(Q37684251)

English

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

scientific article published on February 1990

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

22 August 2017

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 (English)

1 reference

Europe PubMed Central

PMC publication ID

22 August 2017

author name string

S Subramaniam

1

1 reference

Europe PubMed Central

PMC publication ID

22 August 2017

T Marti

2

1 reference

Europe PubMed Central

PMC publication ID

22 August 2017

H G Khorana

3

1 reference

Europe PubMed Central

PMC publication ID

22 August 2017

language of work or name

0 references

publication date

1 February 1990

1 reference

Europe PubMed Central

PMC publication ID

22 August 2017

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

1 reference

Europe PubMed Central

PMC publication ID

22 August 2017

87

1 reference

Europe PubMed Central

PMC publication ID

22 August 2017

3

1 reference

Europe PubMed Central

PMC publication ID

22 August 2017

1013-1017

1 reference

Europe PubMed Central

PMC publication ID

22 August 2017

Cation binding by bacteriorhodopsin

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=53400

23 August 2017

Delipidation of bacteriorhodopsin and reconstitution with exogenous phospholipid.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=53400

23 August 2017

Controlling the pKa of the bacteriorhodopsin Schiff base by use of artificial retinal analogues

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=53400

23 August 2017

Chromophore/protein and chromophore/anion interactions in halorhodopsin

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=53400

23 August 2017

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=53400

23 August 2017

Surface pH controls purple-to-blue transition of bacteriorhodopsin. A theoretical model of purple membrane surface

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=53400

23 August 2017

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=53400

23 August 2017

Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=53400

23 August 2017

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=53400

23 August 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=53400

23 August 2017

Reconstitution of Biological Molecular generators of electric current. Bacteriorhodopsin

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=53400

6 September 2017

Effect of acid pH on the absorption spectra and photoreactions of bacteriorhodopsin

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=53400

6 September 2017

Chromophore equilibria in bacteriorhodopsin

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=53400

14 September 2017

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=53400

28 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=53400

23 June 2018

The purple to blue transition of bacteriorhodopsin is accompanied by a loss of the hexagonal lattice and a conformational change.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=53400

23 June 2018

Structure-function studies on bacteriorhodopsin. X. Individual substitutions of arginine residues by glutamine affect chromophore formation, photocycle, and proton translocation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=53400

23 June 2018

Structure-function studies on bacteriorhodopsin. IX. Substitutions of tryptophan residues affect protein-retinal interactions in bacteriorhodopsin

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=53400

23 June 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/1967832

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/1967832

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Effects of anion binding on the deprotonation reactions of halorhodopsin

1 reference

https://pubmed.ncbi.nlm.nih.gov/1967832

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Conserved amino acids in F-helix of bacteriorhodopsin form part of a retinal binding pocket

1 reference

https://pubmed.ncbi.nlm.nih.gov/1967832

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Proton transport by bacteriorhodopsin through an interface film

1 reference

https://pubmed.ncbi.nlm.nih.gov/1967832

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Salt and pH-dependent changes of the purple membrane absorption spectrum

1 reference

https://pubmed.ncbi.nlm.nih.gov/1967832

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1073/PNAS.87.3.1013

1 reference

Europe PubMed Central

PMC publication ID

22 August 2017

1990PNAS...87.1013S

0 references

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

22 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

22 August 2017

ResearchGate publication ID

0 references

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