Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsin (Q34322532)

1 August 2017

title

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

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1 August 2017

H Otto

1

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1 August 2017

T Marti

2

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1 August 2017

M Holz

3

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1 August 2017

T Mogi

4

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1 August 2017

M Lindau

5

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1 August 2017

H G Khorana

6

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1 August 2017

M P Heyn

7

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1 August 2017

language of work or name

English

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publication date

1 December 1989

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

1 August 2017

published in

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1 August 2017

volume

86

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1 August 2017

issue

23

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1 August 2017

page(s)

9228-9232

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

1 August 2017

cites work

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=298467

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

6 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=298467

Aspartic acid substitutions affect proton translocation by bacteriorhodopsin

6 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=298467

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

6 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=298467

Bacteriorhodopsin, a membrane protein that uses light to translocate protons

6 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=298467

Bacteriorhodopsin's M412 intermediate contains a 13-cis, 14-s-trans, 15-anti-retinal Schiff base chromophore.

6 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=298467

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

6 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=298467

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

6 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=298467

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

6 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=298467

Role of aspartate-96 in proton translocation by bacteriorhodopsin.

6 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=298467

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

6 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=298467

Effects of tyrosine-26 and tyrosine-64 nitration on the photoreactions of bacteriorhodopsin

6 July 2018

1 reference

12 December 2020

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

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12 December 2020

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

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12 December 2020

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

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12 December 2020

Conformational changes of bacteriorhodopsin detected by Fourier transform infrared difference spectroscopy

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12 December 2020

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

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12 December 2020

Identifiers

DOI

10.1073/PNAS.86.23.9228

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1 August 2017

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1 August 2017

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