Relationship of proton uptake on the cytoplasmic surface and reisomerization of the retinal in the bacteriorhodopsin photocycle: an attempt to understand the complex kinetics of the pH changes and the N and O intermediates.
about
Glutamic acid 204 is the terminal proton release group at the extracellular surface of bacteriorhodopsin.Kinetic and thermodynamic study of the bacteriorhodopsin photocycle over a wide pH range.Membrane potential stabilizes the O intermediate in liposomes containing bacteriorhodopsin.Molecular mechanism of protein-retinal coupling in bacteriorhodopsin.The role of water in the extracellular half channel of bacteriorhodopsin.Mutation of a surface residue, lysine-129, reverses the order of proton release and uptake in bacteriorhodopsin; guanidine hydrochloride restores itProton binding within a membrane protein by a protonated water clusterReversal of the surface charge asymmetry in purple membrane due to single amino acid substitutions.The residues Leu 93 and Asp 96 act independently in the bacteriorhodopsin photocycle: studies with the leu 93-->Ala, Asp 96-->Asn double mutant.Functional significance of a protein conformation change at the cytoplasmic end of helix F during the bacteriorhodopsin photocycle.Relationship of proton release at the extracellular surface to deprotonation of the schiff base in the bacteriorhodopsin photocycleElectric signals during the bacteriorhodopsin photocycle, determined over a wide pH range.On the protein residues that control the yield and kinetics of O(630) in the photocycle of bacteriorhodopsinTrapping and spectroscopic identification of the photointermediates of bacteriorhodopsin at low temperatures.pH dependence of light-driven proton pumping by an archaerhodopsin from Tibet: comparison with bacteriorhodopsin.Structure changes upon deprotonation of the proton release group in the bacteriorhodopsin photocycle.In situ determination of transient pKa changes of internal amino acids of bacteriorhodopsin by using time-resolved attenuated total reflection Fourier-transform infrared spectroscopyReducing the flexibility of retinal restores a wild-type-like photocycle in bacteriorhodopsin mutants defective in protein-retinal couplingBreaking the carboxyl rule: lysine 96 facilitates reprotonation of the Schiff base in the photocycle of a retinal protein from Exiguobacterium sibiricum.Titration of aspartate-85 in bacteriorhodopsin: what it says about chromophore isomerization and proton release.Initial photophysical characterization of the proteorhodopsin optical proton sensor (PROPS).
P2860
Q30417307-76FFE0CD-F062-4A55-89E5-79F7B4578A89Q30432028-78258126-BFF1-4A90-9CE2-04B76232AE78Q30784822-BAE9E297-0D67-4CCC-8E27-EC880480EDCEQ33757959-DE9F9700-79AC-4CBE-B533-05C967C2AB1CQ33907847-C54F4673-26F4-45DE-861D-F24D8A92B6A0Q33916909-C89A8FB1-1E74-42FD-BD33-BA7192EE55E0Q33928561-AC5B02E5-F5EF-4519-80D6-DADC953E8E63Q34017784-003B32EC-83CD-440B-A201-AEA77CABDD95Q34017789-9F68DB4C-72B8-4786-BB41-E93E91D38159Q34047640-218BF864-655E-4039-91F5-FA36F0CAB0E6Q34129210-7B4FFB62-51EB-4C20-BD0E-E8F8AF138340Q34169662-E4AAB77F-A90B-4034-8E8F-30AAD3B388E1Q34172227-D0332146-DF35-4031-9DED-D8DEF4F33090Q34257544-92C6ADC1-5F1C-44B3-B763-7ECC0E056CE6Q34524582-FC1AFB03-57A0-4FE6-94B1-242463B1F232Q36150767-B1D6BE17-A8A2-443D-864B-1BE1711FA3AAQ36354305-79B6D790-ABB4-4589-8C9A-458A1A925224Q36764554-2770CB3B-2CE2-47E3-8A7E-C3DD667101F1Q37175176-C1E7D175-B93E-4565-A2D3-12276015AB73Q41945254-AF763353-584B-4E2F-BEF3-849C4DA3DF20Q42581452-1E1FA87B-E757-4084-99B2-42C963A615E7
P2860
Relationship of proton uptake on the cytoplasmic surface and reisomerization of the retinal in the bacteriorhodopsin photocycle: an attempt to understand the complex kinetics of the pH changes and the N and O intermediates.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年学术文章
@wuu
1993年学术文章
@zh
1993年学术文章
@zh-cn
1993年学术文章
@zh-hans
1993年学术文章
@zh-my
1993年学术文章
@zh-sg
1993年學術文章
@yue
1993年學術文章
@zh-hant
name
Relationship of proton uptake ...... and the N and O intermediates.
@en
Relationship of proton uptake ...... and the N and O intermediates.
@nl
type
label
Relationship of proton uptake ...... and the N and O intermediates.
@en
Relationship of proton uptake ...... and the N and O intermediates.
@nl
prefLabel
Relationship of proton uptake ...... and the N and O intermediates.
@en
Relationship of proton uptake ...... and the N and O intermediates.
@nl
P2093
P356
P1433
P1476
Relationship of proton uptake ...... and the N and O intermediates.
@en
P2093
P304
10239-10248
P356
10.1021/BI00089A046
P407
P577
1993-09-01T00:00:00Z