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Volumn 82, Issue 6, 2006, Pages 1398-1405

Water as a cofactor in the unidirectional light-driven proton transfer steps in bacteriorhodopsin

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIORHODOPSIN; PROTON; WATER;

EID: 33846467755     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1562/2006-01-16-IR-779     Document Type: Review
Times cited : (17)

References (82)
  • 2
    • 0029903197 scopus 로고    scopus 로고
    • Electron-crystallographic refinement of the structure of bacteriorhodopsin
    • Grigorieff, N., T. A. Ceska, K. H. Downing, J. M. Baldwin and R. Henderson (1996) Electron-crystallographic refinement of the structure of bacteriorhodopsin. J. Mol. Biol. 259, 393-421.
    • (1996) J. Mol. Biol , vol.259 , pp. 393-421
    • Grigorieff, N.1    Ceska, T.A.2    Downing, K.H.3    Baldwin, J.M.4    Henderson, R.5
  • 4
    • 0020008581 scopus 로고
    • Raman spectra of bacteriorhodopsin's primary photoproduct: Evidence for a distorted 13-cis retinal chromophore
    • Braiman, M. and R. Mathies (1982) Raman spectra of bacteriorhodopsin's primary photoproduct: Evidence for a distorted 13-cis retinal chromophore. Proc. Natl. Acad. Sci. USA 79, 403-407.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 403-407
    • Braiman, M.1    Mathies, R.2
  • 5
    • 0016723355 scopus 로고
    • Bacteriorhodopsin: A light-driven proton pump in Halobacterium halobium
    • Lozier, R. H., R. A. Bogomolni and W. Stoeckenius (1975) Bacteriorhodopsin: A light-driven proton pump in Halobacterium halobium. Biophys. J. 15, 955-963.
    • (1975) Biophys. J , vol.15 , pp. 955-963
    • Lozier, R.H.1    Bogomolni, R.A.2    Stoeckenius, W.3
  • 6
    • 0000005909 scopus 로고
    • Time-resolved step-scan FT-IR investigations of the transition from KL to L in the bacteriorhodopsin photocycle: Identification of chromophore twist by assigning hydrogen-out-of-plane (HOOP) bending vibrations
    • Weidlich, O. and F. Siebert (1993) Time-resolved step-scan FT-IR investigations of the transition from KL to L in the bacteriorhodopsin photocycle: Identification of chromophore twist by assigning hydrogen-out-of-plane (HOOP) bending vibrations. Appl. Spectrosc. 47, 1394-1399.
    • (1993) Appl. Spectrosc , vol.47 , pp. 1394-1399
    • Weidlich, O.1    Siebert, F.2
  • 7
    • 0027478957 scopus 로고
    • Time-resolved infrared spectral analysis of the KL-to-L conversion in the photocycle of bacteriorhodopsin
    • Sasaki, J., A. Maeda, C. Kato and H. Hamaguchi (1993) Time-resolved infrared spectral analysis of the KL-to-L conversion in the photocycle of bacteriorhodopsin. Biochemistry 32, 867-871.
    • (1993) Biochemistry , vol.32 , pp. 867-871
    • Sasaki, J.1    Maeda, A.2    Kato, C.3    Hamaguchi, H.4
  • 8
    • 0028944068 scopus 로고
    • Nanosecond time-resolved infrared spectroscopy distinguishes two K species in the bacteriorhodopsin photocycle
    • Sasaki, J., T. Yuzawa, H. Kandori, A. Maeda and H. Hamaguchi (1995) Nanosecond time-resolved infrared spectroscopy distinguishes two K species in the bacteriorhodopsin photocycle. Biophys. J. 68, 2073-2080.
    • (1995) Biophys. J , vol.68 , pp. 2073-2080
    • Sasaki, J.1    Yuzawa, T.2    Kandori, H.3    Maeda, A.4    Hamaguchi, H.5
  • 9
    • 33751156797 scopus 로고    scopus 로고
    • Protein dynamics in the bacteriorhodopsin photocycle: A nanosecond step-scan FTIR investigation of the KL to L transition
    • Hage, W., M. Kim, H. Frei and R. A. Mathies (1996) Protein dynamics in the bacteriorhodopsin photocycle: A nanosecond step-scan FTIR investigation of the KL to L transition. J. Phys. Chem. 100, 16026-16033.
    • (1996) J. Phys. Chem , vol.100 , pp. 16026-16033
    • Hage, W.1    Kim, M.2    Frei, H.3    Mathies, R.A.4
  • 10
    • 0031075390 scopus 로고    scopus 로고
    • Two bathointermediates of the bacteriorhodopsin photocycle, distinguished by nanosecond time-resolved FTIR spectroscopy at room temperature
    • Dioumaev, A. K. and M. S. Braiman (1997) Two bathointermediates of the bacteriorhodopsin photocycle, distinguished by nanosecond time-resolved FTIR spectroscopy at room temperature. J. Phys. Chem. B 101, 1665-1672.
    • (1997) J. Phys. Chem. B , vol.101 , pp. 1665-1672
    • Dioumaev, A.K.1    Braiman, M.S.2
  • 12
    • 0025820289 scopus 로고
    • Thermodynamics and energy coupling in the bacteriorhodopsin photocycle
    • Váró, G. and J. K. Lanyi (1991) Thermodynamics and energy coupling in the bacteriorhodopsin photocycle. Biochemistry 30, 5016-5022.
    • (1991) Biochemistry , vol.30 , pp. 5016-5022
    • Váró, G.1    Lanyi, J.K.2
  • 14
    • 0021848415 scopus 로고
    • Determination of retinal chromophore structure in bacteriorhodopsin with resonance Raman spectroscopy
    • Smith, S. O., J. Lugtenburg and R. A. Mathies (1985) Determination of retinal chromophore structure in bacteriorhodopsin with resonance Raman spectroscopy. J. Membr. Biol. 85, 95-109.
    • (1985) J. Membr. Biol , vol.85 , pp. 95-109
    • Smith, S.O.1    Lugtenburg, J.2    Mathies, R.A.3
  • 15
    • 0025829307 scopus 로고
    • From femtoseconds to biology: Mechanism of bacteriorhodopsin's light-driven proton pump
    • Mathies, R. A., S. W. Lin, J. B. Ames and W. T. Pollard (1991) From femtoseconds to biology: Mechanism of bacteriorhodopsin's light-driven proton pump. Annu. Rev. Biophys. Biophys. Chem. 20, 491-518.
    • (1991) Annu. Rev. Biophys. Biophys. Chem , vol.20 , pp. 491-518
    • Mathies, R.A.1    Lin, S.W.2    Ames, J.B.3    Pollard, W.T.4
  • 17
    • 0032539982 scopus 로고    scopus 로고
    • Local-access model for proton transfer in bacteriorhodopsin
    • Brown, L. S., A. K. Dioumaev, R. Needleman and J. K. Lanyi (1998) Local-access model for proton transfer in bacteriorhodopsin. Biochemistry 37, 3982-3993.
    • (1998) Biochemistry , vol.37 , pp. 3982-3993
    • Brown, L.S.1    Dioumaev, A.K.2    Needleman, R.3    Lanyi, J.K.4
  • 18
    • 0024289369 scopus 로고
    • Vibrational spectroscopy of bacteriorhodopsin mutants: Light-driven proton transport involves protonation changes of aspartic acid residues 85, 96 and 212
    • Braiman, M. S., T. Mogi, T. Marti, L. J. Stern, H. G. Khorana and K. J. Rothschild (1988) Vibrational spectroscopy of bacteriorhodopsin mutants: Light-driven proton transport involves protonation changes of aspartic acid residues 85, 96 and 212. Biochemistry 27, 8516-8520.
    • (1988) Biochemistry , vol.27 , pp. 8516-8520
    • Braiman, M.S.1    Mogi, T.2    Marti, T.3    Stern, L.J.4    Khorana, H.G.5    Rothschild, K.J.6
  • 19
    • 0025629995 scopus 로고
    • Simultaneous monitoring of light-induced changes in protein side-group protonation, chromophore isomerization, and backbone motion of bacteriorhodopsin by time-resolved Fourier transform infrared spectroscopy
    • Gerwert, K., G. Souvignier and B. Hess (1990) Simultaneous monitoring of light-induced changes in protein side-group protonation, chromophore isomerization, and backbone motion of bacteriorhodopsin by time-resolved Fourier transform infrared spectroscopy. Proc. Natl. Acad. Sci. USA 87, 9774-9778.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 9774-9778
    • Gerwert, K.1    Souvignier, G.2    Hess, B.3
  • 20
    • 0026717983 scopus 로고
    • Structures of aspartic acid-96 in the L and N intermediates of bacteriorhodopsin: 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 bacteriorhodopsin: 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
  • 21
    • 0024707259 scopus 로고
    • Role of aspartate-96 in proton translocation by bacteriorhodopsin
    • Gerwert, K., B. Hess, J. Soppa and D. Oesterhelt (1989) Role of aspartate-96 in proton translocation by bacteriorhodopsin. Proc. Natl. Acad. Sci. USA 86, 4943-4947.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 4943-4947
    • Gerwert, K.1    Hess, B.2    Soppa, J.3    Oesterhelt, D.4
  • 22
    • 0025968915 scopus 로고
    • Protein dynamics in the bacteriorhodopsin photocycle: Submillisecond Fourier transform infrared spectra of the L, M, and N photointermediates
    • Braiman, M., O. Bousche and K. Rothschild (1991) Protein dynamics in the bacteriorhodopsin photocycle: Submillisecond Fourier transform infrared spectra of the L, M, and N photointermediates. Proc. Natl. Acad. Sci. USA 88, 2388-2392.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2388-2392
    • Braiman, M.1    Bousche, O.2    Rothschild, K.3
  • 23
    • 0346366810 scopus 로고    scopus 로고
    • Crystal structure of the L intermediate of bacteriorhodopsin: Evidence for vertical translocation of a water molecule during the proton pumping cycle
    • Kouyama, T., T. Nishikawa, T. Tokuhisa and H. Okumura (2004) Crystal structure of the L intermediate of bacteriorhodopsin: Evidence for vertical translocation of a water molecule during the proton pumping cycle. J. Mol. Biol. 335, 531-546.
    • (2004) J. Mol. Biol , vol.335 , pp. 531-546
    • Kouyama, T.1    Nishikawa, T.2    Tokuhisa, T.3    Okumura, H.4
  • 24
    • 17644426679 scopus 로고    scopus 로고
    • Relocation of water molecules between the Schiff base and the Thr46-Asp96 region during light-driven unidirectional proton transport by bacteriorhodopsin: An FTIR study of the N intermediate
    • Maeda, A., R. B. Gennis, S. P. Balashov and T. G. Ebrey (2005) Relocation of water molecules between the Schiff base and the Thr46-Asp96 region during light-driven unidirectional proton transport by bacteriorhodopsin: An FTIR study of the N intermediate. Biochemistry 44, 5960-5968.
    • (2005) Biochemistry , vol.44 , pp. 5960-5968
    • Maeda, A.1    Gennis, R.B.2    Balashov, S.P.3    Ebrey, T.G.4
  • 25
    • 33846519913 scopus 로고    scopus 로고
    • Participation of internal water molecules and clusters in the unidirectional light-induced proton transfer in bacteriorhodopsin
    • Edited by M. Wada, K. Shimazaki and M. Iino, pp, Springer-Verlag, Tokyo
    • Maeda, A., S. P. Balashov and T. G. Ebrey (2005) Participation of internal water molecules and clusters in the unidirectional light-induced proton transfer in bacteriorhodopsin. In Light Sensing in Plants (Edited by M. Wada, K. Shimazaki and M. Iino), pp. 213-221. Springer-Verlag, Tokyo.
    • (2005) Light Sensing in Plants , pp. 213-221
    • Maeda, A.1    Balashov, S.P.2    Ebrey, T.G.3
  • 26
    • 0037466289 scopus 로고    scopus 로고
    • 2′ intermediates of the photocycle
    • 2′ intermediates of the photocycle. J. Mol. Biol. 328, 439-450.
    • (2003) J. Mol. Biol , vol.328 , pp. 439-450
    • Lanyi, J.K.1    Schobert, B.2
  • 27
    • 3543033483 scopus 로고    scopus 로고
    • What is the real crystallographic structure of the L photointermediate of bacteriorhodopsin?
    • Lanyi, J. K. (2004) What is the real crystallographic structure of the L photointermediate of bacteriorhodopsin? Biochim. Biophys. Acta 1658, 14-22.
    • (2004) Biochim. Biophys. Acta , vol.1658 , pp. 14-22
    • Lanyi, J.K.1
  • 28
    • 3142613053 scopus 로고    scopus 로고
    • Mechanism of primary proton transfer in bacteriorhodopsin
    • Bondar, A.-N., M. Elstner, S. Suhai, J. C. Smith and S. Fischer (2004) Mechanism of primary proton transfer in bacteriorhodopsin. Structure 12, 1281-1288.
    • (2004) Structure , vol.12 , pp. 1281-1288
    • Bondar, A.-N.1    Elstner, M.2    Suhai, S.3    Smith, J.C.4    Fischer, S.5
  • 29
    • 7744225102 scopus 로고    scopus 로고
    • Key role of electrostatic interactions in bacteriorhodopsin proton transfer
    • Bondar, A.-N., S. Fischer, J. C. Smith, M. Elstner and S. Suhai (2004) Key role of electrostatic interactions in bacteriorhodopsin proton transfer. J. Am. Chem. Soc. 126, 14668-14677.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 14668-14677
    • Bondar, A.-N.1    Fischer, S.2    Smith, J.C.3    Elstner, M.4    Suhai, S.5
  • 30
    • 85005500629 scopus 로고
    • Application of FTIR spectroscopy to the structural study on the function of bacteriorhodopsin
    • Maeda, A. (1995) Application of FTIR spectroscopy to the structural study on the function of bacteriorhodopsin. Isr. J. Chem. 35, 387-400.
    • (1995) Isr. J. Chem , vol.35 , pp. 387-400
    • Maeda, A.1
  • 31
    • 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
  • 32
    • 0025298852 scopus 로고
    • Water molecules and exchangeable hydrogen ions at the active center of bacteriorhodopsin localized by neutron diffraction. Elements of the proton pathway?
    • Papadopulos, 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
    • Papadopulos, G.1    Dencher, N.A.2    Zaccai, G.3    Büldt, G.4
  • 33
    • 0028266198 scopus 로고
    • Evidence for a bound water molecule next to the retinal Schiff base in bacteriorhodopsin and rhodopsin: A resonance Raman study of the Schiff base hydrogen/deuterium exchange
    • Deng, H., L. Huang, R. Callender and T. Ebrey (1994) Evidence for a bound water molecule next to the retinal Schiff base in bacteriorhodopsin and rhodopsin: A resonance Raman study of the Schiff base hydrogen/deuterium exchange. Biophys. J. 66, 1129-1136.
    • (1994) Biophys. J , vol.66 , pp. 1129-1136
    • Deng, H.1    Huang, L.2    Callender, R.3    Ebrey, T.4
  • 34
    • 0024973388 scopus 로고
    • Nuclear magnetic resonance study of the Schiff base in bacteriorhodopsin: Counterion effects on the nitrogen-15 shift anisotropy
    • DeGroot, H. J. M., G. S. Harbison, J. Herzfeld and R. G. Griffin (1990) Nuclear magnetic resonance study of the Schiff base in bacteriorhodopsin: Counterion effects on the nitrogen-15 shift anisotropy. Biochemistry 28, 3346-3353.
    • (1990) Biochemistry , vol.28 , pp. 3346-3353
    • DeGroot, H.J.M.1    Harbison, G.S.2    Herzfeld, J.3    Griffin, R.G.4
  • 35
    • 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
  • 36
    • 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. Sasaki, 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    Sasaki, J.2    Yamazaki, Y.3    Needleman, R.4    Lanyi, J.K.5
  • 39
    • 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. Saitô, 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    Saitô, H.3    Kandori, H.4    Needleman, R.5    Lanyi, J.K.6    Maeda, A.7
  • 40
    • 0029828763 scopus 로고    scopus 로고
    • Hydration of the counterion of the Schiff base in the chloride-transporting mutant of bacteriorhodopsin; FTIR and FT-Raman studies of the effects on anion binding when Asp85 is replaced with a neutral residue
    • Chon, Y.-S., J. Sasaki, H. Kandori, L. S. Brown, J. K. Lanyi, R. Needleman and A. Maeda (1996) Hydration of the counterion of the Schiff base in the chloride-transporting mutant of bacteriorhodopsin; FTIR and FT-Raman studies of the effects on anion binding when Asp85 is replaced with a neutral residue. Biochemistry 35, 14244-14250.
    • (1996) Biochemistry , vol.35 , pp. 14244-14250
    • Chon, Y.-S.1    Sasaki, J.2    Kandori, H.3    Brown, L.S.4    Lanyi, J.K.5    Needleman, R.6    Maeda, A.7
  • 41
    • 0032502007 scopus 로고    scopus 로고
    • Interaction 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) 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, 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
  • 42
    • 0032546920 scopus 로고
    • Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution
    • 1998
    • Luecke,- H., H.-T. Richter and J. K. Lanyi (1998) Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution. Science 280, 1934-1937.
    • (1934) Science , vol.280
    • Luecke, H.1    Richter, H.-T.2    Lanyi, J.K.3
  • 43
    • 0028073137 scopus 로고
    • Detection of a water molecule in the active site of bacteriorhodopsin: Hydrogen bonding changes during the primary photoreaction
    • Fischer, W. B., S. Sonar, T. Marti, H. G. Khorana and K. J. Rothschild (1994) Detection of a water molecule in the active site of bacteriorhodopsin: Hydrogen bonding changes during the primary photoreaction. Biochemistry 33, 12757-12762.
    • (1994) Biochemistry , vol.33 , pp. 12757-12762
    • Fischer, W.B.1    Sonar, S.2    Marti, T.3    Khorana, H.G.4    Rothschild, K.J.5
  • 45
    • 0028134307 scopus 로고
    • The retinal Schiff base-counterion complex of bacteriorhodopsin: Changed geometry during the photocycle is a cause of proton transfer to aspartate 85
    • Brown, L. S., Y. Gat, M. Sheves, Y. Yamazaki, A. Maeda, R. Needleman and J. K. Lanyi (1994) The retinal Schiff base-counterion complex of bacteriorhodopsin: Changed geometry during the photocycle is a cause of proton transfer to aspartate 85. Biochemistry 33, 12001-12011.
    • (1994) Biochemistry , vol.33 , pp. 12001-12011
    • Brown, L.S.1    Gat, Y.2    Sheves, M.3    Yamazaki, Y.4    Maeda, A.5    Needleman, R.6    Lanyi, J.K.7
  • 47
    • 0036089699 scopus 로고    scopus 로고
    • Magnetic resonance studies on the bacteriorhodopsin pump cycle
    • Herzfeld, J. and J. C. Lansing (2002) Magnetic resonance studies on the bacteriorhodopsin pump cycle. Annu. Rev. Biophys. Biomol. Struct. 31, 73-95.
    • (2002) Annu. Rev. Biophys. Biomol. Struct , vol.31 , pp. 73-95
    • Herzfeld, J.1    Lansing, J.C.2
  • 48
    • 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. L. Tomson, R. B. Gennis, T. G. Ebrey and S. P. 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.L.2    Gennis, R.B.3    Ebrey, T.G.4    Balashov, S.P.5
  • 49
    • 85005616566 scopus 로고
    • Photoreactions of the photointermediates of bacteriorhodopsin
    • Balashov, S. P. (1995) Photoreactions of the photointermediates of bacteriorhodopsin. Isr. J. Chem. 35, 415-428.
    • (1995) Isr. J. Chem , vol.35 , pp. 415-428
    • Balashov, S.P.1
  • 50
    • 0037432333 scopus 로고    scopus 로고
    • Water molecule rearrangements around Leu93 and Trp182 in the formation of the L intermediate in bacteriorhodopsin's photocycle
    • Maeda, A., F. L. Tomson, R. B. Gennis, S. P. Balashov and T. G. Ebrey (2003) Water molecule rearrangements around Leu93 and Trp182 in the formation of the L intermediate in bacteriorhodopsin's photocycle. Biochemistry 42, 2535-2541.
    • (2003) Biochemistry , vol.42 , pp. 2535-2541
    • Maeda, A.1    Tomson, F.L.2    Gennis, R.B.3    Balashov, S.P.4    Ebrey, T.G.5
  • 52
    • 0029738907 scopus 로고    scopus 로고
    • Steric interaction between the 9-methyl group of the retinal and tryptophan 182 controls 3-cis to all-trans reisomerization and proton uptake in the bacteriorhodopsin photocycle
    • Weidlich, O., B. Schalt, N. Friedman, M. Sheves, J. K. Lanyi, L. S. Brown and F. Siebert (1996) Steric interaction between the 9-methyl group of the retinal and tryptophan 182 controls 3-cis to all-trans reisomerization and proton uptake in the bacteriorhodopsin photocycle. Biochemistry 35, 10 807-10 814.
    • (1996) Biochemistry , vol.35
    • Weidlich, O.1    Schalt, B.2    Friedman, N.3    Sheves, M.4    Lanyi, J.K.5    Brown, L.S.6    Siebert, F.7
  • 53
    • 0030904207 scopus 로고    scopus 로고
    • Time-resolved Fourier transform infrared study of structural changes in the last steps of the photocycles of Glu-204 and Leu-93 mutants of bacteriorhodopsin
    • Kandori, H., Y. Yamazaki, M. Hatanaka, R. Needleman, L. S. Brown, H.-T. Richter, J. K. Lanyi and A. Maeda (1997) Time-resolved Fourier transform infrared study of structural changes in the last steps of the photocycles of Glu-204 and Leu-93 mutants of bacteriorhodopsin. Biochemistry 36, 5134-5141.
    • (1997) Biochemistry , vol.36 , pp. 5134-5141
    • Kandori, H.1    Yamazaki, Y.2    Hatanaka, M.3    Needleman, R.4    Brown, L.S.5    Richter, H.-T.6    Lanyi, J.K.7    Maeda, A.8
  • 54
    • 0344629882 scopus 로고    scopus 로고
    • Water-mediated hydrogen-bonded network on the cytoplasmic side of the Schiff base of the L photointermediate of bacteriorhodopsin
    • Maeda, A., J. Herzfeld, M. Belenky, R. Needleman, R. B. Gennis, S. P. Balashov and T. G. Ebrey (2003) Water-mediated hydrogen-bonded network on the cytoplasmic side of the Schiff base of the L photointermediate of bacteriorhodopsin. Biochemistry 42, 14122-14129.
    • (2003) Biochemistry , vol.42 , pp. 14122-14129
    • Maeda, A.1    Herzfeld, J.2    Belenky, M.3    Needleman, R.4    Gennis, R.B.5    Balashov, S.P.6    Ebrey, T.G.7
  • 55
    • 0037076526 scopus 로고    scopus 로고
    • Vibrational frequency and dipolar orientation of the protonated Schiff base in bacteriorhodopsin before and after photoisomerization
    • Kandori, H., M. Bizounok and J. Herzfeld (2002) Vibrational frequency and dipolar orientation of the protonated Schiff base in bacteriorhodopsin before and after photoisomerization. Biochemistry 41, 6026-6031.
    • (2002) Biochemistry , vol.41 , pp. 6026-6031
    • Kandori, H.1    Bizounok, M.2    Herzfeld, J.3
  • 56
    • 22844455879 scopus 로고    scopus 로고
    • Hydrogen bonds with large proton polarizability and proton transfer processes in electrochemistry and biology
    • Zundel, G. (2000) Hydrogen bonds with large proton polarizability and proton transfer processes in electrochemistry and biology. Adv. Chem. Phys. 111, 1-218.
    • (2000) Adv. Chem. Phys , vol.111 , pp. 1-218
    • Zundel, G.1
  • 57
    • 0034702762 scopus 로고    scopus 로고
    • Relocation of internal bound water in bacteriorhodopsin during the photoreaction of M at low temperature: An FTIR study
    • Maeda. A., F. L. Tomson, R. B. Gennis, H. Kandori, T. G. Ebrey and S. P. Balashov (2000) Relocation of internal bound water in bacteriorhodopsin during the photoreaction of M at low temperature: An FTIR study. Biochemistry 39, 10154-10162.
    • (2000) Biochemistry , vol.39 , pp. 10154-10162
    • Maeda, A.1    Tomson, F.L.2    Gennis, R.B.3    Kandori, H.4    Ebrey, T.G.5    Balashov, S.P.6
  • 58
    • 0033536594 scopus 로고    scopus 로고
    • Structural changes in bacteriorhodopsin during ion transport at 2 Å 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 Å 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
  • 62
    • 0036968773 scopus 로고    scopus 로고
    • Crystallographic structure of the retinal and the protein after deprotonation of the Schiff base: The switch in the bacteriorhodopsin photocycle
    • Lanyi, J. K. and B. Schobert (2002) Crystallographic structure of the retinal and the protein after deprotonation of the Schiff base: The switch in the bacteriorhodopsin photocycle. J. Mol. Biol. 321, 727-737.
    • (2002) J. Mol. Biol , vol.321 , pp. 727-737
    • Lanyi, J.K.1    Schobert, B.2
  • 63
    • 3843096037 scopus 로고    scopus 로고
    • Crystal structure of the M intermediate of bacteriorhodopsin: Allosteric structural changes mediated by sliding movement of a transmembrane helix
    • Takeda, K., Y. Matsui, N. Kamiya, S. Adachi, H. Okamura and T. Kouyama (2004) Crystal structure of the M intermediate of bacteriorhodopsin: Allosteric structural changes mediated by sliding movement of a transmembrane helix. J. Mol. Biol. 341, 1023-1037.
    • (2004) J. Mol. Biol , vol.341 , pp. 1023-1037
    • Takeda, K.1    Matsui, Y.2    Kamiya, N.3    Adachi, S.4    Okamura, H.5    Kouyama, T.6
  • 64
    • 0042845836 scopus 로고    scopus 로고
    • The role of small intraprotein cavities in the catalytic cycle of bacteriorhodopsin
    • Friedman, R., E. Nachiel and M. Gutman (2003) The role of small intraprotein cavities in the catalytic cycle of bacteriorhodopsin. Biophys. J. 85, 886-896.
    • (2003) Biophys. J , vol.85 , pp. 886-896
    • Friedman, R.1    Nachiel, E.2    Gutman, M.3
  • 65
    • 30144445932 scopus 로고    scopus 로고
    • Functional waters in intraprotein proton transfer monitored by FTIR difference spectroscopy
    • Garczarek, F. and K. Gerwert (2006) Functional waters in intraprotein proton transfer monitored by FTIR difference spectroscopy. Nature 439, 109-112.
    • (2006) Nature , vol.439 , pp. 109-112
    • Garczarek, F.1    Gerwert, K.2
  • 66
    • 0028324569 scopus 로고
    • Complete identification of C=O stretching vibrational bands of protonated aspartic acid residues in the difference infrared spectra of M and N intermediates versus bacteriorhodopsin
    • Sasaki, J., J. K. Lanyi, R. Needleman, T. Yoshizawa and A. Maeda (1994) Complete identification of C=O stretching vibrational bands of protonated aspartic acid residues in the difference infrared spectra of M and N intermediates versus bacteriorhodopsin. Biochemistry 33, 3178-3184.
    • (1994) Biochemistry , vol.33 , pp. 3178-3184
    • Sasaki, J.1    Lanyi, J.K.2    Needleman, R.3    Yoshizawa, T.4    Maeda, A.5
  • 67
    • 1142310689 scopus 로고    scopus 로고
    • Dynamics of water molecules in the bacteriorhodopsin trimer in explicit lipid/water environment
    • Kandt, C., J. Schlitter and K. Gerwert (2004) Dynamics of water molecules in the bacteriorhodopsin trimer in explicit lipid/water environment. Biophys. J. 86, 705-717.
    • (2004) Biophys. J , vol.86 , pp. 705-717
    • Kandt, C.1    Schlitter, J.2    Gerwert, K.3
  • 68
    • 0034734246 scopus 로고    scopus 로고
    • Atomic resolution structures of bacteriorhodopsin photocycle intermediates: The role of discrete water molecules in the function of this light-driven ion pump
    • Luecke, H. (2000) Atomic resolution structures of bacteriorhodopsin photocycle intermediates: The role of discrete water molecules in the function of this light-driven ion pump. Biochim. Biophys. Acta. 1460, 133-156.
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 133-156
    • Luecke, H.1
  • 69
    • 1942468181 scopus 로고    scopus 로고
    • Crystal structures of bR(D85S) favor a model of bacteriorhodopsin as a hydroxyl-ion pump
    • Facciotti, M. T., S. Rouhani and R. M. Glaeser (2004) Crystal structures of bR(D85S) favor a model of bacteriorhodopsin as a hydroxyl-ion pump. FEBS Lett. 564, 301-306.
    • (2004) FEBS Lett , vol.564 , pp. 301-306
    • Facciotti, M.T.1    Rouhani, S.2    Glaeser, R.M.3
  • 70
    • 0038649076 scopus 로고    scopus 로고
    • Crystallographic structures of the M and N intermediates of bacteriorhodopsin: Assembly of a hydrogen-bonded chain of water molecules between Asp-96 and the retinal Schiff base
    • Schobert, B., L. S. Brown and J. K. Lanyi (2003) Crystallographic structures of the M and N intermediates of bacteriorhodopsin: Assembly of a hydrogen-bonded chain of water molecules between Asp-96 and the retinal Schiff base. J. Mol. Biol. 330, 553-570.
    • (2003) J. Mol. Biol , vol.330 , pp. 553-570
    • Schobert, B.1    Brown, L.S.2    Lanyi, J.K.3
  • 71
    • 0026332339 scopus 로고
    • Water is required for proton transfer from aspartate-96 to the bacteriorhodopsin Schiff base
    • Cao, Y., G. Váró, M. Chang, B. Ni, R. Needleman and J. K. Lanyi (1991) Water is required for proton transfer from aspartate-96 to the bacteriorhodopsin Schiff base. Biochemistry 30, 10972-10979.
    • (1991) Biochemistry , vol.30 , pp. 10972-10979
    • Cao, Y.1    Váró, G.2    Chang, M.3    Ni, B.4    Needleman, R.5    Lanyi, J.K.6
  • 72
    • 14844347271 scopus 로고    scopus 로고
    • Proton binding within a membrane protein by a protonated water cluster
    • Garczarek, F., L. S. Brown, J. K. Lanyi and K. Gerwert (2005) Proton binding within a membrane protein by a protonated water cluster. Proc. Natl. Acad. Sci. USA 102, 3633-3638.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 3633-3638
    • Garczarek, F.1    Brown, L.S.2    Lanyi, J.K.3    Gerwert, K.4
  • 73
    • 0029053721 scopus 로고
    • Experimental evidence for hydrogen-bonded network proton transfer in bacteriorhodopsin shown by Fourier transform infrared spectroscopy using azide as catalysis
    • Le Courte, J., J. Tittor, D. Oesterhelt and K. Gerwert (1995) Experimental evidence for hydrogen-bonded network proton transfer in bacteriorhodopsin shown by Fourier transform infrared spectroscopy using azide as catalysis. Proc. Natl. Acad. Sci. USA 92, 4962-4966.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4962-4966
    • Le Courte, J.1    Tittor, J.2    Oesterhelt, D.3    Gerwert, K.4
  • 74
    • 0024325044 scopus 로고
    • A defective proton pump, point-mutated bacteriorhodopsin Asp96 → Asn is fully reactivated by azide
    • Tittor, J., C. Soell, D. Oesterhelt, H.-J. Butt and E. Bamberg (1989) A defective proton pump, point-mutated bacteriorhodopsin Asp96 → Asn is fully reactivated by azide. EMBO J. 8, 3477-3482.
    • (1989) EMBO J , vol.8 , pp. 3477-3482
    • Tittor, J.1    Soell, C.2    Oesterhelt, D.3    Butt, H.-J.4    Bamberg, E.5
  • 75
    • 0035829539 scopus 로고    scopus 로고
    • Water conduction through the hydrophobic channel of a carbon nanotube
    • Hummer, G., J. C. Rasaiah and J. P. Noworyta (2001) Water conduction through the hydrophobic channel of a carbon nanotube. Nature 414, 188-190.
    • (2001) Nature , vol.414 , pp. 188-190
    • Hummer, G.1    Rasaiah, J.C.2    Noworyta, J.P.3
  • 76
    • 0035902770 scopus 로고    scopus 로고
    • Microsecond exchange of internal water molecules in bacteriorhodopsin
    • Gottschalk, M., N. A. Dencher and B. Halle (2001) Microsecond exchange of internal water molecules in bacteriorhodopsin. J. Mol. Biol. 311, 605-621.
    • (2001) J. Mol. Biol , vol.311 , pp. 605-621
    • Gottschalk, M.1    Dencher, N.A.2    Halle, B.3
  • 78
    • 0027429642 scopus 로고
    • A model-independent approach to assigning bacteriorhodopsin's intramolecular reactions to photocycle intermediates
    • Hessling, B., G. Souvignir and K. Gerwert (1993) A model-independent approach to assigning bacteriorhodopsin's intramolecular reactions to photocycle intermediates. Biophys. J. 65, 1929-1941.
    • (1993) Biophys. J , vol.65 , pp. 1929-1941
    • Hessling, B.1    Souvignir, G.2    Gerwert, K.3
  • 79
    • 0041417311 scopus 로고    scopus 로고
    • Time-resolved step-scan Fourier transform infrared spectroscopy reveals differences between early and late M intermediates of bacteriorhodopsin
    • Rödig, C., I. Chizov, O. Weidlich and F. Siebert (1999) Time-resolved step-scan Fourier transform infrared spectroscopy reveals differences between early and late M intermediates of bacteriorhodopsin. Biophys. J. 76, 2687-2701.
    • (1999) Biophys. J , vol.76 , pp. 2687-2701
    • Rödig, C.1    Chizov, I.2    Weidlich, O.3    Siebert, F.4
  • 80
    • 0027491027 scopus 로고
    • Thermal motions and function of bacteriorhodopsin in purple membranes: Effects of temperature and hydration studied by neutron scattering
    • Ferrand, M., A. J. Dianoux, W. Petry and G. Zaccai (1993) Thermal motions and function of bacteriorhodopsin in purple membranes: Effects of temperature and hydration studied by neutron scattering. Proc. Natl. Acad. Sci. USA 90, 9668-9672.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9668-9672
    • Ferrand, M.1    Dianoux, A.J.2    Petry, W.3    Zaccai, G.4
  • 82
    • 0036931523 scopus 로고    scopus 로고
    • Pressure dependence of the photocycle kinetics of bacteriorhodopsin
    • Klink, B. U., R. Winter, M. Engelhard and I. Chizhof (2002) Pressure dependence of the photocycle kinetics of bacteriorhodopsin. Biophys. J. 83, 3490-3498.
    • (2002) Biophys. J , vol.83 , pp. 3490-3498
    • Klink, B.U.1    Winter, R.2    Engelhard, M.3    Chizhof, I.4


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