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Article

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

Biochimica et biophysica acta - 30 Jan 1992

Lanyi J K, Tittor J, Váró G, Krippahl G, Oesterhelt D

Abstract excerpt

The consequences of replacing Asp-85 with glutamate in bacteriorhodopsin, as expressed in Halobacterium sp. GRB, were investigated. Similarly to the in vitro mutated and in Escherichia coli expressed protein, the chromophore was found to exist as a mixture of blue (absorption maximum 615 nm) and red (532 nm) forms, depending on the pH. However, we found two widely separated pKa values (about 5.4 and 10.4 without...

Topics

Aspartic Acid
Bacteriorhodopsins
Biological Transport
Escherichia coli
Glutamates
Glutamic Acid
Halobacterium
Hydrogen-Ion Concentration
Kinetics
Mutation
Photochemistry

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protons

Spectrophotometry, Ultraviolet

X-Ray Diffraction

Source

Identifiers

PMID: 1346749

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1346749-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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Influence of the size and protonation state of acidic residue 85 on the absorption spectrum and photoreaction of the bacteriorhodopsin chromophore.PMID 1346749Read ↗

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