Experimental evidence for hydrogen-bonded network proton transfer in bacteriorhodopsin shown by Fourier-transform infrared spectroscopy using azide as catalyst (Q34278113)

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English	Experimental evidence for hydrogen-bonded network proton transfer in bacteriorhodopsin shown by Fourier-transform infrared spectroscopy using azide as catalyst	scientific article

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scholarly article

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Europe PubMed Central

PubMed publication ID

1 August 2017

Experimental evidence for hydrogen-bonded network proton transfer in bacteriorhodopsin shown by Fourier-transform infrared spectroscopy using azide as catalyst (English)

1 reference

Europe PubMed Central

PubMed publication ID

1 August 2017

infrared spectroscopy

1 reference

based on heuristic

inferred from title

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author name string

Le Coutre J

1

1 reference

Europe PubMed Central

PubMed publication ID

1 August 2017

Tittor J

2

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Europe PubMed Central

PubMed publication ID

1 August 2017

Oesterhelt D

3

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Europe PubMed Central

PubMed publication ID

1 August 2017

Gerwert K

4

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Europe PubMed Central

PubMed publication ID

1 August 2017

language of work or name

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publication date

1 May 1995

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PubMed publication ID

1 August 2017

number of pages

5

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inferred from page(s)

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

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Europe PubMed Central

PubMed publication ID

1 August 2017

92

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Europe PubMed Central

PubMed publication ID

1 August 2017

11

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Europe PubMed Central

PubMed publication ID

1 August 2017

4962-4966

1 reference

Europe PubMed Central

PubMed publication ID

1 August 2017

The photocycle of the chloride pump halorhodopsin. I: Azide-catalyzed deprotonation of the chromophore is a side reaction of photocycle intermediates inactivating the pump.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=41827

6 July 2018

Simultaneous monitoring of light-induced changes in protein side-group protonation, chromophore isomerization, and backbone motion of bacteriorhodopsin by time-resolved Fourier-transform infrared spectroscopy

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=41827

6 July 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=41827

6 July 2018

Resonance Raman evidence for an all-trans to 13-cis isomerization in the proton-pumping cycle of bacteriorhodopsin

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=41827

6 July 2018

Hydrogen bonded chain mechanisms for proton conduction and proton pumping

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=41827

6 July 2018

Tunable Laser Resonance Raman Spectroscopy of Bacteriorhodopsin

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=41827

6 July 2018

Functions of a New Photoreceptor Membrane

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=41827

6 July 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=41827

6 July 2018

Deprotonation of the Schiff base of bacteriorhodopsin is obligate in light-induced proton pumping

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=41827

6 July 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=41827

6 July 2018

Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsin

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=41827

6 July 2018

A defective proton pump, point-mutated bacteriorhodopsin Asp96----Asn is fully reactivated by azide.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=41827

6 July 2018

Aspartic acids 96 and 85 play a central role in the function of bacteriorhodopsin as a proton pump

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=41827

6 July 2018

Role of aspartate-96 in 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=41827

6 July 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=41827

6 July 2018

A model-independent approach to assigning bacteriorhodopsin's intramolecular reactions to photocycle intermediates

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=41827

28 October 2018

Study of intermediate N using mutant forms of bacteriorhodopsin at Asp-96

1 reference

https://pubmed.ncbi.nlm.nih.gov/7761432

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Water molecules and exchangeable hydrogen ions at the active centre of bacteriorhodopsin localized by neutron diffraction. Elements of the proton pathway?

1 reference

https://pubmed.ncbi.nlm.nih.gov/7761432

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Small weak acids stimulate proton transfer events in site-directed mutants of the two ionizable residues, GluL212 and AspL213, in the QB-binding site of Rhodobacter sphaeroides reaction center

1 reference

https://pubmed.ncbi.nlm.nih.gov/7761432

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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/7761432

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Molecular dynamics study of bacteriorhodopsin and artificial pigments

1 reference

https://pubmed.ncbi.nlm.nih.gov/7761432

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/7761432

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/7761432

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Bacteriorhodopsin in ice

1 reference

https://pubmed.ncbi.nlm.nih.gov/7761432

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1073/PNAS.92.11.4962

1 reference

Europe PubMed Central

PubMed publication ID

1 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

1 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

1 August 2017

ResearchGate publication ID

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