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Article

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

The Journal of biological chemistry - 25 Jun 1991

Needleman R, Chang M, Ni B, Váró G, Fornés J, White S H, Lanyi J K

Abstract excerpt

The gene coding for bacteriorhodopsin was modified in vitro to replace Asp212 with asparagine and expressed in Halobacterium halobium. X-ray diffraction measurements showed that the major lattice dimension of purple membrane containing the mutated bacteriorhodopsin was the same as wild type. At pH greater than 7, the Asp212----Asn chromophore was blue (absorption maximum at 585 nm) and exhibited a photocycle...

Topics

Asparagine
Aspartic Acid
Bacteriorhodopsins
Genes, Bacterial
Halobacterium
Hydrogen-Ion Concentration
Mutation
Plasmids
Protons
Schiff Bases
Spectrum Analysis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

X-Ray Diffraction

Source

Identifiers

PMID: 1646807

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1646807-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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Properties of Asp212----Asn bacteriorhodopsin suggest that Asp212 and Asp85 both participate in a counterion and proton acceptor complex near the Schiff base.PMID 1646807Read ↗

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 ↗

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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 ↗

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