Glutamic Acid 204 is the Terminal Proton Release Group at the Extracellular Surface of Bacteriorhodopsin (Q30417307)

21 June 2017

title

Glutamic acid 204 is the terminal proton release group at the extracellular surface of bacteriorhodopsin (English)

1 reference

21 June 2017

Glutamic Acid 204 is the Terminal Proton Release Group at the Extracellular Surface of Bacteriorhodopsin (English)

1 reference

https://api.crossref.org/works/10.1074/JBC.270.45.27122

1 June 2024

author name string

L. S. Brown

1

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1 June 2024

J. Sasaki

2

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1 June 2024

H. Kandori

3

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1 June 2024

A. Maeda

4

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R. Needleman

5

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J. K. Lanyi

6

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1 June 2024

language of work or name

English

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publication date

1 November 1995

1 reference

21 June 2017

10 November 1995

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National Center for Biotechnology Information

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=7592966

full work available at URL

1 June 2024

http://www.jbc.org/article/S0021925818881182/pdf

file format

Portable Document Format

online access status

open access

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https://api.elsevier.com/content/article/PII:S0021925818881182?httpAccept=text/xml

1 June 2024

1 reference

https://api.crossref.org/works/10.1074/JBC.270.45.27122

https://api.elsevier.com/content/article/PII:S0021925818881182?httpAccept=text/plain

1 June 2024

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https://syndication.highwire.org/content/doi/10.1074/jbc.270.45.27122

1 June 2024

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Journal of Biological Chemistry

1 June 2024

published in

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21 June 2017

volume

270

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21 June 2017

issue

45

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21 June 2017

page(s)

27122-27126

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Effect of the arginine-82 to alanine mutation in bacteriorhodopsin on dark adaptation, proton release, and the photochemical cycle.

21 June 2017

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Infrared spectroscopic detection of light-induced change in chloride-arginine interaction in halorhodopsin

21 January 2018

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Estimated acid dissociation constants of the Schiff base, Asp-85, and Arg-82 during the bacteriorhodopsin photocycle

21 January 2018

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The retinal Schiff base-counterion complex of bacteriorhodopsin: changed geometry during the photocycle is a cause of proton transfer to aspartate 85.

21 January 2018

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Relationship of proton uptake on the cytoplasmic surface and reisomerization of the retinal in the bacteriorhodopsin photocycle: an attempt to understand the complex kinetics of the pH changes and the N and O intermediates

21 January 2018

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Solid-state 13C and 15N NMR study of the low pH forms of bacteriorhodopsin

21 January 2018

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Alternative translocation of protons and halide ions by bacteriorhodopsin

21 January 2018

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Detection of a water molecule in the active-site of bacteriorhodopsin: hydrogen bonding changes during the primary photoreaction.

21 January 2018

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Surface-bound optical probes monitor protein translocation and surface potential changes during the bacteriorhodopsin photocycle

21 January 2018

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Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy

21 January 2018

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Solid-state 13C NMR study of tyrosine protonation in dark-adapted bacteriorhodopsin

21 January 2018

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Mechanism of light-dependent proton translocation by bacteriorhodopsin

21 January 2018

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Proton translocation mechanism and energetics in the light-driven pump bacteriorhodopsin

21 January 2018

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Bacteriorhodopsin: a light-driven proton pump in Halobacterium Halobium

21 January 2018

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From femtoseconds to biology: mechanism of bacteriorhodopsin's light-driven proton pump

21 January 2018

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Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane

21 January 2018

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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

21 January 2018

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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

21 January 2018

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Effects of Asp-96----Asn, Asp-85----Asn, and Arg-82----Gln single-site substitutions on the photocycle of bacteriorhodopsin

21 January 2018

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Inversion of proton translocation in bacteriorhodopsin mutants D85N, D85T, and D85,96N.

21 January 2018

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Pathways of proton release in the bacteriorhodopsin photocycle

21 January 2018

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Pathway of proton uptake in the bacteriorhodopsin photocycle

21 January 2018

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

21 January 2018

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Proton transfer from Asp-96 to the bacteriorhodopsin Schiff base is caused by a decrease of the pKa of Asp-96 which follows a protein backbone conformational change

1 June 2024

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

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Molecular dynamics study of bacteriorhodopsin and artificial pigments

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Water structural changes in the bacteriorhodopsin photocycle: analysis by Fourier transform infrared spectroscopy

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Interaction of aspartate-85 with a water molecule and the protonated Schiff base in the L intermediate of bacteriorhodopsin: a Fourier-transform infrared spectroscopic study

1 June 2024

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Mechanism of proton pumping in bacteriorhodopsin by solid-state NMR: the protonation state of tyrosine in the light-adapted and M states

1 June 2024

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Complete identification of C = O stretching vibrational bands of protonated aspartic acid residues in the difference infrared spectra of M and N intermediates versus bacteriorhodopsin

1 June 2024

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Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin.

1 June 2024

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Water structural changes at the proton uptake site (the Thr46-Asp96 domain) in the L intermediate of bacteriorhodopsin

1 June 2024

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1 June 2024

Identifiers

1 reference

21 June 2017

1 reference