(Q36354305)

English

In situ determination of transient pKa changes of internal amino acids of bacteriorhodopsin by using time-resolved attenuated total reflection Fourier-transform infrared spectroscopy

scientific article

In more languages

Statements

scholarly article

1 reference

Europe PubMed Central

13 August 2017

In situ determination of transient pKa changes of internal amino acids of bacteriorhodopsin by using time-resolved attenuated total reflection Fourier-transform infrared spectroscopy (English)

1 reference

Europe PubMed Central

13 August 2017

infrared spectroscopy

1 reference

based on heuristic

inferred from title

0 references

Joachim Heberle

object named as

J Heberle

5

0 references

Ramona Schlesinger

object named as

R Schlesinger

2

0 references

author name string

C Zscherp

1

1 reference

Europe PubMed Central

13 August 2017

J Tittor

3

1 reference

Europe PubMed Central

13 August 2017

D Oesterhelt

4

1 reference

Europe PubMed Central

13 August 2017

language of work or name

0 references

publication date

1 May 1999

1 reference

Europe PubMed Central

13 August 2017

number of pages

6

1 reference

based on heuristic

inferred from page(s)

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

1 reference

Europe PubMed Central

13 August 2017

96

1 reference

Europe PubMed Central

13 August 2017

10

1 reference

Europe PubMed Central

13 August 2017

5498-5503

1 reference

Europe PubMed Central

13 August 2017

Redshift of the purple membrane absorption band and the deprotonation of tyrosine residues at high pH: Origin of the parallel photocycles of trans-bacteriorhodopsin

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=21888

30 September 2017

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=21888

30 September 2017

Lipid patches in membrane protein oligomers: crystal structure of the bacteriorhodopsin-lipid complex

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=21888

30 September 2017

Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=21888

30 September 2017

Surface of bacteriorhodopsin revealed by high-resolution electron crystallography

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=21888

30 September 2017

X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=21888

30 September 2017

A molecular mechanism for energy coupling in a membrane transport protein, the lactose permease of Escherichia coli

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=21888

30 September 2017

Protonation dynamics of the extracellular and cytoplasmic surface of bacteriorhodopsin in the purple membrane

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=21888

30 September 2017

Arginine-82 regulates the pKa of the group responsible for the light-driven proton release in bacteriorhodopsin

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=21888

30 September 2017

A large photolysis-induced pKa increase of the chromophore counterion in bacteriorhodopsin: implications for ion transport mechanisms of retinal proteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=21888

30 September 2017

Calculated coupling of electron and proton transfer in the photosynthetic reaction center of Rhodopseudomonas viridis

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=21888

30 September 2017

Electron-crystallographic refinement of the structure of bacteriorhodopsin

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=21888

30 September 2017

Electron diffraction analysis of structural changes in 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=21888

30 September 2017

pH-induced structural changes in bacteriorhodopsin studied by 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=21888

30 September 2017

Glutamic Acid 204 is the Terminal Proton Release Group at the Extracellular Surface of Bacteriorhodopsin

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=21888

30 September 2017

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=21888

30 September 2017

Structural changes in bacteriorhodopsin during proton translocation revealed by neutron diffraction

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=21888

30 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=21888

30 September 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=21888

30 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=21888

30 September 2017

Surface-bound optical probes monitor protein translocation and surface potential changes during the bacteriorhodopsin photocycle

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=21888

30 September 2017

Flash photometric experiments on the photochemical cycle of bacteriorhodopsin

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=21888

30 September 2017

Coupling H+ transport and ATP synthesis in F1F0-ATP synthases: glimpses of interacting parts in a dynamic molecular machine

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=21888

30 September 2017

Mechanism of ion transport across membranes. Bacteriorhodopsin as a prototype for proton pumps

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=21888

29 June 2018

A linkage of the pKa's of asp-85 and glu-204 forms part of the reprotonation switch of bacteriorhodopsin

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=21888

29 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=21888

29 June 2018

Pathways of proton release 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=21888

29 June 2018

Electrostatic calculations of the pKa values of ionizable groups in bacteriorhodopsin

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=21888

29 June 2018

pK(a) calculations along a bacteriorhodopsin molecular dynamics trajectory.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=21888

22 September 2018

Existence of a proton transfer chain in bacteriorhodopsin: participation of Glu-194 in the release of protons to the extracellular surface

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=21888

22 September 2018

Relationship of proton uptake on the cytoplasmic surface and reisomerization of the retinal in the bacteriorhodopsin photocycle: an attempt to understand the complex kinetics of the pH changes and the N and O intermediates

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=21888

22 September 2018

Atr/Ft-Ir Difference Spectroscopy of Biological Matter with Microsecond Time Resolution

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.96.10.5498

21 January 2018

Infrared Difference Spectra of the Intermediates L, M, N, and O of the Bacteriorhodopsin Photoreaction Obtained by Time-Resolved Attenuated Total Reflection Spectroscopy

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.96.10.5498

21 January 2018

D38 Is an Essential Part of the Proton Translocation Pathway in Bacteriorhodopsin†

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.96.10.5498

21 January 2018

Infrared spectroscopy applied to biochemical and biological problems

1 reference

https://pubmed.ncbi.nlm.nih.gov/10318912

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Long-range electrostatic interaction in the bacterial photosynthetic reaction centre

1 reference

https://pubmed.ncbi.nlm.nih.gov/10318912

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Bacteriorhodopsin's intramolecular proton-release pathway consists of a hydrogen-bonded network

1 reference

https://pubmed.ncbi.nlm.nih.gov/10318912

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Photoreaction of bacteriorhodopsin at high pH: origins of the slow decay component of M

1 reference

https://pubmed.ncbi.nlm.nih.gov/10318912

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Resonance Raman and optical transient studies on the light-induced proton pump of bacteriorhodopsin reveal parallel photocycles

1 reference

https://pubmed.ncbi.nlm.nih.gov/10318912

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Proton transfer from Asp-96 to the bacteriorhodopsin Schiff base is caused by a decrease of the pKa of Asp-96 which follows a protein backbone conformational change

1 reference

https://pubmed.ncbi.nlm.nih.gov/10318912

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/10318912

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Structures of aspartic acid-96 in the L and N intermediates of bacteriorhodopsin: analysis by Fourier transform infrared spectroscopy

1 reference

https://pubmed.ncbi.nlm.nih.gov/10318912

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Internal electron transfer in cytochrome c oxidase is coupled to the protonation of a group close to the bimetallic site

1 reference

https://pubmed.ncbi.nlm.nih.gov/10318912

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Aspartic acid-212 of bacteriorhodopsin is ionized in the M and N photocycle intermediates: an FTIR study on specifically 13C-labeled reconstituted purple membranes

1 reference

https://pubmed.ncbi.nlm.nih.gov/10318912

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Fourier transform infrared study of the N intermediate of bacteriorhodopsin

1 reference

https://pubmed.ncbi.nlm.nih.gov/10318912

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Mitochondrial phosphate transport protein. replacements of glutamic, aspartic, and histidine residues affect transport and protein conformation and point to a coupled proton transport path

1 reference

https://pubmed.ncbi.nlm.nih.gov/10318912

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Glutamate-194 to cysteine mutation inhibits fast light-induced proton release in bacteriorhodopsin

1 reference

https://pubmed.ncbi.nlm.nih.gov/10318912

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1073/PNAS.96.10.5498

1 reference

Europe PubMed Central

13 August 2017

1999PNAS...96.5498Z

0 references

1 reference

Europe PubMed Central

13 August 2017

1 reference

Europe PubMed Central

13 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=Q36354305&oldid=1769128229"