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Mutation of a surface residue, lysine-129, reverses the order of proton release and uptake in bacteriorhodopsin; guanidine hydrochloride restores it

Author

Rajni Govindjee

Thomas G. Ebrey

1941 -

Published in: Biophysical Journal

Date of publication: February 1, 1997

Language: English

Bibliographic databases:

Cites articles 37

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Authors

May 1, 1975

Flash photometric experiments on the photochemical cycle of bacteriorhodopsin
November 1, 1979

Chromophore equilibria in bacteriorhodopsin
September 1, 1979

Effect of acid pH on the absorption spectra and photoreactions of bacteriorhodopsin
September 1, 1982

Acid-base equilibrium of the Schiff base in bacteriorhodopsin.
December 1, 1989

Isolation of a gene that encodes a new retinal protein, archaerhodopsin, from Halobacterium sp. aus-1
September 1, 1990

Quantum efficiency of the photochemical cycle of bacteriorhodopsin

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June 1, 1990

Transmembrane protein structure: spin labeling of bacteriorhodopsin mutants
February 1, 1990

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
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
December 1, 1990

Bacteriorhodopsin in ice. Accelerated proton transfer from the purple membrane surface
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

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December 1, 1991

Australian Halobacteria and their retinal-protein ion pumps
April 1, 1991

Archaerhodopsin-2, from Halobacterium sp. aus-2 further reveals essential amino acid residues for light-driven proton pumps
April 1, 1992

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

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

Surface-bound optical probes monitor protein translocation and surface potential changes during the bacteriorhodopsin photocycle
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
February 1, 1993

Two light-transducing membrane proteins: bacteriorhodopsin and the mammalian rhodopsin
October 1, 1993

Effect of the arginine-82 to alanine mutation in bacteriorhodopsin on dark adaptation, proton release, and the photochemical cycle.
December 1, 1993

Proton translocation mechanism and energetics in the light-driven pump bacteriorhodopsin
September 1, 1993

Relationship of proton uptake on the cytoplasmic surface and reisomerization of the retinal in the bacteriorhodopsin photocycle: an attempt to understand the complex kinetics of the pH changes and the N and O intermediates
September 1, 1993

pH dependence of light-induced proton release by bacteriorhodopsin
May 1, 1994

Environmental effects on the protonation states of active site residues in bacteriorhodopsin
January 1, 1994

Surface charge of bacteriorhodopsin detected with covalently bound pH indicators at selected extracellular and cytoplasmic sites
November 1, 1994

Covalently bound pH-indicator dyes at selected extracellular or cytoplasmic sites in bacteriorhodopsin. 2. Rotational orientation of helices D and E and kinetic correlation between M formation and proton release in bacteriorhodopsin micelles
March 1, 1994

Molecular dynamics study of bacteriorhodopsin and artificial pigments
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pH dependence of the absorption spectra and photochemical transformations of the archaerhodopsins
April 1, 1995

Chemical reconstitution of a chloride pump inactivated by a single point mutation
July 1, 1995

The two pKa's of aspartate-85 and control of thermal isomerization and proton release in the arginine-82 to lysine mutant of bacteriorhodopsin

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November 1, 1995

Glutamic acid 204 is the terminal proton release group at the extracellular surface of bacteriorhodopsin,Glutamic Acid 204 is the Terminal Proton Release Group at the Extracellular Surface of Bacteriorhodopsin
April 1, 1995

Effects of substitution of tyrosine 57 with asparagine and phenylalanine on the properties of bacteriorhodopsin

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