A large photolysis-induced pKa increase of the chromophore counterion in bacteriorhodopsin: implications for ion transport mechanisms of retinal proteins.
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Specific neosaxitoxin interactions with the Na+ channel outer vestibule determined by mutant cycle analysis.Deformation of helix C in the low temperature L-intermediate of bacteriorhodopsinFactors influencing the energetics of electron and proton transfers in proteins. What can be learned from calculations.Progress toward an explicit mechanistic model for the light-driven pump, bacteriorhodopsin.Evidence that aspartate-85 has a higher pK(a) in all-trans than in 13-cisbacteriorhodopsin.Two groups control light-induced Schiff base deprotonation and the proton affinity of Asp85 in the Arg82 his mutant of bacteriorhodopsin.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.Structure changes upon deprotonation of the proton release group in the bacteriorhodopsin photocycle.Transport bicycles.In situ determination of transient pKa changes of internal amino acids of bacteriorhodopsin by using time-resolved attenuated total reflection Fourier-transform infrared spectroscopyPhotocycle of Exiguobacterium sibiricum rhodopsin characterized by low-temperature trapping in the IR and time-resolved studies in the visibleGloeobacter rhodopsin, limitation of proton pumping at high electrochemical loadCoordinating the structural rearrangements associated with unidirectional proton transfer in the bacteriorhodopsin photocycle induced by deprotonation of the proton-release group: a time-resolved difference FTIR spectroscopic study.Structural changes due to the deprotonation of the proton release group in the M-photointermediate of bacteriorhodopsin as revealed by time-resolved FTIR spectroscopy.A role for internal water molecules in proton affinity changes in the Schiff base and Asp85 for one-way proton transfer in bacteriorhodopsin.Chloride ion binding to bacteriorhodopsin at low pH: an infrared spectroscopic study.Time-resolved step-scan Fourier transform infrared spectroscopy reveals differences between early and late M intermediates of bacteriorhodopsin.Properties of the stochastic energization-relaxation channel model for vectorial ion transport.Fourier transform infrared evidence for early deprotonation of Asp(85) at alkaline pH in the photocycle of bacteriorhodopsin mutants containing E194Q.Mechanism of ion transport across membranes. Bacteriorhodopsin as a prototype for proton pumps.Evidence for the first phase of the reprotonation switch of bacteriorhodopsin from time-resolved photovoltage and flash photolysis experiments on the photoreversal of the M-intermediate.Bacteriorhodopsin-like channelrhodopsins: Alternative mechanism for control of cation conductance.
P2860
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P2860
A large photolysis-induced pKa increase of the chromophore counterion in bacteriorhodopsin: implications for ion transport mechanisms of retinal proteins.
description
1996 nî lūn-bûn
@nan
1996 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
A large photolysis-induced pKa ...... echanisms of retinal proteins.
@ast
A large photolysis-induced pKa ...... echanisms of retinal proteins.
@en
type
label
A large photolysis-induced pKa ...... echanisms of retinal proteins.
@ast
A large photolysis-induced pKa ...... echanisms of retinal proteins.
@en
prefLabel
A large photolysis-induced pKa ...... echanisms of retinal proteins.
@ast
A large photolysis-induced pKa ...... echanisms of retinal proteins.
@en
P2093
P2860
P1433
P1476
A large photolysis-induced pKa ...... echanisms of retinal proteins.
@en
P2093
A K Dioumaev
M S Braiman
P2860
P304
P356
10.1016/S0006-3495(96)79637-6
P407
P577
1996-02-01T00:00:00Z