(Q34030987)

30 July 2017

1 reference

title

Role of internal water molecules in bacteriorhodopsin (English)

1 reference

30 July 2017

H Kandori

1

1 reference

PubMed ID

10984599

30 July 2017

language of work or name

English

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publication date

1 August 2000

1 reference

Biochimica et Biophysica Acta

30 July 2017

1 reference

30 July 2017

1460

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30 July 2017

177-191

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30 July 2017

1

1 reference

The ATP synthase--a splendid molecular machine

30 July 2017

1 reference

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Internal water molecules and H‐bonding in biological macromolecules: A review of structural features with functional implications

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Time-resolved dynamics of proton transfer in proteinous systems

7 January 2021

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Molecular mechanisms for proton transport in membranes

7 January 2021

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Structure and dynamics of a proton wire: a theoretical study of H+ translocation along the single-file water chain in the gramicidin A channel

7 January 2021

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Interruption of the water chain in the reaction center from Rhodobacter sphaeroides reduces the rates of the proton uptake and of the second electron transfer to QB

7 January 2021

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Structures of metal sites of oxidized bovine heart cytochrome c oxidase at 2.8 A.

7 January 2021

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Structure at 2.8 A resolution of cytochrome c oxidase from Paracoccus denitrificans

7 January 2021

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Molecular architecture of the rotary motor in ATP synthase

7 January 2021

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From femtoseconds to biology: mechanism of bacteriorhodopsin's light-driven proton pump

7 January 2021

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https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

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

7 January 2021

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Closing in on bacteriorhodopsin: progress in understanding the molecule

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Electron-crystallographic refinement of the structure of bacteriorhodopsin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Surface of bacteriorhodopsin revealed by high-resolution electron crystallography

7 January 2021

1 reference

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The structure of bacteriorhodopsin at 3.0 A resolution based on electron crystallography: implication of the charge distribution

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Protein, lipid and water organization in bacteriorhodopsin crystals: a molecular view of the purple membrane at 1.9 A resolution

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Structure of bacteriorhodopsin at 1.55 A resolution

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Specific lipid-protein interactions in a novel honeycomb lattice structure of bacteriorhodopsin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Determination of retinal chromophore structure in bacteriorhodopsin with resonance Raman spectroscopy

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

FTIR difference spectroscopy of bacteriorhodopsin: toward a molecular model

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Infrared spectroscopy applied to biochemical and biological problems

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Molecular reaction mechanisms of proteins monitored by time-resolved FTIR-spectroscopy

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Conformational changes of bacteriorhodopsin detected by Fourier transform infrared difference spectroscopy

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

pH-induced structural changes in bacteriorhodopsin studied by Fourier transform infrared spectroscopy

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Complete identification of C = O stretching vibrational bands of protonated aspartic acid residues in the difference infrared spectra of M and N intermediates versus bacteriorhodopsin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Fourier transform infrared study of the N intermediate of bacteriorhodopsin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

A model-independent approach to assigning bacteriorhodopsin's intramolecular reactions to photocycle intermediates

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Time-resolved Fourier transform infrared spectroscopy of the bacteriorhodopsin mutant Tyr-185-->Phe: Asp-96 reprotonates during O formation; Asp-85 and Asp-212 deprotonate during O decay

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Time-resolved fourier transform infrared study of structural changes in the last steps of the photocycles of Glu-204 and Leu-93 mutants of bacteriorhodopsin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Relationship of proton release at the extracellular surface to deprotonation of the schiff base in the bacteriorhodopsin photocycle

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Functional roles of aspartic acid residues at the cytoplasmic surface of bacteriorhodopsin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Pathways of proton release in the bacteriorhodopsin photocycle

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Effect of the arginine-82 to alanine mutation in bacteriorhodopsin on dark adaptation, proton release, and the photochemical cycle.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

The two pKa's of aspartate-85 and control of thermal isomerization and proton release in the arginine-82 to lysine mutant of bacteriorhodopsin.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Glutamic acid 204 is the terminal proton release group at the extracellular surface of bacteriorhodopsin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Effect of intermolecular orientation upon proton transfer within a polarizable medium

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Role of water in bacteriorhodopsin's chromophore: resonance Raman study

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Nuclear magnetic resonance study of the Schiff base in bacteriorhodopsin: counterion effects on the 15N shift anisotropy

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Hydration effects on the photocycle of bacteriorhodopsin in thin layers of purple membrane

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Photoelectric signals from dried oriented purple membranes of Halobacterium halobium

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Distortions in the photocycle of bacteriorhodopsin at moderate dehydration

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Water structural changes in the bacteriorhodopsin photocycle: analysis by Fourier transform infrared spectroscopy

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

The complex extracellular domain regulates the deprotonation and reprotonation of the retinal Schiff base during the bacteriorhodopsin photocycle

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Hydrogen bonds of water and C==O groups coordinate long-range structural changes in the L photointermediate of bacteriorhodopsin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Effects of arginine-82 on the interactions of internal water molecules in bacteriorhodopsin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Hydration of the counterion of the Schiff base in the chloride-transporting mutant of bacteriorhodopsin: FTIR and FT-raman studies of the effects of anion binding when Asp85 is replaced with a neutral residue.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Trp86 --> Phe replacement in bacteriorhodopsin affects a water molecule near Asp85 and light adaptation

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Detection of a water molecule in the active-site of bacteriorhodopsin: hydrogen bonding changes during the primary photoreaction.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Chromophore-protein-water interactions in the L intermediate of bacteriorhodopsin: FTIR study of the photoreaction of L at 80 K

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Intramembrane signaling mediated by hydrogen-bonding of water and carboxyl groups in bacteriorhodopsin and rhodopsin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Interaction of tryptophan-182 with the retinal 9-methyl group in the L intermediate of bacteriorhodopsin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Structure and function of bacterial photosynthetic reaction centres

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

General concept for ion translocation by halobacterial retinal proteins: the isomerization/switch/transfer (IST) model

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Chloride and proton transport in bacteriorhodopsin mutant D85T: different modes of ion translocation in a retinal protein.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Local-access model for proton transfer in bacteriorhodopsin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Connectivity of the retinal Schiff base to Asp85 and Asp96 during the bacteriorhodopsin photocycle: the local-access model

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Bacteriorhodopsin as a model for proton pumps

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

A three-dimensional difference map of the N intermediate in the bacteriorhodopsin photocycle: part of the F helix tilts in the M to N transition

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Structure of the N intermediate of bacteriorhodopsin revealed by x-ray diffraction.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

The tertiary structural changes in bacteriorhodopsin occur between M states: X-ray diffraction and Fourier transform infrared spectroscopy

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Protein conformational changes in the bacteriorhodopsin photocycle

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Mechanism of light-dependent proton translocation by bacteriorhodopsin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Interaction of proton and chloride transfer pathways in recombinant bacteriorhodopsin with chloride transport activity: implications for the chloride translocation mechanism

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Conversion of bacteriorhodopsin into a chloride ion pump

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Orientation of the bacteriorhodopsin chromophore probed by polarized Fourier transform infrared difference spectroscopy

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Structural change of threonine 89 upon photoisomerization in bacteriorhodopsin as revealed by polarized FTIR spectroscopy

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Localization and orientation of functional water molecules in bacteriorhodopsin as revealed by polarized Fourier transform infrared spectroscopy

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

High-resolution X-ray structure of an early intermediate in the bacteriorhodopsin photocycle

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Structural changes in bacteriorhodopsin during ion transport at 2 angstrom resolution

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Existence of two L photointermediates of halorhodopsin from Halobacterium salinarium, differing in their protein and water FTIR bands

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Water structural changes in lumirhodopsin, metarhodopsin I, and metarhodopsin II upon photolysis of bovine rhodopsin: analysis by Fourier transform infrared spectroscopy

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

FTIR spectroscopy reveals microscopic structural changes of the protein around the rhodopsin chromophore upon photoisomerization

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Structural dynamics of water and the peptide backbone around the Schiff base associated with the light-activated process of octopus rhodopsin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Transmembrane signaling mediated by water in bovine rhodopsin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Water and peptide backbone structure in the active center of bovine rhodopsin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

The hydrogen-bonding network of water molecules and the peptide backbone in the region connecting Asp83, Gly120, and Glu113 in bovine rhodopsin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Hydrogen bonding changes of internal water molecules in rhodopsin during metarhodopsin I and metarhodopsin II formation

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

Local and distant protein structural changes on photoisomerization of the retinal in bacteriorhodopsin.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0005-2728%2800%2900138-9

10.1016/S0005-2728(00)00138-9

7 January 2021

Identifiers

DOI

1 reference

30 July 2017

1 reference

PubMed ID

10984599