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Importance of bound divalent cations to the tyrosine deprotonation during the photocycle of bacteriorhodopsin.
Proc Natl Acad Sci U S A. 1985 Jun;82(11):3662-4. doi: 10.1073/pnas.82.11.3662.
2
On the molecular mechanisms of the Schiff base deprotonation during the bacteriorhodopsin photocycle.
Proc Natl Acad Sci U S A. 1986 Nov;83(22):8580-4. doi: 10.1073/pnas.83.22.8580.
3
Effect of genetic modification of tyrosine-185 on the proton pump and the blue-to-purple transition in bacteriorhodopsin.
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4
Redshift of the purple membrane absorption band and the deprotonation of tyrosine residues at high pH: Origin of the parallel photocycles of trans-bacteriorhodopsin.
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5
Evidence for the involvement of more than one metal cation in the Schiff base deprotonation process during the photocycle of bacteriorhodopsin.
Proc Natl Acad Sci U S A. 1987 Jun;84(12):4094-8. doi: 10.1073/pnas.84.12.4094.
6
Photoreactions of bacteriorhodopsin at acid pH.
Biophys J. 1989 Dec;56(6):1143-51. doi: 10.1016/S0006-3495(89)82761-4.
7
Substitution of amino acids Asp-85, Asp-212, and Arg-82 in bacteriorhodopsin affects the proton release phase of the pump and the pK of the Schiff base.
Proc Natl Acad Sci U S A. 1990 Feb;87(3):1018-22. doi: 10.1073/pnas.87.3.1018.
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Interaction between Asp-85 and the proton-releasing group in bacteriorhodopsin. A study of an O-like photocycle intermediate.
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9
Effects of tyrosine-26 and tyrosine-64 nitration on the photoreactions of bacteriorhodopsin.
Biochemistry. 1985 Dec 17;24(26):7733-40. doi: 10.1021/bi00347a035.
10
Cation binding by bacteriorhodopsin.
Proc Natl Acad Sci U S A. 1985 Jan;82(2):396-400. doi: 10.1073/pnas.82.2.396.
引用本文的文献
1
Nature of the individual Ca binding sites in Ca-regenerated bacteriorhodopsin.
Biophys J. 1992 May;61(5):1201-6. doi: 10.1016/S0006-3495(92)81929-X.
2
Evidence for the involvement of more than one metal cation in the Schiff base deprotonation process during the photocycle of bacteriorhodopsin.
Proc Natl Acad Sci U S A. 1987 Jun;84(12):4094-8. doi: 10.1073/pnas.84.12.4094.
3
On the molecular mechanisms of the Schiff base deprotonation during the bacteriorhodopsin photocycle.
Proc Natl Acad Sci U S A. 1986 Nov;83(22):8580-4. doi: 10.1073/pnas.83.22.8580.
4
Comparison of the dynamics of the primary events of bacteriorhodopsin in its trimeric and monomeric states.
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5
Specific binding sites for cations in bacteriorhodopsin.
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6
Time-resolved Fourier transform infrared spectroscopy of the polarizable proton continua and the proton pump mechanism of bacteriorhodopsin.
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7
Binding of calcium ions to bacteriorhodopsin.
Biophys J. 1999 Jun;76(6):3219-26. doi: 10.1016/S0006-3495(99)77473-4.
8
Cation binding sites on the projected structure of bacteriorhodopsin.
Biophys J. 1986 Aug;50(2):277-84. doi: 10.1016/S0006-3495(86)83461-0.
9
Deprotonation of lipid-depleted bacteriorhodopsin.
Proc Natl Acad Sci U S A. 1988 Aug;85(16):5918-22. doi: 10.1073/pnas.85.16.5918.
10
Tryptophan fluorescence quenching as a monitor for the protein conformation changes occurring during the photocycle of bacteriorhodopsin under different perturbations.
Proc Natl Acad Sci U S A. 1989 Aug;86(15):5815-9. doi: 10.1073/pnas.86.15.5815.
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Effect of iodination of the purple membrane on the photocycle of bacteriorhodopsin.
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The role of tyrosine residues in the function of bacteriorhodopsin. Specific nitration of tyrosine 26.
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Light-dependent nitration of bacteriorhodopsin.
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On the protein (tyrosine)-chromophore (protonated Schiff base) coupling in bacteriorhodopsin.
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Salt and pH-dependent changes of the purple membrane absorption spectrum.
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Bacteriorhodopsin and related pigments of halobacteria.
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Rhodopsin-like protein from the purple membrane of Halobacterium halobium.
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Photoreceptor protein from the purple membrane of Halobacterium halobium. Molecular weight and retinal binding site.
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Bacteriorhodopsin: a light-driven proton pump in Halobacterium Halobium.
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Analogies between respiration and a light-driven proton pump as sources of energy for active glutamate transport in Halobacterium holobium.
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