(Q37568911)

English

Replacement of leucine-93 by alanine or threonine slows down the decay of the N and O intermediates in the photocycle of bacteriorhodopsin: implications for proton uptake and 13-cis-retinal----all-trans-retinal reisomerization

scientific article published on August 1, 1991

In more languages

Statements

scholarly article

1 reference

Europe PubMed Central

21 August 2017

Replacement of leucine-93 by alanine or threonine slows down the decay of the N and O intermediates in the photocycle of bacteriorhodopsin: implications for proton uptake and 13-cis-retinal----all-trans-retinal reisomerization (English)

1 reference

Europe PubMed Central

21 August 2017

1 reference

based on heuristic

inferred from title

Sriram Subramaniam

1

object named as

S. Subramaniam

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A1650486

21 October 2022

author name string

D. A. Greenhalgh

2

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A1650486

21 October 2022

P. Rath

3

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A1650486

21 October 2022

K. J. Rothschild

4

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A1650486

21 October 2022

H. G. Khorana

5

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A1650486

21 October 2022

language of work or name

0 references

publication date

1 August 1991

1 reference

Europe PubMed Central

21 August 2017

full work available at URL

https://europepmc.org/articles/PMC52191

online access status

content deliverer

Europe PubMed Central

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A1650486

21 October 2022

https://europepmc.org/articles/PMC52191?pdf=render

Portable Document Format

online access status

content deliverer

Europe PubMed Central

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A1650486

21 October 2022

https://pnas.org/doi/pdf/10.1073/pnas.88.15.6873

1 reference

10.1073/PNAS.88.15.6873

https://api.crossref.org/works/10.1073/PNAS.88.15.6873

21 October 2022

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

1 reference

Europe PubMed Central

21 August 2017

88

1 reference

Europe PubMed Central

21 August 2017

6873-6877

1 reference

Europe PubMed Central

21 August 2017

15

1 reference

Europe PubMed Central

21 August 2017

Millisecond Fourier-transform infrared difference spectra of bacteriorhodopsin's M412 photoproduct

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=52191

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=52191

23 August 2017

Orientation of the protonated retinal Schiff base group in bacteriorhodopsin from absorption linear dichroism

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=52191

23 August 2017

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=52191

23 August 2017

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=52191

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=52191

23 August 2017

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=52191

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=52191

23 August 2017

The reaction of hydroxylamine with bacteriorhodopsin studied with mutants that have altered photocycles: selective reactivity of different photointermediates

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=52191

23 August 2017

Protein dynamics in the bacteriorhodopsin photocycle: submillisecond Fourier transform infrared spectra of the L, M, and N photointermediates

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=52191

23 August 2017

Resonance Raman studies of the purple membrane

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=52191

23 August 2017

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=52191

6 September 2017

Bacteriorhodopsin and the purple membrane of halobacteria

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=52191

6 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=52191

28 September 2017

Time-resolved X-ray diffraction study of structural changes associated with the photocycle of bacteriorhodopsin

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=52191

28 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=52191

25 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=52191

25 June 2018

Transmembrane location of retinal in bacteriorhodopsin by neutron diffraction.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=52191

25 June 2018

Ultraviolet-visible transient spectroscopy of bacteriorhodopsin mutants. Evidence for two forms of tyrosine-185----phenylalanine.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=52191

25 June 2018

The role of back-reactions and proton uptake during the N----O transition in bacteriorhodopsin's photocycle: a kinetic resonance Raman study

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=52191

25 June 2018

Bacteriorhodopsin mutants containing single substitutions of serine or threonine residues 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=52191

25 June 2018

Kinetic and spectroscopic evidence for an irreversible step between deprotonation and reprotonation of the Schiff base in the bacteriorhodopsin photocycle

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=52191

25 June 2018

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/1650486

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/1650486

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1073/PNAS.88.15.6873

1 reference

Europe PubMed Central

21 August 2017

1991PNAS...88.6873S

0 references

1 reference

Europe PubMed Central

21 August 2017

1 reference

Europe PubMed Central

21 August 2017

ResearchGate publication ID

0 references

Sitelinks

Wikipedia(0 entries)

Wikibooks(0 entries)

Wikinews(0 entries)

Wikiquote(0 entries)

Wikisource(0 entries)

Wikiversity(0 entries)

Wikivoyage(0 entries)

Wiktionary(0 entries)

Multilingual sites(0 entries)

Retrieved from "https://www.wikidata.org/w/index.php?title=Q37568911&oldid=1755499892"