Inventaire - your friends and communities are your best library

Effects of individual genetic substitutions of arginine residues on the deprotonation and reprotonation kinetics of the Schiff base during the bacteriorhodopsin photocycle

Published in: Biophysical Journal

Date of publication: July 1, 1991

Language: English

Bibliographic databases:

Cites articles 29

Date

Title

Authors

1974

Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane
September 1, 1975

Bacteriorhodopsin: a light-driven proton pump in Halobacterium Halobium
January 1, 1975

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

Primary photochemical processes in bacteriorhodopsin
June 1, 1976

Energetics and chronology of phototransients in the light response of the purple membrane of Halobacterium halobium
March 1, 1978

Illumination-dependent changes in the intrinsic fluorescence of bacteriorhodopsin
April 1, 1979

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

Amino acid sequence of bacteriorhodopsin
August 1, 1980

Isotope effects and activation parameters for chemically modified bacteriorhodopsin

,
June 1982

Bacteriorhodopsin and related pigments of halobacteria
April 1, 1984

Specific amino acid substitutions in bacterioopsin: Replacement of a restriction fragment in the structural gene by synthetic DNA fragments containing altered codons
November 1, 1984

On the protein (tyrosine)-chromophore (protonated Schiff base) coupling in bacteriorhodopsin
January 1, 1985

Light-driven protonation changes of internal aspartic acids of bacteriorhodopsin: an investigation by static and time-resolved infrared difference spectroscopy using [4-13C]aspartic acid labeled purple membrane
January 1, 1986

Methods for mutagenesis of the bacterioopsin gene.
July 1, 1987

Structure-function studies on bacteriorhodopsin. V. Effects of amino acid substitutions in the putative helix F.
September 1, 1988

Effects of amino acid substitutions in the F helix of bacteriorhodopsin. Low temperature ultraviolet/visible difference spectroscopy
June 1, 1988

Bacteriorhodopsin, a membrane protein that uses light to translocate protons
November 1, 1988

Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212
May 1, 1988

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

,
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

Substitution of amino acids in helix F of bacteriorhodopsin: effects on the photochemical cycle
December 1, 1989

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

Structure-function studies on bacteriorhodopsin. X. Individual substitutions of arginine residues by glutamine affect chromophore formation, photocycle, and proton translocation
July 1, 1989

Role of aspartate-96 in proton translocation by bacteriorhodopsin.
June 20, 1990

Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
June 1, 1990

Effect of genetic modification of tyrosine-185 on the proton pump and the blue-to-purple transition in bacteriorhodopsin
June 1, 1990

Solid-state 13C NMR study of tyrosine protonation in dark-adapted bacteriorhodopsin
June 1, 1990

Transmembrane protein structure: spin labeling of bacteriorhodopsin mutants
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

Article -

Welcome to inventaire

The library of your friends and communities

Learn more