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

Author

Rajni Govindjee

Thomas G. Ebrey

1941 -

Published in: Biophysical Journal

Date of publication: August 1, 1991

Language: English

Bibliographic databases:

Cites articles 42

Date

Title

Authors

February 1966

Hydrogen ion buffers for biological research,Hydrogen Ion Buffers for Biological Research*
July 1, 1968

Studies of the location of tyrosyl and tryptophyl residues in proteins. I. Solvent perturbation data of model compounds
September 1, 1968

Investigation of the Near and Far Ultraviolet Denaturation Difference Spectra of Dehydrogenases
April 1, 1969

Changes in Ultraviolet Absorption Produced by Alteration of Protein Conformation
January 1, 1974

The Structure and Spectra of the Chromophore of the Visual Pigments
February 1, 1975

The pH dependence of the hydrolysis of benzoyl-L-arginine ethyl ester in cooled mixed solvents
January 1, 1975

Improved isolation procedures for the purple membrane of Halobacterium halobium,Improved Isolation Procedures for the Purple Membrane of Halobacterium Halobium
July 1, 1976

Retinal has a highly dipolar vertically excited singlet state: implications for vision
December 1, 1976

Photochemical reaction of bacteriorhodopsin
September 1, 1978

Flash-induced volume changes of bacteriorhodopsin-containing membrane fragments and their relationship to proton movements and absorbance transients
April 1, 1979

Kinetic interaction between aromatic residues and the retinal chromophore of bacteriorhodopsin during the photocycle
April 1, 1979

The structural basis of the functioning of bacteriorhodopsin: an overview,The structural basis of the functioning of bacteriorhodopsin: An overview
December 1, 1979

Interpretations of the effects of pH on the spectra of purple membrane
February 1, 1981

Environmental effects on formation and photoreaction of the M412 photoproduct of bacteriorhodopsin: implications for the mechanism of proton pumping
September 1, 1982

Acid-base equilibrium of the Schiff base in bacteriorhodopsin.
December 1, 1982

Restriction of motion of protein side chains during the photocycle of bacteriorhodopsin
September 1, 1983

A spectrofluorometric study of the environment of tryptophans in bacteriorhodopsin.
November 1, 1984

On the protein (tyrosine)-chromophore (protonated Schiff base) coupling in bacteriorhodopsin
November 1, 1984

A correlation between proton pumping and the bacteriorhodopsin photocycle

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December 1, 1984

Selective nitration of tyrosines-26 and -64 in bacteriorhodopsin with tetranitromethane
October 1, 1984

Testing kinetic models for the bacteriorhodopsin photocycle--II. Inclusion of an O to M backreaction
January 1, 1986

Evidence for a tyrosine protonation change during the primary phototransition of bacteriorhodopsin at low temperature
February 1, 1986

Chromophore/protein interaction in bacterial sensory rhodopsin and bacteriorhodopsin
August 1, 1987

Bacteriorhodopsin mutants containing single tyrosine to phenylalanine substitutions are all active in proton translocation
October 1, 1987

Tyrosine and carboxyl protonation changes in the bacteriorhodopsin photocycle. 1. M412 and L550 intermediates
September 1, 1988

Independent photocycles of the spectrally distinct forms of bacteriorhodopsin

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May 1, 1988

Direct observation of the femtosecond excited-state cis-trans isomerization in bacteriorhodopsin

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April 1, 1989

Replacement of aspartic acid-96 by asparagine in bacteriorhodopsin slows both the decay of the M intermediate and the associated proton movement
December 1, 1989

Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsin
June 1, 1989

Aspartic acids 96 and 85 play a central role in the function of bacteriorhodopsin as a proton pump

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August 1, 1989

Bacteriorhodopsin mutants of Halobacterium sp. GRB. II. Characterization of mutants
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Conserved amino acids in F-helix of bacteriorhodopsin form part of a retinal binding pocket

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