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A defective proton pump, point-mutated bacteriorhodopsin Asp96----Asn is fully reactivated by azide.

Author

Hans-Jürgen Butt

1961 -

Ernst Bamberg

1940 -

Published in: The EMBO Journal

Date of publication: November 1, 1989

Language: English

Bibliographic databases:

Cites articles 37

Date

Title

Authors

August 1, 1973

Reversible Photolysis of the Purple Complex in the Purple Membrane of Halobacterium halobium
December 1, 1975

Arrhenius parameters of phototransients in Halobacterium halobium in physiological conditions
December 1, 1976

Incorporation of bacteriorhodopsin into a bilayer lipid membrane; a photoelectric-spectroscopic study
September 1, 1977

Bacteriorhodopsin-loaded charged synthetic membranes utilization of light energy to generate electrical current,Bacteriorhodopsin-loaded charged synthetic membranes. Utilization of light energy to generate electrical current
May 1, 1977

Identification of retinal isomers isolated from bacteriorhodopsin
August 1, 1978

Mechanism of generation and regulation of photopotential by bacteriorhodopsin in bimolecular lipid membrane,Mechanism of generation and regulation of photopotential by bacteriorhodopsin in bimolecular lipid membrane. The quenching effect of blue light
March 1, 1978

A mechanism for the light-driven proton pump 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
September 1, 1980

Light isomerizes the chromophore of bacteriorhodopsin
July 1, 1981

Proton conduction in bacteriorhodopsin via a hydrogen-bonded chain with large proton polarizability,Proton conduction in bacteriophodopsin via a hydrogen-bonded chain with large proton polarizability
June 1982

Bacteriorhodopsin and related pigments of halobacteria
January 1, 1983

Hydrogen bonded chain mechanisms for proton conduction and proton pumping
November 1, 1984

A polychromatic flash photolysis apparatus (PFPA)
September 1, 1985

The photocycle of the chloride pump halorhodopsin. II: Quantum yields and a kinetic model
September 1, 1985

The photocycle of the chloride pump halorhodopsin. I: Azide-catalyzed deprotonation of the chromophore is a side reaction of photocycle intermediates inactivating the pump
March 1, 1985

The effect of protonation and electrical interactions on the stereochemistry of retinal schiff bases
March 1, 1985

Time-resolved photoelectric and absorption signals from oriented purple membranes immobilized in gel
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
August 1, 1986

How Many M Forms are there in the Bacteriorhodopsin Photocycle?
January 1, 1986

Flash spectroscopic studies of the kinetics of the halorhodopsin photocycle
October 1, 1986

Mechanism of base-catalyzed Schiff base deprotonation in halorhodopsin
January 1, 1987

The halo-opsin gene. II. Sequence, primary structure of halorhodopsin and comparison with bacteriorhodopsin
October 1, 1987

Tyrosine and carboxyl protonation changes in the bacteriorhodopsin photocycle. 2. Tyrosines-26 and -64
April 1, 1988

Bacteriorhodopsin's L550 intermediate contains a C14-C15 s-trans-retinal chromophore
February 1, 1988

Chromophore/protein and chromophore/anion interactions in halorhodopsin
June 1, 1988

Aspartic acid substitutions affect proton translocation by bacteriorhodopsin
January 1, 1988

Structure and function of bacteriorhodopsin
November 1, 1988

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

Vibrational spectroscopy of bacteriorhodopsin mutants: I. Tyrosine-185 protonates and deprotonates during the photocycle
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
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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