Molecular dynamics study of the M412 intermediate of bacteriorhodopsin (Q34047909)

30 July 2017

title

Molecular dynamics study of the M412 intermediate of bacteriorhodopsin (English)

1 reference

30 July 2017

D Xu

1

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30 July 2017

M Sheves

series ordinal

2

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30 July 2017

K Schulten

series ordinal

3

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30 July 2017

language of work or name

English

0 references

publication date

1 December 1995

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30 July 2017

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30 July 2017

volume

69

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30 July 2017

issue

6

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30 July 2017

page(s)

2745-2760

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Evidence for light-induced 13-cis, 14-s-cis isomerization in bacteriorhodopsin obtained by FTIR difference spectroscopy using isotopically labelled retinals

30 July 2017

cites work

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The back photoreaction of the M intermediate in the photocycle of bacteriorhodopsin: mechanism and evidence for two M species

5 July 2018

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Molecular dynamics study of the proton pump cycle of bacteriorhodopsin

5 July 2018

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Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin.

5 July 2018

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Photoreaction of the N intermediate of bacteriorhodopsin, and its relationship to the decay kinetics of the M intermediate

5 July 2018

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The proton transfers in the cytoplasmic domain of bacteriorhodopsin are facilitated by a cluster of interacting residues

5 July 2018

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Light-induced isomerization causes an increase in the chromophore tilt in the M intermediate of bacteriorhodopsin: a neutron diffraction study.

5 July 2018

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Hydrogen bonded chain mechanisms for proton conduction and proton pumping

5 July 2018

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Electron diffraction analysis of the M412 intermediate of bacteriorhodopsin

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1236512

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

5 July 2018

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

5 July 2018

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

5 July 2018

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Structure-function studies on bacteriorhodopsin. VIII. Substitutions of the membrane-embedded prolines 50, 91, and 186: the effects are determined by the substituting amino acids.

5 July 2018

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Role of aspartate-96 in proton translocation by bacteriorhodopsin.

5 July 2018

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Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy

5 July 2018

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Vibrational spectroscopy of bacteriorhodopsin mutants. Evidence for the interaction of aspartic acid 212 with tyrosine 185 and possible role in the proton pump mechanism.

5 July 2018

1 reference

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Octopus photoreceptor membranes. Surface charge density and pK of the Schiff base of the pigments

5 July 2018

1 reference

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Slow-cooling protocols for crystallographic refinement by simulated annealing

5 July 2018

1 reference

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Protonation and deprotonation of the M, N, and O intermediates during the bacteriorhodopsin photocycle.

5 July 2018

1 reference

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Interconversions of the M, N, and O intermediates in the bacteriorhodopsin photocycle.

5 July 2018

1 reference

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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

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1236512

Thermodynamics and energy coupling in the bacteriorhodopsin photocycle

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1236512

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

5 July 2018

1 reference

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

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1236512

Bacteriorhodopsin mutants containing single substitutions of serine or threonine residues are all active in proton translocation.

5 July 2018

1 reference

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

5 July 2018

1 reference

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

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1236512

Participation of bacteriorhodopsin active-site lysine backbone in vibrations associated with retinal photochemistry

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1236512

A residue substitution near the beta-ionone ring of the retinal affects the M substates of bacteriorhodopsin

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1236512

Protein changes associated with reprotonation of the Schiff base in the photocycle of Asp96-->Asn bacteriorhodopsin. The MN intermediate with unprotonated Schiff base but N-like protein structure

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1236512

Asp85 is the only internal aspartic acid that gets protonated in the M intermediate and the purple&#x2010;to&#x2010;blue transition of bacteriorhodopsin A solid&#x2010;state13C CP&#x2010;MAS NMR investigation

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1236512

Electrostatic calculations of the pKa values of ionizable groups in bacteriorhodopsin

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1236512

Bacteriorhodopsin: a light-driven proton pump in Halobacterium Halobium

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1236512

Hydration effects on cis--trans isomerization of bacteriorhodopsin

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1236512

Resonance Raman studies of the purple membrane

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1236512

Identification of retinal isomers isolated from bacteriorhodopsin

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1236512

Conversion of light energy to electrostatic energy in the proton pump of Halobacterium halobium

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1236512

Temperature-dependent X-ray diffraction as a probe of protein structural dynamics

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1236512

Energetics of enzyme catalysis

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1236512

Enthalpy changes during the photochemical cycle of bacteriorhodopsin

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1236512

On the heterogeneity of the M population in the photocycle of bacteriorhodopsin.

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1236512

Why ion pair reversal by protein engineering is unlikely to succeed

28 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1236512

High resolution 13C-solid state NMR of bacteriorhodopsin: assignment of specific aspartic acids and structural implications of single site mutations

28 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1236512

A mechanism for the light-driven proton pump of Halobacterium halobium

28 October 2018

1 reference

https://pubmed.ncbi.nlm.nih.gov/8599681

12 December 2020

Bacteriorhodopsin mutants of Halobacterium sp. GRB. II. Characterization of mutants

1 reference

https://pubmed.ncbi.nlm.nih.gov/8599681

12 December 2020

Water molecules and exchangeable hydrogen ions at the active centre of bacteriorhodopsin localized by neutron diffraction. Elements of the proton pathway?

1 reference

https://pubmed.ncbi.nlm.nih.gov/8599681

12 December 2020

The role of water in retinal complexation to bacterio-opsin

1 reference

https://pubmed.ncbi.nlm.nih.gov/8599681

12 December 2020

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/8599681

12 December 2020

Site-directed isotope labeling and ATR-FTIR difference spectroscopy of bacteriorhodopsin: the peptide carbonyl group of Tyr 185 is structurally active during the bR-->N transition

1 reference

https://pubmed.ncbi.nlm.nih.gov/8599681

12 December 2020

Molecular dynamics study of bacteriorhodopsin and artificial pigments

1 reference

https://pubmed.ncbi.nlm.nih.gov/8599681

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/8599681

12 December 2020

Dynamics of ligand binding to myoglobin

1 reference

https://pubmed.ncbi.nlm.nih.gov/8599681

12 December 2020

An isomerization model for the pump cycle of bacteriorhodopsin

1 reference

https://pubmed.ncbi.nlm.nih.gov/8599681

12 December 2020

Active site lysine backbone undergoes conformational changes in the bacteriorhodopsin photocycle

1 reference

https://pubmed.ncbi.nlm.nih.gov/8599681

12 December 2020

10.1016/S0006-3495(95)80146-3

Identifiers

DOI

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30 July 2017

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30 July 2017

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