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Volumn 72, Issue 5, 2000, Pages 714-718

Water and carboxyl group environments in the dehydration blueshift of bacteriorhodopsin

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIORHODOPSIN; CARBOXYL GROUP; CARBOXYLIC ACID; PROTON PUMP; SCHIFF BASE; WATER;

EID: 0034335267     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1562/0031-8655(2000)072<0714:WACGEI>2.0.CO;2     Document Type: Article
Times cited : (5)

References (27)
  • 1
    • 0031282975 scopus 로고    scopus 로고
    • Mechanism of ion transport across membranes. Bacteriorhodopsin as a prototype for proton pumps
    • Lanyi, J. K. (1997) Mechanism of ion transport across membranes. Bacteriorhodopsin as a prototype for proton pumps. J. Biol. Chem. 272, 31 209-31 212.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31209-31212
    • Lanyi, J.K.1
  • 3
    • 0018937951 scopus 로고
    • Effect of water on the structure of bacteriorhodopsin and photochemical processes in purple membranes
    • Lazarev, Y. and E. Terpugov (1980) Effect of water on the structure of bacteriorhodopsin and photochemical processes in purple membranes. Biochim. Biophys. Acta 590, 324-338.
    • (1980) Biochim. Biophys. Acta , vol.590 , pp. 324-338
    • Lazarev, Y.1    Terpugov, E.2
  • 4
    • 0000217440 scopus 로고
    • Role of water in bacteriorhodopsin's chromophore: Resonance Raman study
    • Hildebrandt, P. and M. Stockburger (1984) Role of water in bacteriorhodopsin's chromophore: resonance Raman study. Biochemistry 23, 5539-5548.
    • (1984) Biochemistry , vol.23 , pp. 5539-5548
    • Hildebrandt, P.1    Stockburger, M.2
  • 5
    • 0013124534 scopus 로고
    • Dehydration-induced molecular structural changes of purple membrane of Halobacterium halobium
    • Draheim, J., N. Gibson and J. Cassim (1988) Dehydration-induced molecular structural changes of purple membrane of Halobacterium halobium. Biophys. J. 54, 931-944.
    • (1988) Biophys. J. , vol.54 , pp. 931-944
    • Draheim, J.1    Gibson, N.2    Cassim, J.3
  • 6
    • 0029017477 scopus 로고
    • The role of water in retinal complexation to bacterio-opsin
    • Rousso, I., I. Grodsky, A. Lewis and M. Sheves (1995) The role of water in retinal complexation to bacterio-opsin. J. Biol. Chem. 270, 13 860-13 868.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13860-13868
    • Rousso, I.1    Grodsky, I.2    Lewis, A.3    Sheves, M.4
  • 7
    • 0030901231 scopus 로고    scopus 로고
    • The tertiary structural changes in bacteriorhodopsin occur between M states: X-ray diffraction and Fourier transform infrared spectroscopy
    • Sass, H. J., I. W. Schachowa, G. Rapp, M. H. J. Koch, D. Oesterhelt, N. A. Dencher and G. Büldt (1997) The tertiary structural changes in bacteriorhodopsin occur between M states: X-ray diffraction and Fourier transform infrared spectroscopy. EMBO J. 16, 1484-1491.
    • (1997) EMBO J. , vol.16 , pp. 1484-1491
    • Sass, H.J.1    Schachowa, I.W.2    Rapp, G.3    Koch, M.H.J.4    Oesterhelt, D.5    Dencher, N.A.6    Büldt, G.7
  • 8
    • 0017749540 scopus 로고
    • Hydration effects on the photocycle of bacteriorhodopsin in thin layers of purple membrane
    • Korenstein, R. and B. Hess (1977) Hydration effects on the photocycle of bacteriorhodopsin in thin layers of purple membrane. Nature 270, 184-186.
    • (1977) Nature , vol.270 , pp. 184-186
    • Korenstein, R.1    Hess, B.2
  • 10
    • 84989754368 scopus 로고
    • Cooperativity of the dehydration blue-shift of bacteriorhodopsin
    • Renthal, R. and R. Regalado (1991) Cooperativity of the dehydration blue-shift of bacteriorhodopsin. Photochem. Photobiol. 54, 931-935.
    • (1991) Photochem. Photobiol. , vol.54 , pp. 931-935
    • Renthal, R.1    Regalado, R.2
  • 11
    • 0025877453 scopus 로고
    • Protein hydration and function
    • Rupley, J. A. and G. Careri (1991) Protein hydration and function. Adv. Protein Chem. 41, 37-172.
    • (1991) Adv. Protein Chem. , vol.41 , pp. 37-172
    • Rupley, J.A.1    Careri, G.2
  • 12
    • 0016376428 scopus 로고
    • Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane
    • Oesterhelt, D. and W. Stoeckenius (1974) Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane. Methods Enzymol. 31, 667-678.
    • (1974) Methods Enzymol. , vol.31 , pp. 667-678
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 13
    • 0023086126 scopus 로고
    • Infrared studies of water induced conformational changes in bacteriorhodopsin
    • Varo, G. and L. Eisenstein (1987) Infrared studies of water induced conformational changes in bacteriorhodopsin. Eur. Biophys. J. 14, 63-168.
    • (1987) Eur. Biophys. J. , vol.14 , pp. 63-168
    • Varo, G.1    Eisenstein, L.2
  • 14
    • 0026717983 scopus 로고
    • Structures of aspartic acid-96 in the L and N intermediates of bacterio-rhodopsin: Analysis by Fourier transform infrared spectroscopy
    • Maeda, A., J. Sasaki, Y. Shichida, T. Yoshizawa, M. Chang, B. Ni, R. Needleman and J. K. Lanyi (1992) Structures of aspartic acid-96 in the L and N intermediates of bacterio-rhodopsin: analysis by Fourier transform infrared spectroscopy. Biochemistry 31, 4684-4690.
    • (1992) Biochemistry , vol.31 , pp. 4684-4690
    • Maeda, A.1    Sasaki, J.2    Shichida, Y.3    Yoshizawa, T.4    Chang, M.5    Ni, B.6    Needleman, R.7    Lanyi, J.K.8
  • 15
    • 0026602025 scopus 로고
    • Water structural changes in the bacteriorhodopsin photocycle: Analysis by Fourier transform infrared spectroscopy
    • Maeda, A., J. Sasaki, Y. Shichida and T. Yoshizawa (1992) Water structural changes in the bacteriorhodopsin photocycle: analysis by Fourier transform infrared spectroscopy. Biochemistry 31, 462-467.
    • (1992) Biochemistry , vol.31 , pp. 462-467
    • Maeda, A.1    Sasaki, J.2    Shichida, Y.3    Yoshizawa, T.4
  • 16
    • 0033529250 scopus 로고    scopus 로고
    • Chromophore-protein-water interactions in the L intermediate of bacteriorhodopsin: FTIR study of the photoreaction of L at 80 K
    • Maeda, A., F. Tomson, R. Gennis, T. Ebrey and S. Balashov (1999) Chromophore-protein-water interactions in the L intermediate of bacteriorhodopsin: FTIR study of the photoreaction of L at 80 K. Biochemistry 38, 8800-8807.
    • (1999) Biochemistry , vol.38 , pp. 8800-8807
    • Maeda, A.1    Tomson, F.2    Gennis, R.3    Ebrey, T.4    Balashov, S.5
  • 17
    • 0028279038 scopus 로고
    • Interaction of aspartate-85 with a water molecule and the protonated Schiff base in the L intermediate of bacteriorhodopsin: A Fourier-transform infrared spectroscopic study
    • Maeda, A., J. Sasakei, Y. Yamazaki, R. Needleman and J. K. Lanyi (1994) Interaction of aspartate-85 with a water molecule and the protonated Schiff base in the L intermediate of bacteriorhodopsin: a Fourier-transform infrared spectroscopic study. Biochemistry 33, 1713-1717.
    • (1994) Biochemistry , vol.33 , pp. 1713-1717
    • Maeda, A.1    Sasakei, J.2    Yamazaki, Y.3    Needleman, R.4    Lanyi, J.K.5
  • 18
    • 0030235615 scopus 로고    scopus 로고
    • Dehydration effects on D96N bactedorhodopsin films
    • Dyukova, T. and E. Lukashev (1996) Dehydration effects on D96N bactedorhodopsin films. Thin Solid Films 283, 1-4.
    • (1996) Thin Solid Films , vol.283 , pp. 1-4
    • Dyukova, T.1    Lukashev, E.2
  • 20
    • 0029883202 scopus 로고    scopus 로고
    • Hydrogen bonds of water and C=O groups coordinate long-range structural changes in the L photointermediate of bacteriorhodopsin
    • Yamazaki, Y., S. Tuzi, H. Saito, H. Kandori, R. Needleman, J. K. Lanyi and A. Maeda (1996) Hydrogen bonds of water and C=O groups coordinate long-range structural changes in the L photointermediate of bacteriorhodopsin. Biochemistry 35, 4063-4068.
    • (1996) Biochemistry , vol.35 , pp. 4063-4068
    • Yamazaki, Y.1    Tuzi, S.2    Saito, H.3    Kandori, H.4    Needleman, R.5    Lanyi, J.K.6    Maeda, A.7
  • 21
    • 0032502007 scopus 로고    scopus 로고
    • Inter-action of the protonated Schiff base with the peptide backbone of Valine 49 and the intervening water molecule in the N photointermediate of bacteriorhodopsin
    • Yamazaki, Y., H. Kandori, R. Needleman, J. K. Lanyi and A. Maeda (1998) Inter-action 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, 1559-1564.
    • (1998) Biochemistry , vol.37 , pp. 1559-1564
    • Yamazaki, Y.1    Kandori, H.2    Needleman, R.3    Lanyi, J.K.4    Maeda, A.5
  • 22
    • 0033536594 scopus 로고    scopus 로고
    • Structural changes in bacteriorhodopsin during ion transport at 2 Angstrom resolution
    • Luecke, H., B. Schobert, H.-T. Richter, J.-P. Cartailler and J. K. Lanyi (1999) Structural changes in bacteriorhodopsin during ion transport at 2 Angstrom resolution. Science 286, 255-260.
    • (1999) Science , vol.286 , pp. 255-260
    • Luecke, H.1    Schobert, B.2    Richter, H.-T.3    Cartailler, J.-P.4    Lanyi, J.K.5
  • 23
    • 0014952536 scopus 로고
    • Spectroscopic model for the visual pigments. Influence of microenvironmental polarizability
    • Irving, C. S., G. W. Byers and P. A. Leermakers (1970) Spectroscopic model for the visual pigments. Influence of microenvironmental polarizability. Biochemistry 9, 858-864.
    • (1970) Biochemistry , vol.9 , pp. 858-864
    • Irving, C.S.1    Byers, G.W.2    Leermakers, P.A.3
  • 24
    • 0032544345 scopus 로고    scopus 로고
    • Mechanisms of spectral tuning in blue cone visual pigments. Visible and Raman spectroscopy of blue-shifted rhodopsin mutants
    • Lin, S. W., G. G. Kochendoerfer, K. S. Carroll, D. Wang, R. A. Mathies and T. P. Sakmar (1998) Mechanisms of spectral tuning in blue cone visual pigments. Visible and Raman spectroscopy of blue-shifted rhodopsin mutants. J. Biol. Chem. 273, 24 533-24 591.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24533-24591
    • Lin, S.W.1    Kochendoerfer, G.G.2    Carroll, K.S.3    Wang, D.4    Mathies, R.A.5    Sakmar, T.P.6
  • 26
    • 0034620606 scopus 로고    scopus 로고
    • Origins of deuterium kinetic isotope effects on the proton transfers of the bacteriorhodopsin photocycle
    • Brown, L. S., R. Needleman and J. K. Lanyi (2000) Origins of deuterium kinetic isotope effects on the proton transfers of the bacteriorhodopsin photocycle. Biochemistry 39, 938-945.
    • (2000) Biochemistry , vol.39 , pp. 938-945
    • Brown, L.S.1    Needleman, R.2    Lanyi, J.K.3
  • 27
    • 0025298852 scopus 로고
    • Water molecules and exchangeable hydrogen ions at the active center of bacteriorhodopsin localized by neutron diffraction. Elements of the proton pathway?
    • Papadopoulos, G., N. A. Dencher, G. Zaccai and G. Büldt (1990) Water molecules and exchangeable hydrogen ions at the active center of bacteriorhodopsin localized by neutron diffraction. Elements of the proton pathway? J. Mol. Biol. 214, 15-19.
    • (1990) J. Mol. Biol. , vol.214 , pp. 15-19
    • Papadopoulos, G.1    Dencher, N.A.2    Zaccai, G.3    Büldt, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.