(Q33846264)

English

Replacement of aspartic acid-96 by asparagine in bacteriorhodopsin slows both the decay of the M intermediate and the associated proton movement

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scholarly article

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Europe PubMed Central

PubMed publication ID

29 July 2017

Replacement of aspartic acid-96 by asparagine in bacteriorhodopsin slows both the decay of the M intermediate and the associated proton movement (English)

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

author name string

M Holz

1

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

L A Drachev

2

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

T Mogi

3

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

H Otto

4

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

A D Kaulen

5

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

M P Heyn

6

1 reference

Europe PubMed Central

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29 July 2017

V P Skulachev

7

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Europe PubMed Central

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29 July 2017

H G Khorana

8

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29 July 2017

language of work or name

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publication date

1 April 1989

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29 July 2017

Proceedings of the National Academy of Sciences of the United States of America

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29 July 2017

86

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Europe PubMed Central

PubMed publication ID

29 July 2017

7

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Europe PubMed Central

PubMed publication ID

29 July 2017

2167-2171

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286872

5 July 2018

Rhodopsin and bacteriorhodopsin: structure-function relationships

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286872

5 July 2018

Temperature dependence of photovoltages generated by bacteriorhodopsin

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286872

5 July 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286872

5 July 2018

Aspartic acid substitutions affect proton translocation by bacteriorhodopsin

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286872

5 July 2018

Bacteriorhodopsin mutants containing single tyrosine to phenylalanine substitutions are all active in proton translocation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286872

5 July 2018

Bacteriorhodopsin, a membrane protein that uses light to translocate protons

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286872

5 July 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286872

5 July 2018

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/2648392

12 December 2020

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inferred from PubMed ID database lookup

Refolding of bacteriorhodopsin in lipid bilayers. A thermodynamically controlled two-stage process

1 reference

https://pubmed.ncbi.nlm.nih.gov/2648392

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Fast stages of photoelectric processes in biological membranes. I. Bacteriorhodopsin

1 reference

https://pubmed.ncbi.nlm.nih.gov/2648392

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/2648392

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Conformational changes of bacteriorhodopsin detected by Fourier transform infrared difference spectroscopy

1 reference

https://pubmed.ncbi.nlm.nih.gov/2648392

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1073/PNAS.86.7.2167

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

1989PNAS...86.2167H

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release_2e64bdqn5fffti2hzuxtfbdcwe

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https://api.fatcat.wiki/v0/release/2e64bdqn5fffti2hzuxtfbdcwe

24 November 2022

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PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

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