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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

Published in: Proceedings of the National Academy of Sciences of the United States of America

Date of publication: February 1, 1990

Language: English

Bibliographic databases:

Cites articles 24

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Title

Authors

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Reconstitution of Biological Molecular generators of electric current. Bacteriorhodopsin
September 1, 1977

Proton transport by bacteriorhodopsin through an interface film
September 1, 1979

Effect of acid pH on the absorption spectra and photoreactions of bacteriorhodopsin
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Chromophore equilibria in bacteriorhodopsin
January 1, 1980

Delipidation of bacteriorhodopsin and reconstitution with exogenous phospholipid
July 1, 1981

Fast stages of photoelectric processes in biological membranes. I. Bacteriorhodopsin
November 1, 1984

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January 1, 1985

Cation binding by bacteriorhodopsin

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May 1, 1986

Controlling the pKa of the bacteriorhodopsin Schiff base by use of artificial retinal analogues
February 1, 1986

Effects of anion binding on the deprotonation reactions of halorhodopsin
July 1, 1987

Structure-function studies on bacteriorhodopsin. IV. Purification and renaturation of bacterio-opsin polypeptide expressed in Escherichia coli
February 1, 1988

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

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

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

Surface pH controls purple-to-blue transition of bacteriorhodopsin. A theoretical model of purple membrane surface.
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
November 1, 1989

Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin
January 1, 1989

Replacement of aspartic residues 85, 96, 115, or 212 affects the quantum yield and kinetics of proton release and uptake by bacteriorhodopsin
June 1, 1989

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

,
November 1, 1989

The purple to blue transition of bacteriorhodopsin is accompanied by a loss of the hexagonal lattice and a conformational change
August 1, 1989

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

Structure-function studies on bacteriorhodopsin. IX. Substitutions of tryptophan residues affect protein-retinal interactions in bacteriorhodopsin
July 1, 1989

Conserved amino acids in F-helix of bacteriorhodopsin form part of a retinal binding pocket
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

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