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PMID: 6268211 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Changes in the protonation state of bacterio-opsin during reconstitution of bacteriorhodopsin.

Biophysical journal ·Vol. 31 ·No. 1 ·1980-07-00 ·Pages 139-45

Fischer UC, Oesterhelt D

Abstract

Protonation changes of the protein occur during the reconstitution of bacteriorhodopsin from bacterio-opsin and all-trans retinal in the purple membrane of Halobacterium halobium. The protonation changes are conveniently determined from measures of the pH changes after photoisomerisation of 9-cis retinal in apomembrane preparations, which induces the reconstitution. In addition, to the omega-amino group of the lysine which is involved in the condensation of retinal and bacterio-opsin, the dissociation equilibria of at least two other amino acid residues are changed during the reconstitution. The results are consistent with a proposed model of chromophore structure in which an interaction of the Schiff's base occurs with two protonable amino acid residues.

MeSH Terms

Apoproteins Bacteriorhodopsins/radiation effects Carotenoids/radiation effects Chemical Phenomena Chemistry Diterpenes Halobacterium Hydrogen-Ion Concentration Isomerism Light Models, Chemical Protons Retinaldehyde/radiation effects Ultraviolet Rays Vitamin A/analogs & derivatives

Chemicals

Apoproteins Diterpenes Protons Vitamin A Carotenoids 13-cis-retinal 9-cis-retinal Bacteriorhodopsins bacterio-opsin Retinaldehyde

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Fischer U C

Oesterhelt D

References (12)

12 references, click to expand

Light-dependent reaction of bacteriorhodopsin with hydroxylamine in cell suspensions of Halobacterium halobium: demonstration of an apo-membrane.
FEBS Lett. 1974 Aug 30;44(3):257-61 PMID: 4414481
Visual-pigment spectra: implications of the protonation of the retinal Schiff base.
Biochemistry. 1976 Oct 19;15(21):4593-9 PMID: 974079
Anion-induced wavelength regulation of absorption maxima of Schiff bases of retinal.
Biochemistry. 1972 Feb 29;11(5):848-55 PMID: 5059891
Reversible photolysis of the purple complex in the purple membrane of Halobacterium halobium.
Eur J Biochem. 1973 Aug 17;37(2):316-26 PMID: 4745733
Tunable laser resonance raman spectroscopy of bacteriorhodopsin.
Proc Natl Acad Sci U S A. 1974 Nov;71(11):4462-6 PMID: 4530995
Chromophore equilibria in bacteriorhodopsin.
Biophys J. 1979 Nov;28(2):211-30 PMID: 122264
Photoisomerization, energy storage, and charge separation: a model for light energy transduction in visual pigments and bacteriorhodopsin.
Proc Natl Acad Sci U S A. 1979 Jun;76(6):2503-7 PMID: 288039
Rhodopsin-like protein from the purple membrane of Halobacterium halobium.
Nat New Biol. 1971 Sep 29;233(39):149-52 PMID: 4940442
Studies on rhodopsin. IX. pH and the hydrolysis of indicator yellow.
Biochem J. 1955 Jan;59(1):128-34 PMID: 14351152
Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane.
Methods Enzymol. 1974;31:667-78 PMID: 4418026
The two faces of the purple membrane. II. Differences in surface charge properties revealed by ferritin binding.
J Mol Biol. 1978 Oct 25;125(2):123-35 PMID: 32399
Studies on the retinal-protein interaction in bacteriorhodopsin.
Eur J Biochem. 1977 Jun 15;76(2):499-511 PMID: 19246

Article Info

Journal

Biophysical journal

Abbr.

Biophys J

ISSN

0006-3495

DOI

10.1016/S0006-3495(80)85045-4

Published

1980-07-00

Pages

139-45

Language

English

Region

United States

NLM ID

0370626

PMCID

PMC1328769

Subset

External Links

PubMed source DOI: 10.1016/S0006-3495(80)85045-4 PMC Full Text View journal details

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Changes in the protonation state of bacterio-opsin during reconstitution of bacteriorhodopsin.

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