Atomic resolution structures of bacteriorhodopsin photocycle intermediates: the role of discrete water molecules in the function of this light-driven ion pump (Q34030973)

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English	Atomic resolution structures of bacteriorhodopsin photocycle intermediates: the role of discrete water molecules in the function of this light-driven ion pump	scientific article

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scholarly article

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Europe PubMed Central

PubMed publication ID

30 July 2017

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Europe PubMed Central

Atomic resolution structures of bacteriorhodopsin photocycle intermediates: the role of discrete water molecules in the function of this light-driven ion pump (English)

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

author name string

H Luecke

1

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Europe PubMed Central

PubMed publication ID

30 July 2017

language of work or name

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publication date

1 August 2000

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Europe PubMed Central

PubMed publication ID

30 July 2017

Biochimica et Biophysica Acta

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Europe PubMed Central

PubMed publication ID

30 July 2017

1460

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Europe PubMed Central

PubMed publication ID

30 July 2017

1

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

133-156

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

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

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Understanding structure and function in the light-driven proton pump bacteriorhodopsin

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The structure and mechanism of the family of retinal proteins from halophilic archaea

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Closing in on bacteriorhodopsin: progress in understanding the molecule

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Molecular mechanism of photosignaling by archaeal sensory rhodopsins

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Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism

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NMR studies of retinal proteins

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Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution

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Structure of bacteriorhodopsin at 1.55 A resolution

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Resonance Raman spectra of bacteriorhodopsin's primary photoproduct: evidence for a distorted 13-cis retinal chromophore

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Investigation of the primary photochemistry of bacteriorhodopsin by low-temperature Fourier-transform infrared spectroscopy

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Evidence for a tyrosine protonation change during the primary phototransition of bacteriorhodopsin at low temperature

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

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Effects of the crystalline structure of purple membrane on the kinetics and energetics of the bacteriorhodopsin photocycle

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Pathways of proton release in the bacteriorhodopsin photocycle

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Role of aspartate-96 in proton translocation by bacteriorhodopsin.

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

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Relationship of retinal configuration and internal proton transfer at the end of the bacteriorhodopsin photocycle

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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

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The purple membrane from Halobacterium halobium

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Three-dimensional model of purple membrane obtained by electron microscopy

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

1 reference

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Electron-crystallographic refinement of the structure of bacteriorhodopsin

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Opportunities for Collaboration in Europe

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Time-resolved detection of structural changes during the photocycle of spin-labeled bacteriorhodopsin

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Mapping flexible protein domains at subnanometer resolution with the atomic force microscope

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The Protein Data Bank

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The structure of bacteriorhodopsin: an emerging consensus

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Lipidic cubic phases: a novel concept for the crystallization of membrane proteins

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Lipidic Cubic Phases: New Matrices for the Three-Dimensional Crystallization of Membrane Proteins

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

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

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Three-dimensional crystals of membrane proteins: bacteriorhodopsin

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Orthorhombic crystal form of bacteriorhodopsin nucleated on benzamidine diffracting to 3.6 A resolution

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

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

1 reference

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Met-145 is a key residue in the dark adaptation of bacteriorhodopsin homologs

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Steric interaction between the 9-methyl group of the retinal and tryptophan 182 controls 13-cis to all-trans reisomerization and proton uptake in the bacteriorhodopsin photocycle

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Static and time-resolved absorption spectroscopy of the bacteriorhodopsin mutant Tyr-185-->Phe: evidence for an equilibrium between bR570 and an O-like species

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Molecular mechanism of protein-retinal coupling in bacteriorhodopsin

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

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

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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

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

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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

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Estimated acid dissociation constants of the Schiff base, Asp-85, and Arg-82 during the bacteriorhodopsin photocycle

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Proton translocation mechanism and energetics in the light-driven pump bacteriorhodopsin

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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

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Importance of specific native lipids in controlling the photocycle of bacteriorhodopsin.

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

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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

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Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin

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Chemical and functional studies on the importance of purple membrane lipids in bacteriorhodopsin photocycle behavior

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Structural changes in bacteriorhodopsin during ion transport at 2 angstrom resolution

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Protein conformational changes in the bacteriorhodopsin photocycle

1 reference

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Energy coupling in an ion pump. The reprotonation switch of bacteriorhodopsin

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Chromophore Orientation in Bacteriorhodopsin Determined from the Angular Dependence of Deuterium Nuclear Magnetic Resonance Spectra of Oriented Purple Membranes†

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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

1 reference

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Determination of the transiently lowered pKa of the retinal Schiff base during the photocycle of bacteriorhodopsin

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Titration of aspartate-85 in bacteriorhodopsin: what it says about chromophore isomerization and proton release

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

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

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

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

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Replacement of aspartic acid-96 by asparagine in bacteriorhodopsin slows both the decay of the M intermediate and the associated proton movement

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A defective proton pump, point-mutated bacteriorhodopsin Asp96----Asn is fully reactivated by azide.

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

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

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Arginine activity in the proton-motive photocycle of bacteriorhodopsin: solid-state NMR studies of the wild-type and D85N proteins

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Retinal isomer ratio in dark-adapted purple membrane and bacteriorhodopsin monomers

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Conversion of Bacteriorhodopsin into a Chloride Ion Pump

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

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Keilin's Respiratory Chain Concept and Its Chemiosmotic Consequences

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

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Recollections of the electron crystallographic heavy atom derivative search of purple membrane: the quest for EM structure determination.

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7 January 2021

Identifiers

10.1016/S0005-2728(00)00135-3

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

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