메뉴 건너뛰기




Volumn 121, Issue 3, 1997, Pages 399-406

Intramembrane signaling mediated by hydrogen-bonding of water and carboxyl groups in bacteriorhodopsin and rhodopsin

Author keywords

Bacteriorhodopsin; FT IR; Halorhodopsin; Proton pathway; Rhodopsin

Indexed keywords

ANION; ASPARTIC ACID; BACTERIORHODOPSIN; CARBONYL DERIVATIVE; CARBOXYL GROUP; CHLORIDE; GLUTAMIC ACID; HALORHODOPSIN; PEPTIDE; PROTON; PROTON PUMP; RHODOPSIN; SCHIFF BASE; WATER;

EID: 0030987170     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021602     Document Type: Review
Times cited : (73)

References (62)
  • 1
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryomicroscopy
    • Henderson, R., Baldwin, J.M., Ceska, T.A., Zemlin, F., Beckman, E., and Downing, K.H. (1990) Model for the structure of bacteriorhodopsin based on high-resolution electron cryomicroscopy. J. Mol. Biol. 213, 899-929
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckman, E.5    Downing, K.H.6
  • 3
    • 0025829307 scopus 로고
    • From femtoseconds to biology: Mechanism of bacteriorhodopsin's light-driven proton pump
    • Mathies, R.A., Lin, S.W., Ames, J.B., and Pollard, W.T. (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
  • 4
    • 0027769837 scopus 로고
    • Proton translocation mechanism and energetics in the light-driven proton pump bacteriorhodopsin
    • Lanyi, J.K. (1993) Proton translocation mechanism and energetics in the light-driven proton pump bacteriorhodopsin. Biochim. Biophys. Acta 1183, 241-261
    • (1993) Biochim. Biophys. Acta , vol.1183 , pp. 241-261
    • Lanyi, J.K.1
  • 5
    • 85005688720 scopus 로고    scopus 로고
    • The photocycle of bacteriorhodopsin
    • Lanyi, J.K. and Váró, G. (1996) The photocycle of bacteriorhodopsin. Israel J. Chem. 35, 365-385
    • (1996) Israel J. Chem. , vol.35 , pp. 365-385
    • Lanyi, J.K.1    Váró, G.2
  • 6
    • 85005500629 scopus 로고    scopus 로고
    • Application of FT-IR spectroscopy to the structural study on the function of bacteriorhodopsin
    • Maeda, A. (1996) Application of FT-IR spectroscopy to the structural study on the function of bacteriorhodopsin. Israel J. Chem. 35, 387-400
    • (1996) Israel J. Chem. , vol.35 , pp. 387-400
    • Maeda, A.1
  • 7
    • 0027031210 scopus 로고
    • Time-resolved Fourier transform infrared spectroscopy of the bacteriorhodopsin mutant Tyr185→Phe: Asp-96 reprotonates during O formation; Asp-85 and Asp-212 deprotonate during O-decay
    • Bousché, O., Sonar, S., Krebs, M.P., Khorana, H.G., and Rothschild, K.J. (1992) Time-resolved Fourier transform infrared spectroscopy of the bacteriorhodopsin mutant Tyr185→Phe: Asp-96 reprotonates during O formation; Asp-85 and Asp-212 deprotonate during O-decay. Photochem. Photobiol. 56, 1085- 1096
    • (1992) Photochem. Photobiol. , vol.56 , pp. 1085-1096
    • Bousché, O.1    Sonar, S.2    Krebs, M.P.3    Khorana, H.G.4    Rothschild, K.J.5
  • 8
  • 10
    • 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
  • 11
    • 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., Sasaki, J., Yamazaki, Y., Needleman, R., and Lanyi, J.K. (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
  • 12
    • 84989669798 scopus 로고
    • Fourier transform infrared spectral studies on the Schiff base mode of all-trans bacteriorhodopsin and its photointermediates, K and L
    • 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, K and L. 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
  • 13
    • 0028944068 scopus 로고
    • Nanosecond time-resolved infrared spectroscopy distinguishes two K species in the bacteriorhodopsin
    • Sasaki, J., Yuzawa, T., Kandori, H., Maeda, A., and Hamaguchi, H. (1995) Nanosecond time-resolved infrared spectroscopy distinguishes two K species in the bacteriorhodopsin. 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
  • 14
    • 0027478957 scopus 로고
    • Time-resolved infrared spectral analysis of the KL-to-L conversion in the photocycle of bacteriorhodopsin
    • Sasaki, J., Maeda, A., Kato, C., and Hamaguchi, H. (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
  • 15
    • 0026602025 scopus 로고
    • Water structure changes in bacteriorhodopsin photocycle: Analysis by Fourier transform infrared spectroscopy
    • Maeda, A., Sasaki, J., Shichida, Y., and Yoshizawa, T. (1992) Water structure changes in 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
  • 17
    • 0026054732 scopus 로고
    • Effect of intermolecular orientation upon proton transfer within a polarizable medium
    • Scheiner, S. and Duan, X. (1991) Effect of intermolecular orientation upon proton transfer within a polarizable medium. Biophys. J. 60, 874-883
    • (1991) Biophys. J. , vol.60 , pp. 874-883
    • Scheiner, S.1    Duan, X.2
  • 18
    • 0028075739 scopus 로고
    • The retinal Schiff base- counterion complex of bacteriorhodopsin: Changed geometry daring the photocycle is a cause of proton transfer to aspartate 85
    • Brown, L.S., Gat, Y., Sheves, M., Yamazaki, Y., Maeda, A., Needleman, R., and Lanyi, J.K. (1994) The retinal Schiff base- counterion complex of bacteriorhodopsin: Changed geometry daring 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
  • 19
    • 0029864761 scopus 로고    scopus 로고
    • a of the retinal Schiff base during the photocycle of bacteriorhodopsin
    • a of the retinal Schiff base during the photocycle of bacteriorhodopsin. Proc. Natl. Acad. Sci. USA 93, 1731-1734
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1731-1734
    • Brown, L.S.1    Lanyi, J.K.2
  • 20
    • 0001513332 scopus 로고
    • Molecular dynamics study of the early intermediates in the bacteriorhodopsin photocycle
    • Humphrey, W., Xu, D., Sheves, M., and Schulten, K. (1995) Molecular dynamics study of the early intermediates in the bacteriorhodopsin photocycle. J. Phys. Chem. 99, 14549-14560
    • (1995) J. Phys. Chem. , vol.99 , pp. 14549-14560
    • Humphrey, W.1    Xu, D.2    Sheves, M.3    Schulten, K.4
  • 22
    • 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 on the effects of anion binding when Asp85 is replaced with a neutral residue
    • Chon, Y.-S., Sasaki, J., Kandori, H., Brown, L.S., Lanyi, J.K., Needleman, R., and Maeda, A. (1996) Hydration of the counterion of the Schiff base in the chloride transporting mutant of bacteriorhodopsin: FTIR and FT-Raman studies on the effects of 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
  • 24
    • 0000830257 scopus 로고
    • The halo-opsin gene II. Sequence, primary structure of halorhodopsin and comparison with bacteriorhodopsin
    • Blanck, A. and Oesterhelt, D. (1987) The halo-opsin gene II. Sequence, primary structure of halorhodopsin and comparison with bacteriorhodopsin. EMBO J. 6, 265-273
    • (1987) EMBO J. , vol.6 , pp. 265-273
    • Blanck, A.1    Oesterhelt, D.2
  • 25
    • 0028869129 scopus 로고
    • Light-driven chloride ion transport by halorhodopsin from Natronbacterium pharaonis, 1. The photochemical cycle
    • Váró, G., Brown, L.S., Sasaki, J., Kandori, H., Maeda, A., Needleman, R., and Lanyi, J.K. (1995) Light-driven chloride ion transport by halorhodopsin from Natronbacterium pharaonis, 1. The photochemical cycle. Biochemistry 34, 14490-14499
    • (1995) Biochemistry , vol.34 , pp. 14490-14499
    • Váró, G.1    Brown, L.S.2    Sasaki, J.3    Kandori, H.4    Maeda, A.5    Needleman, R.6    Lanyi, J.K.7
  • 26
    • 0028808334 scopus 로고
    • Light-driven chloride ion transport by halorhodopsin from Natronbacterium pharaonis, 2. Chloride release and uptake, protein conformation change, and thermodynamics
    • Váró, G., Needleman, R., and Lanyi, J.K. (1995) Light-driven chloride ion transport by halorhodopsin from Natronbacterium pharaonis, 2. Chloride release and uptake, protein conformation change, and thermodynamics. Biochemistry 34, 14500-14507
    • (1995) Biochemistry , vol.34 , pp. 14500-14507
    • Váró, G.1    Needleman, R.2    Lanyi, J.K.3
  • 27
    • 0028223284 scopus 로고
    • Infrared spectroscopic detection of light-induced change in chloride-arginine interaction in halorhodopsin
    • Braiman, M.S., Walther, T.J., and Biercheck, D.M. (1994) Infrared spectroscopic detection of light-induced change in chloride-arginine interaction in halorhodopsin. Biochemistry 33, 1629-1723
    • (1994) Biochemistry , vol.33 , pp. 1629-1723
    • Braiman, M.S.1    Walther, T.J.2    Biercheck, D.M.3
  • 28
    • 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, T., 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, T.3    Stern, L.J.4    Khorana, H.G.5    Rothschild, K.J.6
  • 29
    • 0026717983 scopus 로고
    • Structures of aspartic acid-96 in the L and N intermediates of bacteriorhodopsin: Analysis by Fourier transform infrared spectra
    • Maeda, A., Sasaki, J., Shichida, Y., and Yoshizawa, T., Chang, M., Ni, B., Needleman, R., and Lanyi, J.K. (1992) Structures of aspartic acid-96 in the L and N intermediates of bacteriorhodopsin: Analysis by Fourier transform infrared spectra. 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
  • 31
    • 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
  • 32
    • 0028988375 scopus 로고
    • Site-directed isotope labelling and ATR-FTIR difference spectroscopy of bacteriorhodopsin: The peptide carbonyl group of TYR185 is structurally active during the bR→N transition
    • Ludlam, C.F.C., Sonar, S., Lee, C.-P., Coleman, M., Herzfeld, J., RajBhandary, U.L., and Rothschild, K.J. (1995) Site-directed isotope labelling and ATR-FTIR difference spectroscopy of bacteriorhodopsin: the peptide carbonyl group of TYR185 is structurally active during the bR→N transition. Biochemistry 34, 2-6
    • (1995) Biochemistry , vol.34 , pp. 2-6
    • Ludlam, C.F.C.1    Sonar, S.2    Lee, C.-P.3    Coleman, M.4    Herzfeld, J.5    Rajbhandary, U.L.6    Rothschild, K.J.7
  • 33
    • 0029665673 scopus 로고    scopus 로고
    • a's of asp-85 and glu-204 forms part of the reprotonation switch of bacteriorhodopsin
    • a's of asp-85 and glu-204 forms part of the reprotonation switch of bacteriorhodopsin. Biochemistry 35, 4054-4062
    • (1996) Biochemistry , vol.35 , pp. 4054-4062
    • Richter, H.-T.1    Brown, L.S.2    Needleman, R.3    Lanyi, J.K.4
  • 34
    • 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., Lanyi, J.K., Needleman, R., Yoshizawa, T., and Maeda, A. (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
  • 38
    • 0028949144 scopus 로고
    • Relationship of proton release at the extracellular surface to deprotonation of the Schiff base in the bacteriorhodopsin photocycle
    • Cao, Y., Brown, L.S., Sasaki, J., Maeda, A., Needleman, R., and Lanyi, J.K. (1995) Relationship of proton release at the extracellular surface to deprotonation of the Schiff base in the bacteriorhodopsin photocycle. Biophys. J. 68, 1518-1530
    • (1995) Biophys. J. , vol.68 , pp. 1518-1530
    • Cao, Y.1    Brown, L.S.2    Sasaki, J.3    Maeda, A.4    Needleman, R.5    Lanyi, J.K.6
  • 39
    • 0028864699 scopus 로고
    • Glutamic acid-204 is the terminal proton release group at the extracellular surface of bacteriorhodopsin
    • Brown, L.S., Sasaki, J., Kandori, H., Maeda, A., Needleman, R., and Lanyi, J.K. (1995) Glutamic acid-204 is the terminal proton release group at the extracellular surface of bacteriorhodopsin. J. Biol. Chem. 270, 27122-27126
    • (1995) J. Biol. Chem. , vol.270 , pp. 27122-27126
    • Brown, L.S.1    Sasaki, J.2    Kandori, H.3    Maeda, A.4    Needleman, R.5    Lanyi, J.K.6
  • 41
    • 0028783627 scopus 로고
    • The complex extracellular domain regulates the deprotonation and reprotonation of the retinal Schiff base during the bacteriorhodopsin photocycle
    • Brown, L.S., Váró, G., Hatanaka, M., Sasaki, J., Kandori, H., Maeda, A., Friedman, N., Sheves, J., Needleman, R., and Lanyi, J.K. (1995) The complex extracellular domain regulates the deprotonation and reprotonation of the retinal Schiff base during the bacteriorhodopsin photocycle. Biochemistry 34, 12903-12911
    • (1995) Biochemistry , vol.34 , pp. 12903-12911
    • Brown, L.S.1    Váró, G.2    Hatanaka, M.3    Sasaki, J.4    Kandori, H.5    Maeda, A.6    Friedman, N.7    Sheves, J.8    Needleman, R.9    Lanyi, J.K.10
  • 43
    • 0030012776 scopus 로고    scopus 로고
    • Effects of arginine-82 on the interactions of internal water molecules in bacteriorhodopsin
    • Hatanaka, M., Sasaki, J., Kandori, H., Ebrey, T.G., Needleman, R., Lanyi, J.K., and Maeda, A. (1996) Effects of arginine-82 on the interactions of internal water molecules in bacteriorhodopsin. Biochemistry 35, 6308-6312
    • (1996) Biochemistry , vol.35 , pp. 6308-6312
    • Hatanaka, M.1    Sasaki, J.2    Kandori, H.3    Ebrey, T.G.4    Needleman, R.5    Lanyi, J.K.6    Maeda, A.7
  • 44
    • 0024317089 scopus 로고
    • Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsin
    • Otto, H., Marti, T., Holz, M., Mogi, T., Lindau, M., Khorana, H.G., and Heyn, M.P. (1989) Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsin. Proc. Natl. Acad. Sci. USA 86, 9228-9232
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9228-9232
    • Otto, H.1    Marti, T.2    Holz, M.3    Mogi, T.4    Lindau, M.5    Khorana, H.G.6    Heyn, M.P.7
  • 45
    • 0026703071 scopus 로고
    • N intermediate with unprotonated Schiff base but N-like protein structure
    • N intermediate with unprotonated Schiff base but N-like protein structure. J. Biol. Chem. 267, 20782-20786
    • (1992) J. Biol. Chem. , vol.267 , pp. 20782-20786
    • Sasaki, J.1    Shichida, Y.2    Lanyi, J.K.3    Maeda, A.4
  • 47
    • 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
  • 48
    • 0030010796 scopus 로고    scopus 로고
    • D38 is an essential part of the proton translocation pathway in bacteriorhodopsin
    • Riesle, J., Oesterhelt, D., Dencher, N.A., and Heberlé, J. (1996) D38 is an essential part of the proton translocation pathway in bacteriorhodopsin. Biochemistry 35, 6635-6643
    • (1996) Biochemistry , vol.35 , pp. 6635-6643
    • Riesle, J.1    Oesterhelt, D.2    Dencher, N.A.3    Heberlé, J.4
  • 50
    • 0029969750 scopus 로고    scopus 로고
    • Relationship of retinal configuration and internal proton transfer at the end of the bacteriorhodopsin photocycle
    • Richter, H.-T., Needleman, R., Kandori, H., Maeda, A., and Lanyi, J.K. (1996) Relationship of retinal configuration and internal proton transfer at the end of the bacteriorhodopsin photocycle. Biochemistry 35, 15461-15466
    • (1996) Biochemistry , vol.35 , pp. 15461-15466
    • Richter, H.-T.1    Needleman, R.2    Kandori, H.3    Maeda, A.4    Lanyi, J.K.5
  • 51
    • 0028017506 scopus 로고
    • Identification of glutamic acid-113 as the Schiff base proton acceptor in the metarhodopsin II photointermediate of rhodopsin
    • Jäger, F., Fahmy, K., Sakmar, T.P., and Siebert, F. (1994) Identification of glutamic acid-113 as the Schiff base proton acceptor in the metarhodopsin II photointermediate of rhodopsin. Biochemistry 33, 10878-10882
    • (1994) Biochemistry , vol.33 , pp. 10878-10882
    • Jäger, F.1    Fahmy, K.2    Sakmar, T.P.3    Siebert, F.4
  • 52
    • 0028061193 scopus 로고
    • A conserved carboxylic acid group mediates light-dependent proton uptake and signaling by rhodopsin
    • Arnis, S., Fahmy, K., Hofmann, P.K., and Sakmar, T.P. (1994) A conserved carboxylic acid group mediates light-dependent proton uptake and signaling by rhodopsin. J. Biol. Chem. 269, 23879-23881
    • (1994) J. Biol. Chem. , vol.269 , pp. 23879-23881
    • Arnis, S.1    Fahmy, K.2    Hofmann, P.K.3    Sakmar, T.P.4
  • 53
    • 0027317273 scopus 로고
    • Two different forms of metarhodopsin II: Schiff base deprotonation precedes proton uptake and signaling state
    • Arnis, S.M. and Hofmann, K.P. (1993) Two different forms of metarhodopsin II: Schiff base deprotonation precedes proton uptake and signaling state. Proc. Natl. Acad. Sci. USA 90, 7849- 7853
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7849-7853
    • Arnis, S.M.1    Hofmann, K.P.2
  • 54
    • 0024550169 scopus 로고
    • Complete assignment of the hydrogen out-of-plane wagging vibrations of bathorhodopsin: Chromophore structure and energy storage in the primary photoproduct of vision
    • Palings, I., van den Berg, E.M.M., Lugtenburg, J., and Mathies, R.A. (1989) Complete assignment of the hydrogen out-of-plane wagging vibrations of bathorhodopsin: chromophore structure and energy storage in the primary photoproduct of vision. Biochemistry 28, 1498-1507
    • (1989) Biochemistry , vol.28 , pp. 1498-1507
    • Palings, I.1    Van den Berg, E.M.M.2    Lugtenburg, J.3    Mathies, R.A.4
  • 56
    • 0029120750 scopus 로고
    • Changes in structure of the chromophore in the photochemical process of bovine rhodopsin as revealed by FTIR spectroscopy for hydrogen-out-of- plane vibrations
    • Ohkita, Y.J., Susaki, J., Maeda, A., Yoshizawa, T., Groesheek, M., Verdegem, P., and Lugtenburg, J. (1995) Changes in structure of the chromophore in the photochemical process of bovine rhodopsin as revealed by FTIR spectroscopy for hydrogen-out-of- plane vibrations. Biophys. Chem. 56, 71-78
    • (1995) Biophys. Chem. , vol.56 , pp. 71-78
    • Ohkita, Y.J.1    Susaki, J.2    Maeda, A.3    Yoshizawa, T.4    Groesheek, M.5    Verdegem, P.6    Lugtenburg, J.7
  • 57
    • 0031054147 scopus 로고    scopus 로고
    • Structural dynamics of water and the peptide backbone around the Schiff base associated with the lightactivated process of octopus rhodopsin
    • Nishimura, S., Kandori, H., Nakagawa, M., Tsuda, M., and Maeda, A. (1996) Structural dynamics of water and the peptide backbone around the Schiff base associated with the lightactivated process of octopus rhodopsin. Biochemistry 36, 864-070
    • (1996) Biochemistry , vol.36 , pp. 864-1070
    • Nishimura, S.1    Kandori, H.2    Nakagawa, M.3    Tsuda, M.4    Maeda, A.5
  • 58
    • 0027259284 scopus 로고
    • Interaction of GTP-binding protein Gq with photoactivated rhodopsin in the photoreceptor membrane of crayfish
    • Terakita, A., Hariyama, T., Tsukahara, Y., Katsukura, Y., and Tashiro, H. (1993) Interaction of GTP-binding protein Gq with photoactivated rhodopsin in the photoreceptor membrane of crayfish. FEBS Lett. 330, 197-200
    • (1993) FEBS Lett. , vol.330 , pp. 197-200
    • Terakita, A.1    Hariyama, T.2    Tsukahara, Y.3    Katsukura, Y.4    Tashiro, H.5
  • 59
    • 0028803306 scopus 로고
    • FTIR spectroscopy reveals microscopic structural changes of the protein around the rhodopsin chromophore upon photoisomerization
    • Kandori, H. and Maeda, A. (1995) FTIR spectroscopy reveals microscopic structural changes of the protein around the rhodopsin chromophore upon photoisomerization. Biochemistry 34, 14220-14229
    • (1995) Biochemistry , vol.34 , pp. 14220-14229
    • Kandori, H.1    Maeda, A.2
  • 60
    • 0027365358 scopus 로고
    • Water structural changes in lumirhodopsin, metarhodopsin I, and metarhodopsin II upon photolysis of bovine rhodopsin: Analysis by Fourier transform infrared spectroscopy
    • Maeda, A., Ohkita, Y.J., Sasaki, J., Shichida, Y., and Yoshizawa, T. (1993) Water structural changes in lumirhodopsin, metarhodopsin I, and metarhodopsin II upon photolysis of bovine rhodopsin: Analysis by Fourier transform infrared spectroscopy. Biochemistry 32, 12033-12038
    • (1993) Biochemistry , vol.32 , pp. 12033-12038
    • Maeda, A.1    Ohkita, Y.J.2    Sasaki, J.3    Shichida, Y.4    Yoshizawa, T.5
  • 61
    • 0029566281 scopus 로고
    • Structural changes in the lumirhodopsin-to- metarhodopsin I conversion of air-dried bovine rhodopsin
    • Nishimura, S., Sasaki, J., Kandori, H., Lugtenburg, J., and Maeda, A. (1995) Structural changes in the lumirhodopsin-to- metarhodopsin I conversion of air-dried bovine rhodopsin, Biochemistry 34, 16758-16763
    • (1995) Biochemistry , vol.34 , pp. 16758-16763
    • Nishimura, S.1    Sasaki, J.2    Kandori, H.3    Lugtenburg, J.4    Maeda, A.5
  • 62
    • 0029848093 scopus 로고    scopus 로고
    • Structural changes in the peptide backbone in complex formation between activated rhodopsin and transducin studied by FTIR spectroscopy
    • Nishimura, S., Sasaki, J., Kandori, H., Matsuda, T., Fukada, Y., and Maeda, A. (1996) Structural changes in the peptide backbone in complex formation between activated rhodopsin and transducin studied by FTIR spectroscopy. Biochemistry 35, 13267- 13271
    • (1996) Biochemistry , vol.35 , pp. 13267-13271
    • Nishimura, S.1    Sasaki, J.2    Kandori, H.3    Matsuda, T.4    Fukada, Y.5    Maeda, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.