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

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

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

http://www.wikidata.org/entity/Q41945254

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Helix deformation is coupled to vectorial proton transport in the photocycle of bacteriorhodopsin Crystal Structure of Sensory Rhodopsin II at 2.4 Angstroms: Insights into Color Tuning and Transducer Interaction Deformation of helix C in the low temperature L-intermediate of bacteriorhodopsin Crystallographic structure of xanthorhodopsin, the light-driven proton pump with a dual chromophore Crystal structure of the O intermediate of the Leu93→Ala mutant of bacteriorhodopsin Lipid patches in membrane protein oligomers: crystal structure of the bacteriorhodopsin-lipid complex Roles of cytoplasmic arginine and threonine in chloride transport by the bacteriorhodopsin mutant D85T.Photocycle of dried acid purple form of bacteriorhodopsin Kinetic and thermodynamic study of the bacteriorhodopsin photocycle over a wide pH range.Charge motions during the photocycle of pharaonis halorhodopsin.Proton transfer reactions in native and deionized bacteriorhodopsin upon delipidation and monomerization Progress toward an explicit mechanistic model for the light-driven pump, bacteriorhodopsin.Mutation of a surface residue, lysine-129, reverses the order of proton release and uptake in bacteriorhodopsin; guanidine hydrochloride restores it Arginine-82 regulates the pKa of the group responsible for the light-driven proton release in bacteriorhodopsin.Evidence that aspartate-85 has a higher pK(a) in all-trans than in 13-cisbacteriorhodopsin.Perturbed interaction between residues 85 and 204 in Tyr-185-->Phe and Asp-85-->Glu bacteriorhodopsins.Contribution of proton release to the B2 photocurrent of bacteriorhodopsin Connectivity of the retinal Schiff base to Asp85 and Asp96 during the bacteriorhodopsin photocycle: the local-access model Nature of the chromophore binding site of bacteriorhodopsin: the potential role of Arg82 as a principal counterion.Binding of calcium ions to bacteriorhodopsin.Two groups control light-induced Schiff base deprotonation and the proton affinity of Asp85 in the Arg82 his mutant of bacteriorhodopsin.On the protein residues that control the yield and kinetics of O(630) in the photocycle of bacteriorhodopsin Molecular dynamics study of the nature and origin of retinal's twisted structure in bacteriorhodopsin.The photochemical reaction cycle of proteorhodopsin at low pH.pH dependence of light-driven proton pumping by an archaerhodopsin from Tibet: comparison with bacteriorhodopsin.Light-driven Na(+) pump from Gillisia limnaea: a high-affinity Na(+) binding site is formed transiently in the photocycle.Intermediate spectra and photocycle kinetics of the Asp96 --> asn mutant bacteriorhodopsin determined by singular value decomposition with self-modeling Structural insights into the mechanism of proton pumping by bacteriorhodopsin.Proton storage site in bacteriorhodopsin: new insights from quantum mechanics/molecular mechanics simulations of microscopic pK(a) and infrared spectra Green proteorhodopsin reconstituted into nanoscale phospholipid bilayers (nanodiscs) as photoactive monomers.Structural and mechanistic insight from high resolution structures of archaeal rhodopsins.X-ray diffraction of bacteriorhodopsin photocycle intermediates.Schiff base protonation changes in Siberian hamster ultraviolet cone pigment photointermediates H++ 3.0: automating pK prediction and the preparation of biomolecular structures for atomistic molecular modeling and simulations Aspartate-histidine interaction in the retinal schiff base counterion of the light-driven proton pump of Exiguobacterium sibiricum.Photochemical reaction cycle transitions during anion channelrhodopsin gating.Photocycle of Exiguobacterium sibiricum rhodopsin characterized by low-temperature trapping in the IR and time-resolved studies in the visible Long-distance proton transfer with a break in the bacteriorhodopsin active site.Microbial and animal rhodopsins: structures, functions, and molecular mechanisms.Photochromic bacteriorhodopsin mutant with high holographic efficiency and enhanced stability via a putative self-repair mechanism.

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P2860

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

http://www.wikidata.org/entity/Q41945254

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1996 nî lūn-bûn

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1996年の論文

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1996年論文

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1996年論文

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1996年論文

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1996年論文

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1996年论文

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1996年论文

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1996年论文

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Titration of aspartate-85 in b ...... merization and proton release.

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Titration of aspartate-85 in b ...... merization and proton release.

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Titration of aspartate-85 in b ...... merization and proton release.

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Titration of aspartate-85 in b ...... merization and proton release.

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E S Imasheva

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R Govindjee

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S P Balashov

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T G Ebrey

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P2860

Rhodopsin-like protein from the purple membrane of Halobacterium halobium

Protein catalysis of the retinal subpicosecond photoisomerization in the primary process of bacteriorhodopsin photosynthesis.

Studies of an acid-induced species of purple membrane from Halobacterium halobium.

Effect of pH buffer molecules on the light-induced currents from oriented purple membrane.

Correlation between absorption maxima and thermal isomerization rates in bacteriorhodopsin.

Redshift of the purple membrane absorption band and the deprotonation of tyrosine residues at high pH: Origin of the parallel photocycles of trans-bacteriorhodopsin.

Environmental effects on the protonation states of active site residues in bacteriorhodopsin

Photoreactions of bacteriorhodopsin at acid pH

Light-induced currents from oriented purple membrane: I. Correlation of the microsecond component (B2) with the L-M photocycle transition.

Rapid pH change due to bacteriorhodopsin measured with a tin-oxide electrode.

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473-481

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10.1016/S0006-3495(96)79591-7

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