Inventaire - your friends and communities are your best library

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

Author

Sriram Subramaniam

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

Date of publication: January 1, 1989

Language: English

Main subject: quantum yield

Bibliographic databases:

Cites articles 24

Date

Title

Authors

October 1973

Functions of a new photoreceptor membrane,Functions of a New Photoreceptor Membrane
September 1, 1975

Bacteriorhodopsin: a light-driven proton pump in Halobacterium Halobium
September 1, 1976

Kinetics and stoichiometry of light-induced proton release and uptake from purple membrane fragments, Halobacterium halobium cell envelopes, and phospholipid vesicles containing oriented purple membrane
November 1, 1981

Conformational changes of bacteriorhodopsin detected by Fourier transform infrared difference spectroscopy
June 1982

Bacteriorhodopsin and related pigments of halobacteria
January 1, 1982

Resonance Raman spectra of bacteriorhodopsin's primary photoproduct: evidence for a distorted 13-cis retinal chromophore
April 1, 1983

Energy storage in the primary step of the photocycle of bacteriorhodopsin
January 1, 1983

Absolute quantum yields and proof of proton and nonproton transient release and uptake in photoexcited bacteriorhodopsin
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
September 1, 1986

Large transient nonproton ion movements in purple membrane suspensions are abolished by solubilization in Triton X-100.
July 1, 1987

Large scale nonproton ion release and bacteriorhodopsin's state of aggregation in lipid vesicles. I. Monomers
June 1, 1987

Abrupt onset of large scale nonproton ion release in purple membranes caused by increasing pH or ionic strength
July 1, 1987

Structure-function studies on bacteriorhodopsin. V. Effects of amino acid substitutions in the putative helix F.
April 1, 1987

Flash spectroscopy of purple membrane
July 1, 1987

Structure-function studies on bacteriorhodopsin. IV. Purification and renaturation of bacterio-opsin polypeptide expressed in Escherichia coli
July 1, 1987

Structure-function studies on bacteriorhodopsin. II. Improved expression of the bacterio-opsin gene in Escherichia coli
August 1, 1987

Bacteriorhodopsin mutants containing single tyrosine to phenylalanine substitutions are all active in proton translocation
July 1, 1987

Structure-function studies on bacteriorhodopsin. III. Total synthesis of a gene for bacterio-opsin and its expression in Escherichia coli
June 1, 1988

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

Nonproton ion release by purple membranes exhibits cooperativity as shown by determination of the optical cross-section
September 1, 1988

Effects of amino acid substitutions in the F helix of bacteriorhodopsin. Low temperature ultraviolet/visible difference spectroscopy
June 1, 1988

Bacteriorhodopsin, a membrane protein that uses light to translocate protons
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

Article -

Welcome to inventaire

The library of your friends and communities

Learn more