A unifying concept for ion translocation by retinal proteins (Q34549538)

3 August 2017

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title

A unifying concept for ion translocation by retinal proteins (English)

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3 August 2017

3

Bamberg E

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3 August 2017

D. Oesterhelt

1

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A1526960

5 October 2022

J. Tittor

series ordinal

2

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A1526960

5 October 2022

language of work or name

English

1 reference

National Center for Biotechnology Information

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=1526960

5 October 2022

publication date

1 April 1992

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Journal of Bioenergetics and Biomembranes

3 August 2017

published in

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3 August 2017

volume

24

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3 August 2017

issue

2

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3 August 2017

page(s)

181-191

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

3 August 2017

cites work

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Light isomerizes the chromophore of bacteriorhodopsin

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Light-induced changes of the pH gradient and the membrane potential inH. halobium

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

The photocycle of the chloride pump halorhodopsin. I: Azide-catalyzed deprotonation of the chromophore is a side reaction of photocycle intermediates inactivating the pump.

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Anion-induced wavelength regulation of absorption maxima of Schiff bases of retinal

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Aspartic acid substitutions affect proton translocation by bacteriorhodopsin

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

The photocycle of the chloride pump halorhodopsin. II: Quantum yields and a kinetic model.

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

The primary structure of a halorhodopsin from Natronobacterium pharaonis. Structural, functional and evolutionary implications for bacterial rhodopsins and halorhodopsins.

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Solid-state 13C and 15N NMR study of the low pH forms of bacteriorhodopsin

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

The structure of bacteriorhodopsin and its relevance to the visual opsins and other seven-helix G-protein coupled receptors

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Exchange kinetics of the Schiff base proton in bacteriorhodopsin

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Archaerhodopsin-2, from Halobacterium sp. aus-2 further reveals essential amino acid residues for light-driven proton pumps

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Effects of various anions on the Raman spectrum of halorhodopsin

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Primary structure of sensory rhodopsin I, a prokaryotic photoreceptor

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

High-sensitivity neutron diffraction of membranes: Location of the Schiff base end of the chromophore of bacteriorhodopsin

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

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/1526960

12 December 2020

Halorhodopsin, a light-driven electrogenic chloride-transport system

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Structural changes in bacteriorhodopsin during proton translocation revealed by neutron diffraction

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Reversible Photolysis of the Purple Complex in the Purple Membrane of Halobacterium halobium

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Chromophore motion during the bacteriorhodopsin photocycle: polarized absorption spectroscopy of bacteriorhodopsin and its M-state in bacteriorhodopsin crystals

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

The effect of protonation and electrical interactions on the stereochemistry of retinal schiff bases

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Alternative translocation of protons and halide ions by bacteriorhodopsin

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Sensory rhodopsins of halobacteria

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

The orientation of halorhodopsin in the cell membrane of halobacteria

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Structure of the retinal chromophore in the hRL intermediate of halorhodopsin from resonance raman spectroscopy

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

The halo-opsin gene. II. Sequence, primary structure of halorhodopsin and comparison with bacteriorhodopsin.

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

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

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Chromophore equilibria in bacteriorhodopsin

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Mechanism of generation and regulation of photopotential by bacteriorhodopsin in bimolecular lipid membrane

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Halide binding by the purified halorhodopsin chromoprotein. II. New chloride-binding sites revealed by 35Cl NMR

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Transmembrane location of retinal in bacteriorhodopsin by neutron diffraction.

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Time-resolved X-ray diffraction study of structural changes associated with the photocycle of bacteriorhodopsin

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Nature of the primary photochemical events in rhodopsin and bacteriorhodopsin

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Infrared spectroscopic demonstration of a conformational change in bacteriorhodopsin involved in proton pumping

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

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/1526960

12 December 2020

Halorhodopsin: a light-driven chloride ion pump

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Aspartic acids 96 and 85 play a central role in the function of bacteriorhodopsin as a proton pump

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

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://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Effects of anion binding on the deprotonation reactions of halorhodopsin

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Influence of the size and protonation state of acidic residue 85 on the absorption spectrum and photoreaction of the bacteriorhodopsin chromophore

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Replacement of aspartic residues 85, 96, 115, or 212 affects the quantum yield and kinetics of proton release and uptake by bacteriorhodopsin.

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Vibrational spectra of rhodopsin and bacteriorhodopsin

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Determination of retinal Schiff base configuration in bacteriorhodopsin

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Reversible Dissociation of the Purple Complex in Bacteriorhodopsin and Identification of 13-cis and all-trans-Retinal as its Chromophores

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Role of aspartate-96 in proton translocation by bacteriorhodopsin.

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Protonation state of Asp (Glu)-85 regulates the purple-to-blue transition in bacteriorhodopsin mutants Arg-82----Ala and Asp-85----Glu: the blue form is inactive in proton translocation

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Identification of retinal isomers isolated from bacteriorhodopsin

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Two pumps, one principle: light-driven ion transport in halobacteria

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Activation parameters for the halorhodopsin photocycle: a phase lifetime spectroscopic study of the 520- and 640-nanometer intermediates.

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Changes in the protonation state of bacterio-opsin during reconstitution of bacteriorhodopsin

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Anion binding to the chloride pump, halorhodopsin, and its implications for the transport mechanism

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Photoelectric measurements of purple membranes

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Structure and orientation of halorhodopsin in the membrane: a proteolytic fragmentation study

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

The halo-opsin gene. I. Identification and isolation

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Bacteriorhodopsin as an example of a light-driven proton pump

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Thermodynamics and energy coupling in the bacteriorhodopsin photocycle

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Bacteriorhodopsin in ice

1 reference

https://pubmed.ncbi.nlm.nih.gov/1526960

12 December 2020

Identifiers

DOI

10.1007/BF00762676

1 reference

Dimensions Publication ID

3 August 2017

1030501804

0 references

1 reference