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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Deprotonation of D96 in Bacteriorhodopsin Opens the Proton Uptake PathwayFactors influencing the energetics of electron and proton transfers in proteins. What can be learned from calculations.Protein dynamics in the bacteriorhodopsin photocycle: submillisecond Fourier transform infrared spectra of the L, M, and N photointermediates.Control of the pump cycle in bacteriorhodopsin: mechanisms elucidated by solid-state NMR of the D85N mutant.Cl(-) concentration dependence of photovoltage generation by halorhodopsin from Halobacterium salinarum.The back photoreaction of the M intermediate in the photocycle of bacteriorhodopsin: mechanism and evidence for two M species.Effect of genetic modification of tyrosine-185 on the proton pump and the blue-to-purple transition in bacteriorhodopsin.Proton transport by a bacteriorhodopsin mutant, aspartic acid-85-->asparagine, initiated in the unprotonated Schiff base state.Conformationally controlled pK-switching in membrane proteins: one more mechanism specific to the enzyme catalysis?His166 is critical for active-site proton transfer and phototaxis signaling by sensory rhodopsin I.Photoproducts of bacteriorhodopsin mutants: a molecular dynamics study.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.Uv-visible spectroscopy of bacteriorhodopsin mutants: substitution of Arg-82, Asp-85, Tyr-185, and Asp-212 results in abnormal light-dark adaptation.Two progressive substrates of the M-intermediate can be identified in glucose-embedded, wild-type bacteriorhodopsin.pH-induced structural changes in bacteriorhodopsin studied by Fourier transform infrared spectroscopyLight-induced reorientation in the purple membrane.Two-dimensional crystallization of Escherichia coli-expressed bacteriorhodopsin and its D96N variant: high resolution structural studies in projection.Study of the photocycle and charge motions of the bacteriorhodopsin mutant D96N.Photochemical reaction cycle and proton transfers in Neurospora rhodopsin.Effects of individual genetic substitutions of arginine residues on the deprotonation and reprotonation kinetics of the Schiff base during the bacteriorhodopsin photocycleCorrelation 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.Effect of intermolecular orientation upon proton transfer within a polarizable mediumA residue substitution near the beta-ionone ring of the retinal affects the M substates of bacteriorhodopsinOrientation of the protonated retinal Schiff base group in bacteriorhodopsin from absorption linear dichroism.Distortions in the photocycle of bacteriorhodopsin at moderate dehydration.Rapid pH change due to bacteriorhodopsin measured with a tin-oxide electrode.Connectivity of the retinal Schiff base to Asp85 and Asp96 during the bacteriorhodopsin photocycle: the local-access modelOn the protein residues that control the yield and kinetics of O(630) in the photocycle of bacteriorhodopsinExperimental evidence for hydrogen-bonded network proton transfer in bacteriorhodopsin shown by Fourier-transform infrared spectroscopy using azide as catalyst.Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsin.Residue replacements of buried aspartyl and related residues in sensory rhodopsin I: D201N produces inverted phototaxis signals.Inversion of proton translocation in bacteriorhodopsin mutants D85N, D85T, and D85,96N.Chimeric proton-pumping rhodopsins containing the cytoplasmic loop of bovine rhodopsinIntermediate spectra and photocycle kinetics of the Asp96 --> asn mutant bacteriorhodopsin determined by singular value decomposition with self-modelingRemoval of transducer HtrI allows electrogenic proton translocation by sensory rhodopsin I.Light-driven proton or chloride pumping by halorhodopsin.Mechanism of light-dependent proton translocation by bacteriorhodopsin.Two light-transducing membrane proteins: bacteriorhodopsin and the mammalian rhodopsin.Bacterioopsin, haloopsin, and sensory opsin I of the halobacterial isolate Halobacterium sp. strain SG1: three new members of a growing family.
P2860
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P2860
Replacement of aspartic acid-96 by asparagine in bacteriorhodopsin slows both the decay of the M intermediate and the associated proton movement.
description
1989 nî lūn-bûn
@nan
1989 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
name
Replacement of aspartic acid-9 ...... he associated proton movement.
@ast
Replacement of aspartic acid-9 ...... he associated proton movement.
@en
type
label
Replacement of aspartic acid-9 ...... he associated proton movement.
@ast
Replacement of aspartic acid-9 ...... he associated proton movement.
@en
prefLabel
Replacement of aspartic acid-9 ...... he associated proton movement.
@ast
Replacement of aspartic acid-9 ...... he associated proton movement.
@en
P2093
P2860
P356
P1476
Replacement of aspartic acid-9 ...... he associated proton movement.
@en
P2093
A D Kaulen
H G Khorana
L A Drachev
V P Skulachev
P2860
P304
P356
10.1073/PNAS.86.7.2167
P407
P577
1989-04-01T00:00:00Z