(Q41659111)

6 October 2017

1 reference

title

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

1 reference

6 October 2017

Lanyi JK

1

1 reference

PubMed ID

9395442

6 October 2017

language of work or name

English

0 references

publication date

1 December 1997

1 reference

Journal of Biological Chemistry

6 October 2017

1 reference

6 October 2017

272

1 reference

6 October 2017

31209-31212

1 reference

6 October 2017

50

1 reference

Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria

6 October 2017

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

A unifying concept for ion translocation by retinal proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

Bacteriorhodopsin as a model for proton pumps

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

Shuttling between two protein conformations: the common mechanism for sensory transduction and ion transport

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

Electron-crystallographic refinement of the structure of bacteriorhodopsin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

Surface of bacteriorhodopsin revealed by high-resolution electron crystallography

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

FTIR difference spectroscopy of bacteriorhodopsin: toward a molecular model

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

Two light-transducing membrane proteins: bacteriorhodopsin and the mammalian rhodopsin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

Perturbed interaction between residues 85 and 204 in Tyr-185-->Phe and Asp-85-->Glu bacteriorhodopsins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

Surface-bound optical probes monitor protein translocation and surface potential changes during the bacteriorhodopsin photocycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

Covalently bound pH-indicator dyes at selected extracellular or cytoplasmic sites in bacteriorhodopsin. 1. Proton migration along the surface of bacteriorhodopsin micelles and its delayed transfer from surface to bulk.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

Covalently bound pH-indicator dyes at selected extracellular or cytoplasmic sites in bacteriorhodopsin. 2. Rotational orientation of helices D and E and kinetic correlation between M formation and proton release in bacteriorhodopsin micelles.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

Pathways of proton release in the bacteriorhodopsin photocycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

A local electrostatic change is the cause of the large-scale protein conformation shift in bacteriorhodopsin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

Molecular mechanism of protein-retinal coupling in bacteriorhodopsin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

Electron diffraction studies of light-induced conformational changes in the Leu-93 --> Ala bacteriorhodopsin mutant.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

The retinal Schiff base-counterion complex of bacteriorhodopsin: changed geometry during the photocycle is a cause of proton transfer to aspartate 85.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

Thermodynamics and energy coupling in the bacteriorhodopsin photocycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

Structural changes in bacteriorhodopsin during proton translocation revealed by neutron diffraction

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

Crystallographic characterization by X-ray diffraction of the M-intermediate from the photo-cycle of bacteriorhodopsin at room temperature

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

The bacteriorhodopsin photocycle: direct structural study of two substrates of the M-intermediate

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

The two consecutive M substates in the photocycle of bacteriorhodopsin are affected specifically by the D85N and D96N residue replacements

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

Inversion of proton translocation in bacteriorhodopsin mutants D85N, D85T, and D85,96N.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

Acid-base equilibrium of the Schiff base in bacteriorhodopsin.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

Effects of hydrostatic pressure on the kinetics reveal a volume increase during the bacteriorhodopsin photocycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

Functional significance of a protein conformation change at the cytoplasmic end of helix F during the bacteriorhodopsin photocycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

Pathway of proton uptake in the bacteriorhodopsin photocycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

Protein structural change at the cytoplasmic surface as the cause of cooperativity in the bacteriorhodopsin photocycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

Electrochemical proton gradient across the cell membrane of Halobacterium halobium: comparison of the light-induced increase with the increase of intracellular adenosine triphosphate under steady-state illumination

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

Stimulation of ATP synthesis in Halobacterium halobium R1 by light-induced or artificially created proton electrochemical potential gradients across the cell membrane

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

pKa of the protonated Schiff base and aspartic 85 in the bacteriorhodopsin binding site is controlled by a specific geometry between the two residues.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

Molecular dynamics study of the M412 intermediate of bacteriorhodopsin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

Conversion of bacteriorhodopsin into a chloride ion pump

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

Photocycle of halorhodopsin from Halobacterium salinarium

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

Light-driven chloride ion transport by halorhodopsin from Natronobacterium pharaonis. 1. The photochemical cycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

Light-driven chloride ion transport by halorhodopsin from Natronobacterium pharaonis. 2. Chloride release and uptake, protein conformation change, and thermodynamics

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

Light-driven proton or chloride pumping by halorhodopsin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

Proton transport by halorhodopsin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

Arginine-82 regulates the pKa of the group responsible for the light-driven proton release in bacteriorhodopsin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31209

21 January 2018

Identifiers

DOI

10.1074/JBC.272.50.31209

1 reference

release_wdatpu2u3feytfu6xyi7rnbx7i

6 October 2017

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/wdatpu2u3feytfu6xyi7rnbx7i

mapped directly with Wikidata item

24 November 2022

based on heuristic

PubMed ID

9395442

1 reference

PubMed ID

9395442