Water structural changes in the L and M photocycle intermediates of bacteriorhodopsin as revealed by time-resolved step-scan Fourier transform infrared (FTIR) spectroscopy (Q38590732)

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scientific article published on 15 February 2007

Language	Label	Description	Also known as
English	Water structural changes in the L and M photocycle intermediates of bacteriorhodopsin as revealed by time-resolved step-scan Fourier transform infrared (FTIR) spectroscopy	scientific article published on 15 February 2007

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

4 September 2017

Water structural changes in the L and M photocycle intermediates of bacteriorhodopsin as revealed by time-resolved step-scan Fourier transform infrared (FTIR) spectroscopy (English)

1 reference

Europe PubMed Central

PMC publication ID

4 September 2017

author name string

Joel E Morgan

1

1 reference

Europe PubMed Central

PMC publication ID

4 September 2017

Ahmet S Vakkasoglu

2

1 reference

Europe PubMed Central

PMC publication ID

4 September 2017

Robert B Gennis

3

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Europe PubMed Central

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4 September 2017

Akio Maeda

4

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Europe PubMed Central

PMC publication ID

4 September 2017

language of work or name

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publication date

15 February 2007

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Europe PubMed Central

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4 September 2017

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Europe PubMed Central

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4 September 2017

46

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Europe PubMed Central

PMC publication ID

4 September 2017

10

1 reference

Europe PubMed Central

PMC publication ID

4 September 2017

2787-2796

1 reference

Europe PubMed Central

PMC publication ID

4 September 2017

Water as a cofactor in the unidirectional light-driven proton transfer steps in bacteriorhodopsin

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3972897

6 September 2017

Spectral signatures of hydrated proton vibrations in water clusters

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3972897

6 September 2017

Proton binding within a membrane protein by a protonated water cluster

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3972897

6 September 2017

Crystal structure of the L intermediate of bacteriorhodopsin: evidence for vertical translocation of a water molecule during the proton pumping cycle

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3972897

6 September 2017

Deformation of helix C in the low temperature L-intermediate of bacteriorhodopsin

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3972897

6 September 2017

Crystallographic structures of the M and N intermediates of bacteriorhodopsin: assembly of a hydrogen-bonded chain of water molecules between Asp-96 and the retinal Schiff base

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3972897

6 September 2017

Mechanism of Proton Transport in Bacteriorhodopsin from Crystallographic Structures of the K, L, M1, M2, and M2′ Intermediates of the Photocycle

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3972897

6 September 2017

Crystallographic structure of the retinal and the protein after deprotonation of the Schiff base: the switch 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=3972897

6 September 2017

Structure of an early intermediate in the M-state phase of the bacteriorhodopsin photocycle

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3972897

6 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=3972897

6 September 2017

Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3972897

6 September 2017

Coupling photoisomerization of retinal to directional transport in bacteriorhodopsin

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3972897

6 September 2017

How soft is a protein? A protein dynamics force constant measured by neutron scattering.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3972897

6 September 2017

Structural changes in bacteriorhodopsin during ion transport at 2 angstrom resolution

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3972897

6 September 2017

Structure of bacteriorhodopsin at 1.55 A resolution

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3972897

6 September 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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3972897

6 September 2017

Thermal motions and function of bacteriorhodopsin in purple membranes: effects of temperature and hydration studied by neutron scattering

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3972897

6 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3972897

6 September 2017

Nanosecond time-resolved infrared spectroscopy distinguishes two K species 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=3972897

6 September 2017

Environmental effects on formation and photoreaction of the M412 photoproduct of bacteriorhodopsin: implications for the mechanism of proton pumping

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3972897

6 September 2017

Flash spectroscopy of purple membrane

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3972897

6 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=3972897

6 September 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=3972897

6 September 2017

Bacteriorhodopsin: a light-driven proton pump in Halobacterium Halobium

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3972897

6 September 2017

The assignment of the different infrared continuum absorbance changes observed in the 3000-1800-cm(-1) region 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=3972897

14 September 2017

Time-resolved step-scan Fourier transform infrared spectroscopy reveals differences between early and late M intermediates of bacteriorhodopsin

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3972897

14 September 2017

Proton uptake mechanism of bacteriorhodopsin as determined by time-resolved stroboscopic-FTIR-spectroscopy

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3972897

23 June 2018

The proton release group of bacteriorhodopsin controls the rate of the final step of its photocycle at low pH.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3972897

23 June 2018

Spectrally silent transitions 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=3972897

23 June 2018

Water is required for proton transfer from aspartate-96 to the bacteriorhodopsin Schiff base

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3972897

23 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=3972897

23 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=3972897

23 June 2018

Crystal structure of the M intermediate of bacteriorhodopsin: allosteric structural changes mediated by sliding movement of a transmembrane helix

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3972897

31 August 2018

Role of hydrogen-bond network in energy storage of bacteriorhodopsin's light-driven proton pump revealed by ab initio normal-mode analysis

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3972897

31 August 2018

Water-mediated hydrogen-bonded network on the cytoplasmic side of the Schiff base of the L photointermediate of bacteriorhodopsin

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3972897

31 August 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=3972897

31 August 2018

Relocation of water molecules between the Schiff base and the Thr46-Asp96 region during light-driven unidirectional proton transport by bacteriorhodopsin: an FTIR study of the N intermediate

1 reference

https://pubmed.ncbi.nlm.nih.gov/17300175

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Functional waters in intraprotein proton transfer monitored by FTIR difference spectroscopy

1 reference

https://pubmed.ncbi.nlm.nih.gov/17300175

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/17300175

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Relocation of internal bound water in bacteriorhodopsin during the photoreaction of M at low temperatures: an FTIR study

1 reference

https://pubmed.ncbi.nlm.nih.gov/17300175

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Water structural changes at the proton uptake site (the Thr46-Asp96 domain) in the L intermediate of bacteriorhodopsin

1 reference

https://pubmed.ncbi.nlm.nih.gov/17300175

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/17300175

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/17300175

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Interaction of internal water molecules with the schiff base in the L intermediate of the bacteriorhodopsin photocycle

1 reference

https://pubmed.ncbi.nlm.nih.gov/17300175

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/17300175

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Interaction of aspartate-85 with a water molecule and the protonated Schiff base in the L intermediate of bacteriorhodopsin: a Fourier-transform infrared spectroscopic study

1 reference

https://pubmed.ncbi.nlm.nih.gov/17300175

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Interaction of the protonated Schiff base with the peptide backbone of valine 49 and the intervening water molecule in the N photointermediate of bacteriorhodopsin

1 reference

https://pubmed.ncbi.nlm.nih.gov/17300175

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/17300175

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1021/BI0616596

1 reference

Europe PubMed Central

PMC publication ID

4 September 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

4 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

4 September 2017

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