85 on the absorption spectrum and photoreaction of the bacteriorhodopsin chromophore.Semantic proximity Read ↗

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

Structure changes upon deprotonation of the proton release group in the bacteriorhodopsin photocycle.Semantic proximity Read ↗

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

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

Critical role of Asp227 in the photocycle of proteorhodopsin.Semantic proximity Read ↗

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

L105K mutant of proteorhodopsin.Semantic proximity Read ↗

Role of Arg-72 of pharaonis Phoborhodopsin (sensory rhodopsin II) on its photochemistry.Semantic proximity Read ↗

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