메뉴 건너뛰기




Volumn 42, Issue 48, 2003, Pages 14122-14129

Water-Mediated Hydrogen-Bonded Network on the Cytoplasmic Side of the Schiff Base of the L Photointermediate of Bacteriorhodopsin

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CHROMOPHORES; HYDROGEN BONDS; MOLECULAR VIBRATIONS; PROTONS;

EID: 0344629882     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0301542     Document Type: Article
Times cited : (15)

References (53)
  • 1
    • 0016723355 scopus 로고
    • Bacteriorhodopsin: A light-driven proton pump in Halobacterium halobium
    • Lozier, R. H., Bogomolni, R. A., and Stoeckenius, W. (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
  • 2
    • 85005688720 scopus 로고
    • The photocycles of bacteriorhodopsin
    • Lanyi, J. K., and Váró, G. (1995) The photocycles of bacteriorhodopsin, Isr. J. Chem. 35, 365-385.
    • (1995) Isr. J. Chem. , vol.35 , pp. 365-385
    • Lanyi, J.K.1    Váró, G.2
  • 3
    • 0035345448 scopus 로고    scopus 로고
    • Trapping and spectroscopic identification of the photointermediates of bacteriorhodopsin at low temperatures
    • Balashov, S. P., and Ebrey, T. G. (2001) Trapping and spectroscopic identification of the photointermediates of bacteriorhodopsin at low temperatures, Photochem. Photobiol. 73, 453-462.
    • (2001) Photochem. Photobiol. , vol.73 , pp. 453-462
    • Balashov, S.P.1    Ebrey, T.G.2
  • 4
    • 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
  • 5
    • 0034734254 scopus 로고    scopus 로고
    • Role of internal water molecules in bacteriorhodopsin
    • Kandori, H. (2000) Role of internal water molecules in bacteriorhodopsin, Biochim. Biophys. Acta 1460, 177-191.
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 177-191
    • Kandori, H.1
  • 6
    • 0035498348 scopus 로고    scopus 로고
    • Internal water molecules as mobile polar groups for light-induced proton translocation in bacteriorhodopsin and rhodopsin as studied by difference FTIR spectroscopy
    • Maeda, A. (2001) Internal water molecules as mobile polar groups for light-induced proton translocation in bacteriorhodopsin and rhodopsin as studied by difference FTIR spectroscopy, Biochemistry (Moscow) 66, 1555-1569.
    • (2001) Biochemistry (Moscow) , vol.66 , pp. 1555-1569
    • Maeda, A.1
  • 7
    • 84989669798 scopus 로고
    • Fourier transform infrared spectral studies on the Schiff base mode of all-trans bacteriorhodopsin and its photointermediates
    • Maeda, A., Sasaki, J., Pfefferlé, J.-M., Shichida, Y., and Yoshizawa, T. (1991) Fourier transform infrared spectral studies on the Schiff base mode of all-trans bacteriorhodopsin and its photointermediates, Photochem. Photobiol. 54, 911-921.
    • (1991) Photochem. Photobiol. , vol.54 , pp. 911-921
    • Maeda, A.1    Sasaki, J.2    Pfefferlé, J.-M.3    Shichida, Y.4    Yoshizawa, T.5
  • 8
    • 0037076526 scopus 로고    scopus 로고
    • Vibrational frequency and dipolar orientation of the protonated Schiff base in bacteriorhodopsin before and after photoisomerization
    • Kandori, H., Belenky, M., and Herzfeld, J. (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    Belenky, M.2    Herzfeld, J.3
  • 10
    • 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., Mogi, T., Marti, M., Stern, L. J., Khorana, H. G., and Rothschild, K. J. (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, M.3    Stern, L.J.4    Khorana, H.G.5    Rothschild, K.J.6
  • 11
    • 0025868156 scopus 로고
    • Fourier transform infrared study of the N intermediate of bacteriorhodopsin
    • Pfefferlé, J.-M., Maeda, A., Sasaki, J., and Yoshizawa, T. (1991) Fourier transform infrared study of the N intermediate of bacteriorhodopsin, Biochemistry 30, 6548-6556.
    • (1991) Biochemistry , vol.30 , pp. 6548-6556
    • Pfefferlé, J.-M.1    Maeda, A.2    Sasaki, J.3    Yoshizawa, T.4
  • 12
    • 0025820289 scopus 로고
    • Thermodynamics and energy coupling in the bacteriorhodopsin photocycle
    • Váró, G., and Lanyi, J. K. (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
    • 0034734227 scopus 로고    scopus 로고
    • NMR probes of vectoriality in the proton-motive photocycle of bacteriorhodopsin: Evidence for an "electrostatic steering" mechanism
    • Herzfeld, J., and Tounge, B. (2000) NMR probes of vectoriality in the proton-motive photocycle of bacteriorhodopsin: evidence for an "electrostatic steering" mechanism, Biochim. Biophys. Acta 1460, 95-105.
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 95-105
    • Herzfeld, J.1    Tounge, B.2
  • 15
    • 0036089699 scopus 로고    scopus 로고
    • Magnetic resonance studies of the bacteriorhodopsin pump cycle
    • Herzfeld, J., and Lansing, J. C. (2002) Magnetic resonance studies of 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
  • 16
    • 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., and Schobert, B. (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.1    Schobert, B.2
  • 19
    • 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., Tuzi, S., Saitô, H., Kandori, H., Needleman, R., Lanyi, J. K., and Maeda, A. (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
  • 23
    • 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., Tomson, F. L., Gennis, R. B., Balashov, S. P., and Ebrey, T. G. (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
  • 24
    • 0000095780 scopus 로고
    • New intermediates in the photochemical conversions of bacteriorhodopsin
    • Litvin, F. F., and Balashov, S. P. (1977) New intermediates in the photochemical conversions of bacteriorhodopsin, Biophysics 22, 1157-1160.
    • (1977) Biophysics , vol.22 , pp. 1157-1160
    • Litvin, F.F.1    Balashov, S.P.2
  • 25
    • 0017862159 scopus 로고
    • More evidence that light isomerizes the chromophore of purple membrane protein
    • Hurley, J. B., Becher, B., and Ebrey, T. G. (1978) More evidence that light isomerizes the chromophore of purple membrane protein, Nature 272, 87-88.
    • (1978) Nature , vol.272 , pp. 87-88
    • Hurley, J.B.1    Becher, B.2    Ebrey, T.G.3
  • 26
    • 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., Tomson, F. L., Gennis, R. B., Ebrey, T. G., and Balashov, S. P. (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
  • 27
  • 29
    • 0342646933 scopus 로고    scopus 로고
    • Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin
    • Sass, H. J., Büldt, G., Gessenich, R., Hehn, D., Neff, D., Schlesinger, R., Berendzen, J., and Ormos, P. (2000) Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin, Nature 406, 649-653.
    • (2000) Nature , vol.406 , pp. 649-653
    • Sass, H.J.1    Büldt, G.2    Gessenich, R.3    Hehn, D.4    Neff, D.5    Schlesinger, R.6    Berendzen, J.7    Ormos, P.8
  • 31
    • 0029903197 scopus 로고    scopus 로고
    • Electron-crystallographic refinement of the structure of bacteriorhodopsin
    • Grigorieff, N., Ceska, T. A., Downing, K. H., Baldwin, J. M., and Henderson, R. (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
  • 32
    • 0032546920 scopus 로고    scopus 로고
    • Proton-transfer pathways in bacteriorhodopsin at 2.3 Angstrom resolution
    • Luecke, H., Richter, H.-T., and Lanyi, J. K. (1998) Proton-transfer pathways in bacteriorhodopsin at 2.3 Angstrom resolution, Science 280, 1934-1937.
    • (1998) Science , vol.280 , pp. 1934-1937
    • Luecke, H.1    Richter, H.-T.2    Lanyi, J.K.3
  • 34
    • 0032578378 scopus 로고    scopus 로고
    • Lipid patches in membrane protein oligomeres: Crystal structure of the bacteriorhodopsin-lipid complex
    • Essen, L.-O., Siegert, R., Lehmann, W. D., and Oesterhelt, D. (1998) Lipid patches in membrane protein oligomeres: Crystal structure of the bacteriorhodopsin-lipid complex, Proc. Natl. Acad. Sci. U.S.A. 95, 11673-11678.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 11673-11678
    • Essen, L.-O.1    Siegert, R.2    Lehmann, W.D.3    Oesterhelt, D.4
  • 35
    • 0033567092 scopus 로고    scopus 로고
    • Protein, lipid and water organization in bacteriorhodopsin crystals: A molecular view of the purple membrane at 1.9 Å resolution
    • Belrhali, H., Nollert, P., Royant, A., Menzel, C., Rosenbusch, J. P., Landau, E. M., and Pebay-Peyroula, E. (1999) Protein, lipid and water organization in bacteriorhodopsin crystals: a molecular view of the purple membrane at 1.9 Å resolution, Structure 7, 909-917.
    • (1999) Structure , vol.7 , pp. 909-917
    • Belrhali, H.1    Nollert, P.2    Royant, A.3    Menzel, C.4    Rosenbusch, J.P.5    Landau, E.M.6    Pebay-Peyroula, E.7
  • 36
    • 0033605231 scopus 로고    scopus 로고
    • The structure of bacteriorhodopsin at 3.0 Å resolution based on electron crystallography: Implication of the charge distribution
    • Mitsuoka, K., Hirai, T., Murata, K., Miyazawa, A., Kidera, A., Kimura, Y., and Fujiyoshi, Y. (1999) The structure of bacteriorhodopsin at 3.0 Å resolution based on electron crystallography: implication of the charge distribution, J. Mol. Biol. 286, 861-882.
    • (1999) J. Mol. Biol. , vol.286 , pp. 861-882
    • Mitsuoka, K.1    Hirai, T.2    Murata, K.3    Miyazawa, A.4    Kidera, A.5    Kimura, Y.6    Fujiyoshi, Y.7
  • 37
    • 0000557270 scopus 로고    scopus 로고
    • Protein structural changes in bacteriorhodopsin upon photoisomerization as revealed by polarized FTIR spectroscopy
    • Kandori, H., Kinoshita, N., Shichida, Y., and Maeda, A. (1998) Protein structural changes in bacteriorhodopsin upon photoisomerization as revealed by polarized FTIR spectroscopy, J. Phys. Chem. B 102, 7899-7905.
    • (1998) J. Phys. Chem. B , vol.102 , pp. 7899-7905
    • Kandori, H.1    Kinoshita, N.2    Shichida, Y.3    Maeda, A.4
  • 38
    • 0014581408 scopus 로고
    • Growth and nutrition of extremely halophilic bacteria
    • Gochnauer, M. B., and Kushner, D. J. (1969) Growth and nutrition of extremely halophilic bacteria, Can. J. Microbiol. 15, 1157-1165.
    • (1969) Can. J. Microbiol. , vol.15 , pp. 1157-1165
    • Gochnauer, M.B.1    Kushner, D.J.2
  • 39
    • 0016376428 scopus 로고
    • Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane
    • Oesterhelt, D., and Stoeckenius, W. (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
  • 40
    • 0025924636 scopus 로고
    • Properties of Asp212-Asn bacteriorhodopsin suggest that Asp212 and Asp85 both participate in a counterion and proton acceptor complex near the Schiff base
    • Needleman, R., Chang, M., Ni, B., Váró, G., Fornés, J., White, S. H., and Lanyi, J. K. (1991) Properties of Asp212-Asn bacteriorhodopsin suggest that Asp212 and Asp85 both participate in a counterion and proton acceptor complex near the Schiff base, J. Biol. Chem. 266, 11478-11484.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11478-11484
    • Needleman, R.1    Chang, M.2    Ni, B.3    Váró, G.4    Fornés, J.5    White, S.H.6    Lanyi, J.K.7
  • 41
    • 0028239690 scopus 로고
    • The proton transfers in the cytoplasmic domain of bacteriorhodopsin are facilitated by a cluster of interacting residues
    • Brown, L. S., Yamazaki, Y., Maeda, A., Sun, L., Needleman, R., and Lanyi, J. K. (1994) The proton transfers in the cytoplasmic domain of bacteriorhodopsin are facilitated by a cluster of interacting residues, J. Mol. Biol. 239, 401-414.
    • (1994) J. Mol. Biol. , vol.239 , pp. 401-414
    • Brown, L.S.1    Yamazaki, Y.2    Maeda, A.3    Sun, L.4    Needleman, R.5    Lanyi, J.K.6
  • 42
    • 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., Kandori, H., Needleman, R., Lanyi, J. K., and Maeda, A. (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
  • 44
    • 0037418568 scopus 로고    scopus 로고
    • Structural changes of water in the Schiff base region of bacteriorhodopsin: Proposal of a hydration switch model
    • Tanimoto, T., Furutani, Y., and Kandori, H. (2003) Structural changes of water in the Schiff base region of bacteriorhodopsin: proposal of a hydration switch model, Biochemistry 42, 2300-2306.
    • (2003) Biochemistry , vol.42 , pp. 2300-2306
    • Tanimoto, T.1    Furutani, Y.2    Kandori, H.3
  • 45
    • 0034731017 scopus 로고    scopus 로고
    • Direct observation of the bridged water stretching vibrations inside a protein
    • Kandori, H., and Shichida, Y. (2000) Direct observation of the bridged water stretching vibrations inside a protein, J. Am. Chem. Soc. 122, 11745-11746.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 11745-11746
    • Kandori, H.1    Shichida, Y.2
  • 46
    • 0015407488 scopus 로고
    • Intermolecular interaction effects in the amide I vibrations of polypeptides
    • Krimm, S., and Abe, Y. (1972) Intermolecular interaction effects in the amide I vibrations of polypeptides, Proc. Natl. Acad. Sci. U.S.A. 69, 2788-2792.
    • (1972) Proc. Natl. Acad. Sci. U.S.A. , vol.69 , pp. 2788-2792
    • Krimm, S.1    Abe, Y.2
  • 47
    • 0000421383 scopus 로고    scopus 로고
    • Liquid structures and the infrared and isotropic/anisotropic Raman noncoincidence in liquid methanol, a methanol-LiCl solution, and a solvated electron in methanol: Molecular dynamics and ab initio molecular orbital studies
    • Torii, H. (1999) Liquid structures and the infrared and isotropic/anisotropic Raman noncoincidence in liquid methanol, a methanol-LiCl solution, and a solvated electron in methanol: Molecular dynamics and ab initio molecular orbital studies, J. Phys. Chem. A 103, 2843-2850.
    • (1999) J. Phys. Chem. A , vol.103 , pp. 2843-2850
    • Torii, H.1
  • 48
    • 0031684846 scopus 로고    scopus 로고
    • Structural characterization of the L-to-M transition of the bacteriorhodopsin photocycle
    • Hendrickson, F. M., Burkard, F., and Glaeser, R. M. (1998) Structural characterization of the L-to-M transition of the bacteriorhodopsin photocycle, Biophys. J. 75, 1446-1454.
    • (1998) Biophys. J. , vol.75 , pp. 1446-1454
    • Hendrickson, F.M.1    Burkard, F.2    Glaeser, R.M.3
  • 50
    • 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, 1-217.
    • (2000) Adv. Chem. Phys. , vol.111 , pp. 1-217
    • Zundel, G.1
  • 51
    • 0033524454 scopus 로고    scopus 로고
    • Disordered water within a hydrophobic protein cavity visualized by X-ray crystallography
    • Yu, B., Blaber, M., Gronenborn, A. M., Clore, G. M., and Caspar, D. L. (1999) Disordered water within a hydrophobic protein cavity visualized by X-ray crystallography, Proc. Natl. Acad. Sci. U.S.A. 96, 103-108.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 103-108
    • Yu, B.1    Blaber, M.2    Gronenborn, A.M.3    Clore, G.M.4    Caspar, D.L.5
  • 52
    • 0036452022 scopus 로고    scopus 로고
    • Specific damage induced by X-ray radiation and structural changes in the primary photoreaction of bacteriorhodopsin
    • Matsui, Y., Sakai, K., Murakami, M., Shiro, Y., Adachi, S., Okumura, H., and Kouyama, T. (2002) Specific damage induced by X-ray radiation and structural changes in the primary photoreaction of bacteriorhodopsin, J. Mol. Biol. 324, 469-481.
    • (2002) J. Mol. Biol. , vol.324 , pp. 469-481
    • Matsui, Y.1    Sakai, K.2    Murakami, M.3    Shiro, Y.4    Adachi, S.5    Okumura, H.6    Kouyama, T.7
  • 53
    • 0033536594 scopus 로고    scopus 로고
    • Structural changes in bacteriorhodopsin during ion transport at 2 Angstrom resolution
    • Luecke, H., Schobert, B., Richter, H.-T., Cartailler, J.-P., and Lanyi, J. K. (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.