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Titration of aspartate-85 in bacteriorhodopsin: what it says about chromophore isomerization and proton release

Author

Rajni Govindjee

Thomas G. Ebrey

1941 -

Published in: Biophysical Journal

Date of publication: January 1, 1996

Language: English

Bibliographic databases:

Cites articles 45

Date

Title

Authors

September 29, 1971

Rhodopsin-like protein from the purple membrane of Halobacterium halobium,Rhodopsin-like Protein from the Purple Membrane of Halobacterium halobium
December 1, 1973

Reversible Dissociation of the Purple Complex in Bacteriorhodopsin and Identification of 13-cis and all-trans-Retinal as its Chromophores
September 1, 1976

Kinetics and stoichiometry of light-induced proton release and uptake from purple membrane fragments, Halobacterium halobium cell envelopes, and phospholipid vesicles containing oriented purple membrane
December 1, 1977

Effect of light-adaptation on the photoreaction of bacteriorhodopsin from Halobacterium halobium
May 1, 1978

Studies of an acid-induced species of purple membrane from Halobacterium halobium
November 1, 1979

Chromophore equilibria in bacteriorhodopsin
August 1, 1979

Kinetic and spectroscopic effects of protein-chromophore electrostatic interactions in bacteriorhodopsin
September 1, 1979

Effect of acid pH on the absorption spectra and photoreactions of bacteriorhodopsin
March 1, 1984

Dark-adapted bacteriorhodopsin contains 13-cis, 15-syn and all-trans, 15-anti retinal Schiff bases
March 1, 1985

The effect of protonation and electrical interactions on the stereochemistry of retinal schiff bases
June 1, 1987

Effect of lipid surface charges on the purple-to-blue transition of bacteriorhodopsin
September 1, 1988

Chromophore structure in bacteriorhodopsin's N intermediate: implications for the proton-pumping mechanism
November 1, 1988

Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212
December 1, 1989

Photoreactions of bacteriorhodopsin at acid pH
August 1, 1989

Structure-function studies on bacteriorhodopsin. X. Individual substitutions of arginine residues by glutamine affect chromophore formation, photocycle, and proton translocation
May 1, 1990

Light-induced currents from oriented purple membrane: I. Correlation of the microsecond component (B2) with the L-M photocycle transition
December 1, 1990

Purple membrane: surface charge density and the multiple effect of pH and cations
February 1, 1990

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
August 1, 1991

Redshift of the purple membrane absorption band and the deprotonation of tyrosine residues at high pH: Origin of the parallel photocycles of trans-bacteriorhodopsin

,
August 1, 1991

Correlation between absorption maxima and thermal isomerization rates in bacteriorhodopsin
January 1, 1991

Binding of a single divalent cation directly correlates with the blue-to-purple transition in bacteriorhodopsin
July 1, 1991

Effect of pH buffer molecules on the light-induced currents from oriented purple membrane
January 1, 1991

From femtoseconds to biology: mechanism of bacteriorhodopsin's light-driven proton pump
August 1, 1991

Replacement of leucine-93 by alanine or threonine slows down the decay of the N and O intermediates in the photocycle of bacteriorhodopsin: implications for proton uptake and 13-cis-retinal----all-trans-retinal reisomerization
November 1, 1992

Proton uptake mechanism of bacteriorhodopsin as determined by time-resolved stroboscopic-FTIR-spectroscopy
April 1, 1992

A unifying concept for ion translocation by retinal proteins
April 1, 1992

FTIR difference spectroscopy of bacteriorhodopsin: toward a molecular model
September 1, 1992

Pathways of proton release in the bacteriorhodopsin photocycle
June 1, 1992

Asp85 is the only internal aspartic acid that gets protonated in the M intermediate and the purple-to-blue transition of bacteriorhodopsin. A solid-state 13C CP-MAS NMR investigation,Asp85 is the only internal aspartic acid that gets protonated in the M intermediate and the purple&#x2010;to&#x2010;blue transition of bacteriorhodopsin A solid&#x2010;state13C CP&#x2010;MAS NMR investigation
March 1, 1992

Electrostatic calculations of the pKa values of ionizable groups in bacteriorhodopsin
September 1, 1992

Rotational resonance NMR study of the active site structure in bacteriorhodopsin: conformation of the Schiff base linkage
August 1, 1993

Protein catalysis of the retinal subpicosecond photoisomerization in the primary process of bacteriorhodopsin photosynthesis.

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