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Replacement of leucine-93 by alanine or threonine slows down the decay of the N and O intermediates in the photocycle of bacteriorhodopsin: implications for proton uptake and 13-cis-retinal----all-trans-retinal reisomerization

Author

Sriram Subramaniam

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

Date of publication: August 1, 1991

Language: English

Main subject: L-alanine

Bibliographic databases:

Cites articles 24

Date

Title

Authors

June 1, 1977

Resonance Raman studies of the purple membrane
March 1, 1979

Bacteriorhodopsin and the purple membrane of halobacteria
August 1, 1987

Millisecond Fourier-transform infrared difference spectra of bacteriorhodopsin's M412 photoproduct
June 1, 1988

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

Bacteriorhodopsin, a membrane protein that uses light to translocate protons
September 1, 1988

Chromophore structure in bacteriorhodopsin's N intermediate: implications for the proton-pumping mechanism
August 1, 1988

Bacteriorhodopsin photoreaction: identification of a long-lived intermediate N (P,R350) at high pH and its M-like photoproduct
November 1, 1988

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

Orientation of the protonated retinal Schiff base group in bacteriorhodopsin from absorption linear dichroism
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

,
August 1, 1989

Structure-function studies on bacteriorhodopsin. X. Individual substitutions of arginine residues by glutamine affect chromophore formation, photocycle, and proton translocation
June 20, 1990

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

Transmembrane location of retinal in bacteriorhodopsin by neutron diffraction

,
October 1, 1990

Ultraviolet-visible transient spectroscopy of bacteriorhodopsin mutants. Evidence for two forms of tyrosine-185----phenylalanine
August 1, 1990

The role of back-reactions and proton uptake during the N----O transition in bacteriorhodopsin's photocycle: a kinetic resonance Raman study
March 1, 1991

The reaction of hydroxylamine with bacteriorhodopsin studied with mutants that have altered photocycles: selective reactivity of different photointermediates
March 1, 1991

Protein dynamics in the bacteriorhodopsin photocycle: submillisecond Fourier transform infrared spectra of the L, M, and N photointermediates
March 1, 1991

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

Bacteriorhodopsin mutants containing single substitutions of serine or threonine residues are all active in proton translocation
May 1, 1991

Kinetic and spectroscopic evidence for an irreversible step between deprotonation and reprotonation of the Schiff base in the bacteriorhodopsin photocycle

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