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General concept for ion translocation by halobacterial retinal proteins: The isomerization/switch/transfer (IST) model
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of outstanding interest. The authors present a conceptual framework model for the intriguing experimental observation that retinal proteins can change vectoriality and ion specificity. The key feature of the model is that the isomerization (I) of retinal triggers a change in the accessibility of the active center (S), as well as ion transfer (T), and that both compete kinetically.
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Haupts U, Tittor J, Bamberg E, Oesterhelt D. General concept for ion translocation by halobacterial retinal proteins: the isomerization/switch/transfer (IST) model. of outstanding interest Biochemistry. 36:1997;2-7 The authors present a conceptual framework model for the intriguing experimental observation that retinal proteins can change vectoriality and ion specificity. The key feature of the model is that the isomerization (I) of retinal triggers a change in the accessibility of the active center (S), as well as ion transfer (T), and that both compete kinetically.
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Haupts, U.1
Tittor, J.2
Bamberg, E.3
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Intramembrane signaling mediated by hydrogen-bonding of water and carboxyl groups in bacteriorhodopsin and rhodopsin
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Maeda A, Kandori H, Yamazaki Y, Nishimura S, Hatanaka M, Chon Y-S, Sasaki J, Needleman R, Lanyi JK. Intramembrane signaling mediated by hydrogen-bonding of water and carboxyl groups in bacteriorhodopsin and rhodopsin. J Biochem. 121:1997;399-406.
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Lanyi, J.K.1
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Surface of bacteriorhodopsin revealed by high-resolution electron crystallography
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of special interest. Electron crystallographic data on the purple membrane are extended to 3 Å and the structural model contains all the interhelical loops.
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Kimura Y, Vassylyev DG, Miyazawa A, Kidera A, Matsushima M, Mitsuoka K, Murata K, Hirai T, Fujiyoshi Y. Surface of bacteriorhodopsin revealed by high-resolution electron crystallography. of special interest Nature. 389:1997;206-211 Electron crystallographic data on the purple membrane are extended to 3 Å and the structural model contains all the interhelical loops.
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Mitsuoka, K.6
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Hirai, T.8
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X-ray structure of bacteriorhodopsin at 2.5 Å from microcrystals grown in lipidic cubic phases
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of special interest. This new method for crystallizing membrane proteins has the potential to improve the resolution of the bacteriorhodopsin structure
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Pebay-Peyroula, E.1
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Neutron diffraction on purple membranes. Essential water molecules in the light-driven proton pump bacteriorhodopsin
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Experimental evidence for hydrogen-bonded network proton transfer in bacteriorhodopsin shown by Fourier transform infrared spectroscopy using azide as catalyst
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Existence of a proton transfer chain in bacteriorhodopsin: Participation of glu-194 in the release of protons to the extracellular surface
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Dioumaev AK, Richter H-T, Brown LS, Tanio M, Tuzi S, Saitô H, Kimura Y, Needleman R, Lanyi JK. Existence of a proton transfer chain in bacteriorhodopsin: participation of glu-194 in the release of protons to the extracellular surface. Biochemistry. 37:1998;2496-2506.
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Localization and orientation of functional water molecules in bacteriorhodopsin as revealed by polarized Fourier transform infrared spectroscopy
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Time-resolved titrations of the Schiff base and of the asp-85 residue artificial bacteriorhodopsin
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Druckmann, S.1
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Sheves, M.5
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0032502007
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Interaction of the protonated Schiff base with the peptide backbone of valine 49 and the intervening water molecule in the N photointermediate of bacteriorhodopsin
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Yamazaki Y, Kandori H, Needleman R, Lanyi JK, Maeda A. Interaction of the protonated Schiff base with the peptide backbone of valine 49 and the intervening water molecule in the N photointermediate of bacteriorhodopsin. Biochemistry. 37:1997;1559-1564.
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Yamazaki, Y.1
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Maeda, A.5
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0030823236
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Picosecond molecular motions in bacteriorhodopsin from neutron scattering
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of special interest. The authors make use of the potential of neutron scattering experiments to analyze for the first time ground state motions in bacteriorhodopsin. This provides a basis for new theoretical studies.
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Fitter J, Lechner RE, Dencher NA. Picosecond molecular motions in bacteriorhodopsin from neutron scattering. of special interest Biophys J. 73:1997;2126-2137 The authors make use of the potential of neutron scattering experiments to analyze for the first time ground state motions in bacteriorhodopsin. This provides a basis for new theoretical studies.
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Fitter, J.1
Lechner, R.E.2
Dencher, N.A.3
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0032574723
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2H-labelling and neutron scattering
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of special interest. Using differential isotope labeling, the chromophore and the residual structure were analyzed for their ground state dynamics. The resulting statement of a hard core in a soft shell has implications for the functional dynamics for the ion-transport process.
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2H-labelling and neutron scattering. of special interest Proc Natl Acad Sci USA. 95:1998;4970-4975 Using differential isotope labeling, the chromophore and the residual structure were analyzed for their ground state dynamics. The resulting statement of a hard core in a soft shell has implications for the functional dynamics for the ion-transport process.
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Proc Natl Acad Sci USA
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Real, V.1
Patzelt, H.2
Ferrand, M.3
Pfister, C.4
Oesterhelt, D.5
Zaccai, G.6
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20
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Interactions between the protonated Schiff base and its counterion in the photointermediates of bacteriorhodopsin
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Hu JG, Griffin RG, Herzfeld J. Interactions between the protonated Schiff base and its counterion in the photointermediates of bacteriorhodopsin. J Am Chem Soc. 119:1997;9495-9498.
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Hu, J.G.1
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Herzfeld, J.3
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22
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0002659282
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Towards structural investigation on isotope labelled native bacteriorhodopsin in detergent micelles by solution-state NMR spectroscopy
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Patzelt H, Ulrich AS, Egbringhoff H, Düx P, Ashurst J, Simon B, Oschkinat H, Oesterhelt D. Towards structural investigation on isotope labelled native bacteriorhodopsin in detergent micelles by solution-state NMR spectroscopy. J Biomol NMR. 10:1997;95-106.
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Egbringhoff, H.3
Düx, P.4
Ashurst, J.5
Simon, B.6
Oschkinat, H.7
Oesterhelt, D.8
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23
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0030866067
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Ultraviolet resonance Raman spectra of trp-182 and trp-189 in bacteriorhodopsin: Novel information on the structure of trp-182 and its steric interaction with retinal
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Hashimoto S, Obata K, Takeuchi H, Needleman R, Lanyi JK. Ultraviolet resonance Raman spectra of trp-182 and trp-189 in bacteriorhodopsin: novel information on the structure of trp-182 and its steric interaction with retinal. Biochemistry. 36:1997;11583-11590.
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Biochemistry
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Hashimoto, S.1
Obata, K.2
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Needleman, R.4
Lanyi, J.K.5
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24
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0030913277
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Threonine-89 participates in the active site of bacteriorhodopsin: Evidence for a role in color regulation and Schiff base proton transfer
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Russell, T.S.1
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0032549731
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Gai, F.1
Hasson, K.C.2
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27
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Redetermination of the quantum yield of photoisomerization and energy content in the K-intermediate of bacteriorhodopsin photocycle and its mutants by the photoacoustic technique
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of special interest. The authors independently redetermine and reconfirm the essential thermodynamic parameters of bacteriorhodopsin.
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Logunov, S.L.1
El-Sayed, M.A.2
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Structure at 0.85 Å resolution of an early protein photocycle intermediate
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of outstanding interest. The analysis of the functionally important structural dynamics of a photoreceptor by combining high resolution X-ray structural analysis with cryotrapping techniques. This is a first example of the structural analysis of an intermediate of the trans to cis isomerization of a C=C double bond in a chromoprotein.
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Genick UK, Soltis SM, Kuhn P, Canestrelli IL, Getzoff ED. Structure at 0.85 Å resolution of an early protein photocycle intermediate. of outstanding interest Nature. 392:1998;206-209 The analysis of the functionally important structural dynamics of a photoreceptor by combining high resolution X-ray structural analysis with cryotrapping techniques. This is a first example of the structural analysis of an intermediate of the trans to cis isomerization of a C=C double bond in a chromoprotein.
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Nature
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The tertiary structural changes in bacteriorhodopsin occur between M states: X-ray diffraction and Fourier transform infrared spectroscopy
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Sass HJ, Schachowa IW, Rapp G, Koch MHJ, Oesterhelt D, Dencher NA, Büldt G. The tertiary structural changes in bacteriorhodopsin occur between M states: X-ray diffraction and Fourier transform infrared spectroscopy. EMBO J. 16:1997;1484-1491.
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Oesterhelt, D.5
Dencher, N.A.6
Büldt, G.7
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34
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Evidence for charge controlled conformational changes in the photocycle of bacteriorhodopsin
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of special interest. A cytoplasmic surface mutation in bacteriorhodopsin inhibits the reprotonation of the active center, indicating cooperativity in the cytoplasmic half channel.
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Sass HJ, Gessenich R, Koch MHJ, Oesterhelt D, Dencher NA, Büldt G, Rapp G. Evidence for charge controlled conformational changes in the photocycle of bacteriorhodopsin. of special interest Biophys J. 75:1998;399-405 A cytoplasmic surface mutation in bacteriorhodopsin inhibits the reprotonation of the active center, indicating cooperativity in the cytoplasmic half channel.
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Gessenich, R.2
Koch, M.H.J.3
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Dencher, N.A.5
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Rapp, G.7
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The last phase of the reprotonation switch in bacteriorhodopsin: The transition between the M-type and the N-type protein conformation depends on hydration
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Lanyi, J.K.5
Kataoka, M.6
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Structure and hydration of the M-state of the bacteriorhodopsin mutant D96N studied by neutron diffraction
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A local electrostatic change is the cause of the large-scale protein conformation shift in bacteriorhodopsin
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Kataoka, M.4
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Lanyi, J.K.8
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Reconstitution of bacteriorhodopsin from the apoprotein and retinal studied by Fourier transform infrared spectroscopy
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0030770570
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2 transition
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of special interest. The authors use the photochemical back reaction from the M state to the initial state in the FTIR analysis of M substates with different photochemical properties. This is the first time-resolved FTIR study of these M substates.
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2 transition. of special interest Biophys J. 73:1997;2071-2080 The authors use the photochemical back reaction from the M state to the initial state in the FTIR analysis of M substates with different photochemical properties. This is the first time-resolved FTIR study of these M substates.
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Biophys J
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Hessling, B.1
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Time-resolved detection of structural changes during the photocycle of spin-labeled bacteriorhodopsin
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Spin-labeling studies of the conformational changes in the vicinity of D36, D38, T46, and E161 of bacteriorhodopsin during the photocycle
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Rink T, Riesle J, Oesterhelt D, Gerwert K, Steinhoff H-J. Spin-labeling studies of the conformational changes in the vicinity of D36, D38, T46, and E161 of bacteriorhodopsin during the photocycle. Biophys J. 73:1997;983-993.
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