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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

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 19

Date

Title

Authors

November 1, 1979

Chromophore equilibria in bacteriorhodopsin
July 1, 1981

Fast stages of photoelectric processes in biological membranes. I. Bacteriorhodopsin
September 1, 1982

Acid-base equilibrium of the Schiff base in bacteriorhodopsin
May 1, 1986

Controlling the pKa of the bacteriorhodopsin Schiff base by use of artificial retinal analogues
December 1, 1987

Refolding of bacteriorhodopsin in lipid bilayers. A thermodynamically controlled two-stage process
December 1, 1988

Monomeric and aggregated bacteriorhodopsin: Single-turnover proton transport stoichiometry and photochemistry
June 1, 1988

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

Distributed kinetics of the charge movements in bacteriorhodopsin: evidence for conformational substates
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, 1988

Bacteriorhodopsin photoreaction: identification of a long-lived intermediate N (P,R350) at high pH and its M-like photoproduct
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

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

Role of aspartate-96 in proton translocation by bacteriorhodopsin.
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
April 1, 1989

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

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