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

Published in: Biophysical Journal

Date of publication: July 1, 1993

Language: English

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Cites articles 34

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Authors

1974

Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane
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Charge stabilization mechanism in the visual and purple membrane pigments
November 1, 1979

Chromophore equilibria in bacteriorhodopsin
September 1, 1982

Acid-base equilibrium of the Schiff base in bacteriorhodopsin
April 1, 1985

On the mechanism of wavelength regulation in visual pigments
September 1, 1988

Chromophore structure in bacteriorhodopsin's N intermediate: implications for the proton-pumping mechanism
October 1, 1989

Structural changes in bacteriorhodopsin during proton translocation revealed by neutron diffraction
July 1, 1989

Role of aspartate-96 in proton translocation by bacteriorhodopsin.
December 1, 1990

Simultaneous monitoring of light-induced changes in protein side-group protonation, chromophore isomerization, and backbone motion of bacteriorhodopsin by time-resolved Fourier-transform infrared spectroscopy
May 1, 1990

An efficient system for the synthesis of bacteriorhodopsin in Halobacterium halobium
June 20, 1990

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

Electrostatic interactions in macromolecules: theory and applications
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
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

,
May 1, 1991

Thermodynamics and energy coupling in the bacteriorhodopsin photocycle
March 1, 1991

Time-resolved X-ray diffraction study of structural changes associated with the photocycle of bacteriorhodopsin
November 1, 1991

Crystallographic characterization by X-ray diffraction of the M-intermediate from the photo-cycle of bacteriorhodopsin at room temperature
October 1, 1991

The retinylidene Schiff base counterion in bacteriorhodopsin
September 1, 1991

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

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

Electrostatic energy and macromolecular function,Electrostatic Energy and Macromolecular Function
October 1, 1991

Effect of intermolecular orientation upon proton transfer within a polarizable medium
June 1, 1991

Properties of Asp212----Asn bacteriorhodopsin suggest that Asp212 and Asp85 both participate in a counterion and proton acceptor complex near the Schiff base
June 1, 1991

Vibrational spectroscopy of bacteriorhodopsin mutants. Evidence that ASP-96 deprotonates during the M----N transition
July 1, 1991

Fourier transform infrared study of the N intermediate of bacteriorhodopsin
April 1, 1992

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

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

Influence of the size and protonation state of acidic residue 85 on the absorption spectrum and photoreaction of the bacteriorhodopsin chromophore
December 1, 1992

The two consecutive M substates in the photocycle of bacteriorhodopsin are affected specifically by the D85N and D96N residue replacements
September 1, 1992

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

Proton transfer and energy coupling in the bacteriorhodopsin photocycle

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