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Glutamic Acid 204 is the Terminal Proton Release Group at the Extracellular Surface of Bacteriorhodopsin

Published in: Journal of Biological Chemistry

Date of publication: November 1, 1995

Language: English

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Cites articles 35

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
November 1, 1988

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

Nuclear magnetic resonance study of the Schiff base in bacteriorhodopsin: counterion effects on the 15N shift anisotropy
July 1, 1990

Solid-state 13C and 15N NMR study of the low pH forms of bacteriorhodopsin
June 20, 1990

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

Solid-state 13C NMR study of tyrosine protonation in dark-adapted bacteriorhodopsin
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
June 1, 1991

Alternative translocation of protons and halide ions by bacteriorhodopsin
January 1, 1991

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

Effects of Asp-96----Asn, Asp-85----Asn, and Arg-82----Gln single-site substitutions on the photocycle of bacteriorhodopsin
August 1, 1991

Mechanism of proton pumping in bacteriorhodopsin by solid-state NMR: the protonation state of tyrosine in the light-adapted and M states
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
January 1, 1992

Water structural changes in the bacteriorhodopsin photocycle: analysis by Fourier transform infrared spectroscopy
October 1, 1993

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

Estimated acid dissociation constants of the Schiff base, Asp-85, and Arg-82 during the bacteriorhodopsin photocycle
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
March 1, 1993

Mechanism of light-dependent proton translocation by bacteriorhodopsin
December 1, 1993

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

Pathway of proton uptake in the bacteriorhodopsin photocycle
March 1, 1993

Proton transfer from Asp-96 to the bacteriorhodopsin Schiff base is caused by a decrease of the pKa of Asp-96 which follows a protein backbone conformational change
September 1, 1993

pH dependence of light-induced proton release by bacteriorhodopsin
January 1, 1993

Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin
February 1, 1994

Infrared spectroscopic detection of light-induced change in chloride-arginine interaction in halorhodopsin
October 1, 1994

The retinal Schiff base-counterion complex of bacteriorhodopsin: changed geometry during the photocycle is a cause of proton transfer to aspartate 85.
November 1, 1994

Detection of a water molecule in the active-site of bacteriorhodopsin: hydrogen bonding changes during the primary photoreaction
October 1, 1994

Inversion of proton translocation in bacteriorhodopsin mutants D85N, D85T, and D85,96N.
March 1, 1994

Molecular dynamics study of bacteriorhodopsin and artificial pigments
November 1, 1994

Energy coupling in an ion pump. The reprotonation switch of bacteriorhodopsin
February 1, 1994

Interaction of aspartate-85 with a water molecule and the protonated Schiff base in the L intermediate of bacteriorhodopsin: a Fourier-transform infrared spectroscopic study

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