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Volumn 2, Issue C, 1996, Pages 33-139

Characterization of the primary photochemical events in bacteriorhodopsin and rhodopsin

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EID: 77957030452     PISSN: 18745342     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1874-5342(07)80005-5     Document Type: Article
Times cited : (47)

References (383)
  • 1
    • 77957026668 scopus 로고
    • The effects of aromatic amino acid substitutions in the putative helix F on the bacteriorhodopsin photocycle
    • (abstr.)
    • (abstr.). Ahl P.L., Stem L.J., Hackett N.R., Rothschild K.J., and Khorana H.G. The effects of aromatic amino acid substitutions in the putative helix F on the bacteriorhodopsin photocycle. Biophys. J. 51 (1987) 416
    • (1987) Biophys. J. , vol.51 , pp. 416
    • Ahl, P.L.1    Stem, L.J.2    Hackett, N.R.3    Rothschild, K.J.4    Khorana, H.G.5
  • 2
    • 0024297167 scopus 로고
    • Effects of amino acid substitutions in the F helix of bacteriorhodopsin. Low temperature ultraviolet/visible difference spectroscopy
    • Ahl P.L., Stern L.J., During D., Mogi T., Khorana H.G., and Rothschild K.J. Effects of amino acid substitutions in the F helix of bacteriorhodopsin. Low temperature ultraviolet/visible difference spectroscopy. J. Biol. Chem. 263 (1988) 13594-13601
    • (1988) J. Biol. Chem. , vol.263 , pp. 13594-13601
    • Ahl, P.L.1    Stern, L.J.2    During, D.3    Mogi, T.4    Khorana, H.G.5    Rothschild, K.J.6
  • 3
    • 0023759613 scopus 로고
    • Low retinal noise in animals with low body temperature allows high visual sensitivity
    • Aho A.C., Dormer K., Hyden C., Larsen L.O., and Reuter T. Low retinal noise in animals with low body temperature allows high visual sensitivity. Nature 334 (1988) 348-350
    • (1988) Nature , vol.334 , pp. 348-350
    • Aho, A.C.1    Dormer, K.2    Hyden, C.3    Larsen, L.O.4    Reuter, T.5
  • 4
    • 0011198630 scopus 로고
    • Role of retinal isomerizations and rotations in the photocycle of bacteriorhodopsin
    • Albeck A., Friedman N., Sheves M., and Ottolenghi M. Role of retinal isomerizations and rotations in the photocycle of bacteriorhodopsin. J. Am. Chem. Soc. 108 (1986) 4614-4618
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 4614-4618
    • Albeck, A.1    Friedman, N.2    Sheves, M.3    Ottolenghi, M.4
  • 6
    • 0026651047 scopus 로고
    • 13C NMR studies of model compounds for bacteriorhodopsin: factors affecting the retinal chromophore chemical shifts and absorption maximum
    • Albeck A., Livnah N., Gottlieb H., and Sheves M. 13C NMR studies of model compounds for bacteriorhodopsin: factors affecting the retinal chromophore chemical shifts and absorption maximum. J. Am. Chem. 114 (1992) 2400-2411
    • (1992) J. Am. Chem. , vol.114 , pp. 2400-2411
    • Albeck, A.1    Livnah, N.2    Gottlieb, H.3    Sheves, M.4
  • 7
    • 0001489561 scopus 로고
    • Sudden polarization in push-pull polyenes; a model exact study
    • Albert I.D.L., and Ramasesha S. Sudden polarization in push-pull polyenes; a model exact study. J. Phys. Chem. 94 (1990) 6540-6543
    • (1990) J. Phys. Chem. , vol.94 , pp. 6540-6543
    • Albert, I.D.L.1    Ramasesha, S.2
  • 9
    • 0011869670 scopus 로고
    • Ultraviolet resonance raman spectroscopy of bacteriorhodopsin: evidence against tyrosinate in the photocycle
    • Ames J.B., Bolton S.R., Netto M.M., and Mathies R.A. Ultraviolet resonance raman spectroscopy of bacteriorhodopsin: evidence against tyrosinate in the photocycle. J. Am. Chem. Soc. 112 (1990) 9007-9009
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 9007-9009
    • Ames, J.B.1    Bolton, S.R.2    Netto, M.M.3    Mathies, R.A.4
  • 10
    • 0026716606 scopus 로고
    • Time-resolved ultraviolet resonance Raman studies of protein structure: applications to bacteriorhodopsin
    • Ames J.B., Ros M., Raap J., Lugtenburg J., and Mathies R.A. Time-resolved ultraviolet resonance Raman studies of protein structure: applications to bacteriorhodopsin. Biochemistry 31 (1992) 5328-5334
    • (1992) Biochemistry , vol.31 , pp. 5328-5334
    • Ames, J.B.1    Ros, M.2    Raap, J.3    Lugtenburg, J.4    Mathies, R.A.5
  • 11
    • 0018088906 scopus 로고
    • Primary intermediates in the photochemical cycle of bacteriorhodopsin
    • Applebury M.L., Peters K.S., and Rentzepis R. Primary intermediates in the photochemical cycle of bacteriorhodopsin. Biophys. J. 23 (1978) 375-382
    • (1978) Biophys. J. , vol.23 , pp. 375-382
    • Applebury, M.L.1    Peters, K.S.2    Rentzepis, R.3
  • 12
    • 0025746480 scopus 로고
    • Fluorescence from the primary products of the bacteriorhodopsin photocycle
    • Atkinson G.H., Blanchard D., and Brack T.L. Fluorescence from the primary products of the bacteriorhodopsin photocycle. J. Lumin. 48 49 (1991) 410-414
    • (1991) J. Lumin. , vol.48 , Issue.49 , pp. 410-414
    • Atkinson, G.H.1    Blanchard, D.2    Brack, T.L.3
  • 13
    • 0024616590 scopus 로고
    • Picosecond time-re-solved fluorescence spectroscopy of K-590 in the bacteriorhodopsin photocycle
    • Atkinson G.H., Blanchard D., Lemaire H., Brach T.L., and Harashi H. Picosecond time-re-solved fluorescence spectroscopy of K-590 in the bacteriorhodopsin photocycle. Biophys. J. 55 (1989) 263-274
    • (1989) Biophys. J. , vol.55 , pp. 263-274
    • Atkinson, G.H.1    Blanchard, D.2    Lemaire, H.3    Brach, T.L.4    Harashi, H.5
  • 16
    • 84985091477 scopus 로고
    • On the absorption maxima of protonated retinal Schiff bases. An interaction with external charges
    • Baasov T., and Sheves M. On the absorption maxima of protonated retinal Schiff bases. An interaction with external charges. Israel J. Chem. 25 (1985) 53-55
    • (1985) Israel J. Chem. , vol.25 , pp. 53-55
    • Baasov, T.1    Sheves, M.2
  • 17
    • 0023228884 scopus 로고
    • Factors affecting the C=N stretching in protonated retinal schiff base: a model study for bacteriorhodopsin and visual pigments
    • Baasov T., Friedman N., and Sheves M. Factors affecting the C=N stretching in protonated retinal schiff base: a model study for bacteriorhodopsin and visual pigments. Biochemistry 26 (1987) 3210-3217
    • (1987) Biochemistry , vol.26 , pp. 3210-3217
    • Baasov, T.1    Friedman, N.2    Sheves, M.3
  • 18
    • 0342546940 scopus 로고
    • On the C=N stretching frequency of protonated retinal schiff bases
    • Ebrey T.G., Frauenfelder H., Honig B., and Nakanishi K. (Eds), University of Illinois Press
    • Baasov T., Friedman N., and Sheves M. On the C=N stretching frequency of protonated retinal schiff bases. In: Ebrey T.G., Frauenfelder H., Honig B., and Nakanishi K. (Eds). Biophysical studies of retinal proteins (1987), University of Illinois Press 252-261
    • (1987) Biophysical studies of retinal proteins , pp. 252-261
    • Baasov, T.1    Friedman, N.2    Sheves, M.3
  • 19
    • 0020174654 scopus 로고
    • Fourier-transform infrared difference spectroscopy of bacteriorhodopsin and its photoproducts
    • Bagley K., Dollinger G., Eisenstein L., Singh A.K., and Zimanyi L. Fourier-transform infrared difference spectroscopy of bacteriorhodopsin and its photoproducts. Proc. Natl. Acad. Sci. USA 79 (1982) 4972-4976
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 4972-4976
    • Bagley, K.1    Dollinger, G.2    Eisenstein, L.3    Singh, A.K.4    Zimanyi, L.5
  • 21
    • 0024599290 scopus 로고
    • A comparative study of the infrared difference spectra for octopus and bovine rhodopsins and their bathorhodopsin photointermediates
    • Bagley K.A., Eisenstein L., and Ebrey T.G. A comparative study of the infrared difference spectra for octopus and bovine rhodopsins and their bathorhodopsin photointermediates. Biochem-istry 28 (1989) 3366-3373
    • (1989) Biochem-istry , vol.28 , pp. 3366-3373
    • Bagley, K.A.1    Eisenstein, L.2    Ebrey, T.G.3
  • 22
    • 0025740089 scopus 로고
    • Red shift of the purple membrane absorption band and the deprotonation of tyrosine residues at high pH
    • Balashov S.P., Govindjee R., and Ebrey T.G. Red shift of the purple membrane absorption band and the deprotonation of tyrosine residues at high pH. Biophys. J. 60 (1991) 475-490
    • (1991) Biophys. J. , vol.60 , pp. 475-490
    • Balashov, S.P.1    Govindjee, R.2    Ebrey, T.G.3
  • 23
    • 77957086718 scopus 로고
    • Substitution of Arg82 with lysine in bacteriorhodopsin: effects on thermal isomeri-zation, photocycle, and proton release
    • Balashov S.P., Govindgee R., Imasheva E., Misra S., Ebrey T.G., Feng Y., Crouch R.K., and Menick D.R. Substitution of Arg82 with lysine in bacteriorhodopsin: effects on thermal isomeri-zation, photocycle, and proton release. Biophys. J. 66 (1994) A45
    • (1994) Biophys. J. , vol.66
    • Balashov, S.P.1    Govindgee, R.2    Imasheva, E.3    Misra, S.4    Ebrey, T.G.5    Feng, Y.6    Crouch, R.K.7    Menick, D.R.8
  • 24
    • 84989709558 scopus 로고
    • Quantum yield ratio of the forward and back light reactions of bacteriorhodopsin at low temperature and photosteady-state concentration of the bathoproduct K
    • Balashov S.P., Imasheva E.S., Govindjee R., and Ebrey T.G. Quantum yield ratio of the forward and back light reactions of bacteriorhodopsin at low temperature and photosteady-state concentration of the bathoproduct K. Photochem. Photobiol. 54 (1991) 955-961
    • (1991) Photochem. Photobiol. , vol.54 , pp. 955-961
    • Balashov, S.P.1    Imasheva, E.S.2    Govindjee, R.3    Ebrey, T.G.4
  • 25
    • 84989748901 scopus 로고
    • Bathoproducts and conformera of all-trans-and 13-cis-bacteriorhodopsin at 90 K
    • Balashov S.P., Kameyeva N.V., Litvin F.F., and Ebrey T.G. Bathoproducts and conformera of all-trans-and 13-cis-bacteriorhodopsin at 90 K. Photochem. Photobiol. 54 (1991) 949-953
    • (1991) Photochem. Photobiol. , vol.54 , pp. 949-953
    • Balashov, S.P.1    Kameyeva, N.V.2    Litvin, F.F.3    Ebrey, T.G.4
  • 26
    • 0024298870 scopus 로고
    • The thermal limit to seeing
    • Barlow H.B. The thermal limit to seeing. Nature 334 (1988) 296-350
    • (1988) Nature , vol.334 , pp. 296-350
    • Barlow, H.B.1
  • 27
    • 12944262375 scopus 로고
    • What is the origin of photoreceptor noise
    • Barlow Jr. R.B., and Kaplan E. What is the origin of photoreceptor noise. Biol. Bull. 177 (1989) 323
    • (1989) Biol. Bull. , vol.177 , pp. 323
    • Barlow Jr., R.B.1    Kaplan, E.2
  • 28
    • 12944288274 scopus 로고
    • Is photoreceptor noise caused by thermal isomerization of rhodopsin
    • Barlow Jr. R.B., and Silbaugh T.H. Is photoreceptor noise caused by thermal isomerization of rhodopsin. Invest. Ophthalmol. Vis. Sci. Suppl. 30 (1989) 61
    • (1989) Invest. Ophthalmol. Vis. Sci. , Issue.SUPPL. 30 , pp. 61
    • Barlow Jr., R.B.1    Silbaugh, T.H.2
  • 29
    • 0023103347 scopus 로고
    • Cicadian rhythms in Limulus photoreceptors I. Intracellular studies
    • Barlow Jr. R.B., Kaplan E., Renninger G.H., and Saito T. Cicadian rhythms in Limulus photoreceptors I. Intracellular studies. J. Gen Physiol. 89 (1987) 353-378
    • (1987) J. Gen Physiol. , vol.89 , pp. 353-378
    • Barlow Jr., R.B.1    Kaplan, E.2    Renninger, G.H.3    Saito, T.4
  • 31
    • 0026612756 scopus 로고
    • a values of ionizable groups in bacteriorhodopsin
    • a values of ionizable groups in bacteriorhodopsin. J. Mol. Biol. 224 (1992) 473-486
    • (1992) J. Mol. Biol. , vol.224 , pp. 473-486
    • Bashford, D.1    Gerwert, K.2
  • 32
    • 0019225828 scopus 로고
    • Two components of electrical dark noise in toad retinal rod outer segments
    • Baylor D.A., Matthews G., and Yau K.W. Two components of electrical dark noise in toad retinal rod outer segments. J. Physiol. 309 (1980) 591-621
    • (1980) J. Physiol. , vol.309 , pp. 591-621
    • Baylor, D.A.1    Matthews, G.2    Yau, K.W.3
  • 34
    • 0017597719 scopus 로고
    • The quantum efficiency for the photochemical conversion of the purple membrane protein
    • Becher B., and Ebrey T.G. The quantum efficiency for the photochemical conversion of the purple membrane protein. Biophys. J. 17 (1977) 185-191
    • (1977) Biophys. J. , vol.17 , pp. 185-191
    • Becher, B.1    Ebrey, T.G.2
  • 36
    • 0019349025 scopus 로고
    • Photophysics of light transduction in rhodopsin and bacteriorhodopsin
    • Birge R.R. Photophysics of light transduction in rhodopsin and bacteriorhodopsin. Ann. Rev. Biophys. Bioeng. 10 (1981) 315-354
    • (1981) Ann. Rev. Biophys. Bioeng. , vol.10 , pp. 315-354
    • Birge, R.R.1
  • 37
    • 0004064402 scopus 로고
    • Simulation of the primary event in rhodopsin photochemistry using semiempirical molecular dynamics theory
    • Alfano R.R. (Ed), Academic Press., New York
    • Birge R.R. Simulation of the primary event in rhodopsin photochemistry using semiempirical molecular dynamics theory. In: Alfano R.R. (Ed). Biological events probed by ultrafast laser spectroscopy (1982), Academic Press., New York 299-317
    • (1982) Biological events probed by ultrafast laser spectroscopy , pp. 299-317
    • Birge, R.R.1
  • 38
    • 33845375986 scopus 로고
    • Two-photon spectroscopy of protein-bound chromophores
    • Birge R.R. Two-photon spectroscopy of protein-bound chromophores. Acc. Chem. Res. 19 (1986) 138-146
    • (1986) Acc. Chem. Res. , vol.19 , pp. 138-146
    • Birge, R.R.1
  • 39
    • 0025303725 scopus 로고
    • Nature of the primary photochemical events in rhodopsin and bacteriorhodopsin. Biochim
    • Birge R.R. Nature of the primary photochemical events in rhodopsin and bacteriorhodopsin. Biochim. Biophys. Acta 1016 (1990) 293-327
    • (1990) Biophys. Acta , vol.1016 , pp. 293-327
    • Birge, R.R.1
  • 40
    • 0025653013 scopus 로고
    • Photophysics and molecular electronic applications of the rhodopsins
    • Birge R.R. Photophysics and molecular electronic applications of the rhodopsins. Annu. Rev. Phys. Chem. 41 (1990) 683-733
    • (1990) Annu. Rev. Phys. Chem. , vol.41 , pp. 683-733
    • Birge, R.R.1
  • 41
    • 0027193359 scopus 로고
    • a of the rhodopsin chromophore. Is this how nature minimizes photoreceptor noise?
    • a of the rhodopsin chromophore. Is this how nature minimizes photoreceptor noise?. Biophys. J. 64 (1993) 1371-1372
    • (1993) Biophys. J. , vol.64 , pp. 1371-1372
    • Birge, R.R.1
  • 42
    • 77957026282 scopus 로고
    • On the molecular origins of thermal noise in vertebrate and invertebrate photoreceptors
    • in press
    • in press. Birge R.R., and Barlow R.B. On the molecular origins of thermal noise in vertebrate and invertebrate photoreceptors. Biophys. Chem. (1994)
    • (1994) Biophys. Chem.
    • Birge, R.R.1    Barlow, R.B.2
  • 43
    • 0000419948 scopus 로고
    • Origins of inhomogeneous broadening in the vibronic spectra of visual chromophores and visual pigments
    • Birge R.R., Bocian D.F., and Hubbard L.M. Origins of inhomogeneous broadening in the vibronic spectra of visual chromophores and visual pigments. J. Am. Chem. Soc. 104 (1982) 1196-1207
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 1196-1207
    • Birge, R.R.1    Bocian, D.F.2    Hubbard, L.M.3
  • 44
    • 0008233847 scopus 로고
    • Quantum efficiencies of primary photochemical processes in vertebrate rhodopsin
    • Ebrey T., Frauenfelder H., Honig B., and Nakanishi K. (Eds), University of Illinois Press
    • Birge R.R., and Callender R.H. Quantum efficiencies of primary photochemical processes in vertebrate rhodopsin. In: Ebrey T., Frauenfelder H., Honig B., and Nakanishi K. (Eds). Biophysical studies of retinal proteins (1987), University of Illinois Press 270-281
    • (1987) Biophysical studies of retinal proteins , pp. 270-281
    • Birge, R.R.1    Callender, R.H.2
  • 45
    • 0020741491 scopus 로고
    • Energy storage in the primary step of the photocycle of bacteriorhodopsin
    • Birge R.R., and Cooper T.M. Energy storage in the primary step of the photocycle of bacteriorhodopsin. Biophys. J. 42 (1983) 61-69
    • (1983) Biophys. J. , vol.42 , pp. 61-69
    • Birge, R.R.1    Cooper, T.M.2
  • 46
    • 33845182926 scopus 로고
    • A spectroscopic, photocalorimetric and theoretical investigation of the quantum efficiency of the primary event in bacteriorhodopsin
    • Birge R.R., Cooper T.M., Lawrence A.F., Masthay M.B., Vasilakis C., Zhang C.F., and Zidovetzki R. A spectroscopic, photocalorimetric and theoretical investigation of the quantum efficiency of the primary event in bacteriorhodopsin. J. Am. Chem. Soc. 111 (1989) 4063-4074
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 4063-4074
    • Birge, R.R.1    Cooper, T.M.2    Lawrence, A.F.3    Masthay, M.B.4    Vasilakis, C.5    Zhang, C.F.6    Zidovetzki, R.7
  • 48
    • 0023845290 scopus 로고
    • The nature of the primary photochemical events in rhodopsin and isorhodopsin
    • Birge R.R., Einterz C.M., Knapp H.M., and Murray L.P. The nature of the primary photochemical events in rhodopsin and isorhodopsin. Biophys. J. 53 (1988) 367-385
    • (1988) Biophys. J. , vol.53 , pp. 367-385
    • Birge, R.R.1    Einterz, C.M.2    Knapp, H.M.3    Murray, L.P.4
  • 49
    • 0010306004 scopus 로고
    • Origins of the quantum efficiency duality in the primary photochemical event of bacteriorhodopsin
    • Birge R.R., and Mantsch H.H. (Eds), The International Society for Optical Engineering, Bellingham, Washing- ton
    • Birge R.R., Findsen L.A., Lawrence A.F., Masthay M.B., and Zhang C.F. Origins of the quantum efficiency duality in the primary photochemical event of bacteriorhodopsin. In: Birge R.R., and Mantsch H.H. (Eds). Biomolecular spectroscopy (1989), The International Society for Optical Engineering, Bellingham, Washing- ton 103-112
    • (1989) Biomolecular spectroscopy , pp. 103-112
    • Birge, R.R.1    Findsen, L.A.2    Lawrence, A.F.3    Masthay, M.B.4    Zhang, C.F.5
  • 50
    • 0000407691 scopus 로고
    • Molecular dynamics of the primary photochemical event in bacteriorhodopsin. Theoretical evidence for an excited singlet state assignment for the J intermediat
    • Birge R.R., Findsen L.A., and Pierce B.M. Molecular dynamics of the primary photochemical event in bacteriorhodopsin. Theoretical evidence for an excited singlet state assignment for the J intermediat. J. Am. Chem. Soc. 109 (1987) 5041-5043
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 5041-5043
    • Birge, R.R.1    Findsen, L.A.2    Pierce, B.M.3
  • 51
    • 0001078762 scopus 로고
    • Molecular dynamics of cis-trans isomerization in rhodopsin
    • Birge R.R., and Hubbard L.M. Molecular dynamics of cis-trans isomerization in rhodopsin. J. Am. Chem. Soc. 102 (1980) 2195-2204
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 2195-2204
    • Birge, R.R.1    Hubbard, L.M.2
  • 52
    • 0019421990 scopus 로고
    • Molecular dynamics of trans-cis isomerization in bathorhodop-sin
    • Birge R.R., and Hubbard L.M. Molecular dynamics of trans-cis isomerization in bathorhodop-sin. Biophys. J. 34 (1981) 517-534
    • (1981) Biophys. J. , vol.34 , pp. 517-534
    • Birge, R.R.1    Hubbard, L.M.2
  • 54
    • 0001754447 scopus 로고
    • Two-photon, 13C and two-dimen-sional 1H NMR spectroscopic studies of retinal schiff bases, protonated schiff bases, and schiff base salts: Evidence for a prot ππ* excited state level ordering reversal
    • Birge R.R., Murray L.P., Zidovetzki R., and Knapp H.M. Two-photon, 13C and two-dimen-sional 1H NMR spectroscopic studies of retinal schiff bases, protonated schiff bases, and schiff base salts: Evidence for a prot ππ* excited state level ordering reversal. J. Am. Chem. Soc. 109 (1987) 2090-2101
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 2090-2101
    • Birge, R.R.1    Murray, L.P.2    Zidovetzki, R.3    Knapp, H.M.4
  • 55
    • 84892222460 scopus 로고
    • The nature of the primary photochemical events in bacteriorho- dopsin and rhodopsin
    • Zewail A.H. (Ed), Harwood Academic
    • Birge R.R., and Pierce B.M. The nature of the primary photochemical events in bacteriorho- dopsin and rhodopsin. In: Zewail A.H. (Ed). Photochemistry and Photobiology (1983), Harwood Academic 841-855
    • (1983) Photochemistry and Photobiology , pp. 841-855
    • Birge, R.R.1    Pierce, B.M.2
  • 57
    • 36549094506 scopus 로고
    • Two-photon spectroscopy of light adapted bacteriorhodopsin
    • Birge R.R., and Zhang C.F. Two-photon spectroscopy of light adapted bacteriorhodopsin. J. Chem. Phys. 92 (1990) 7178-7195
    • (1990) J. Chem. Phys. , vol.92 , pp. 7178-7195
    • Birge, R.R.1    Zhang, C.F.2
  • 58
    • 0011549802 scopus 로고
    • Picosecond time-resolved absorption and fluorescence in the bacteriorhodopsin photocycle: Vibrationally-excited species
    • Blanchard D., Gilmore D.A., Brack T.L., Lemaire H., Hughes D., and Atkinson G.H. Picosecond time-resolved absorption and fluorescence in the bacteriorhodopsin photocycle: Vibrationally-excited species. Chem. Phys. 154 (1991) 155-170
    • (1991) Chem. Phys. , vol.154 , pp. 155-170
    • Blanchard, D.1    Gilmore, D.A.2    Brack, T.L.3    Lemaire, H.4    Hughes, D.5    Atkinson, G.H.6
  • 59
    • 0015510057 scopus 로고
    • Effect of selected hydrogen bonding solvents on the absorption maxima of n-retinylidene-n-butylammonium salts
    • Blatz P.E., and Mohler J.H. Effect of selected hydrogen bonding solvents on the absorption maxima of n-retinylidene-n-butylammonium salts. Biochemistry 11 (1972) 3240-3242
    • (1972) Biochemistry , vol.11 , pp. 3240-3242
    • Blatz, P.E.1    Mohler, J.H.2
  • 62
    • 0018936353 scopus 로고
    • Action spectrum and quantum efficiency for proton pumping in Halobacterium Halobium
    • Bogomolni R.A., Baker R.A., Lozier R.H., and Stoeckenius W. Action spectrum and quantum efficiency for proton pumping in Halobacterium Halobium. Biochemistry 19 (1980) 2152-2159
    • (1980) Biochemistry , vol.19 , pp. 2152-2159
    • Bogomolni, R.A.1    Baker, R.A.2    Lozier, R.H.3    Stoeckenius, W.4
  • 63
    • 0022053675 scopus 로고
    • Energy storage in the primary photoreaction of bovine rhodopsin. A photoacoustic study
    • Boucher F., and Leblanc R.M. Energy storage in the primary photoreaction of bovine rhodopsin. A photoacoustic study. Photochem. Photobiol. 41 (1985) 459-465
    • (1985) Photochem. Photobiol. , vol.41 , pp. 459-465
    • Boucher, F.1    Leblanc, R.M.2
  • 64
    • 0011164031 scopus 로고
    • Picosecond time-resolved resonance raman spectrum of the K-590 intermediate in the room temperature bacteriorhodopsin photocycle
    • Brack T.L., and Atkinson G.H. Picosecond time-resolved resonance raman spectrum of the K-590 intermediate in the room temperature bacteriorhodopsin photocycle. J. Molec. Struct. 214 (1989) 289-303
    • (1989) J. Molec. Struct. , vol.214 , pp. 289-303
    • Brack, T.L.1    Atkinson, G.H.2
  • 65
    • 0019123462 scopus 로고
    • Resonance raman evidence for an all-trans to 13-cis isomerization in the proton-pumping cycle of bacteriorhodopsin
    • Braiman M., and Mathies R. Resonance raman evidence for an all-trans to 13-cis isomerization in the proton-pumping cycle of bacteriorhodopsin. Biochemistry 19 (1980) 5421-5428
    • (1980) Biochemistry , vol.19 , pp. 5421-5428
    • Braiman, M.1    Mathies, R.2
  • 66
    • 0020008581 scopus 로고
    • Resonance raman spectra of bacteriorhodopsin's primary photo-product for a distorted 13-cis retinal chromophore
    • Braiman M., and Mathies R. Resonance raman spectra of bacteriorhodopsin's primary photo-product for a distorted 13-cis retinal chromophore. Proc. Natl. Acad. Sci. USA 79 (1982) 403-407
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 403-407
    • Braiman, M.1    Mathies, R.2
  • 67
    • 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. Vibrational spectroscopy of bacteriorhodopsin mutants: Light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212. Biochemistry 27 (1988) 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
  • 70
    • 0017226063 scopus 로고
    • Molecular flow resonance Raman effect from retinal and rhodopsin
    • Callender R.H., Doukas A., Crouch R., and Nakanishi K. Molecular flow resonance Raman effect from retinal and rhodopsin. Biochemistry 15 (1976) 1621-1629
    • (1976) Biochemistry , vol.15 , pp. 1621-1629
    • Callender, R.H.1    Doukas, A.2    Crouch, R.3    Nakanishi, K.4
  • 71
    • 0026332339 scopus 로고
    • Water is required for proton transfer from aspartate-96 to the bacteriorhodopsin schiff base
    • Cao Y., Váró G., Chang M., Ni B., Needleman R., and Lanyi J.K. Water is required for proton transfer from aspartate-96 to the bacteriorhodopsin schiff base. Biochemistry 30 (1991) 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
  • 73
    • 0016668270 scopus 로고
    • X-ray diffraction studies of retinal rods I structure of the disc membrane, effect of illumination
    • Chabre M. X-ray diffraction studies of retinal rods I structure of the disc membrane, effect of illumination. Biochim. Biophys. Acta 382 (1975) 322-335
    • (1975) Biochim. Biophys. Acta , vol.382 , pp. 322-335
    • Chabre, M.1
  • 74
    • 0020009436 scopus 로고
    • X-ray and neutron diffraction of retinal rod outer segments
    • Packer L. (Ed), Academic Press, New York
    • Chabre M., and Worcester D.L. X-ray and neutron diffraction of retinal rod outer segments. In: Packer L. (Ed). Methods in Enzymology (1982), Academic Press, New York 593-604
    • (1982) Methods in Enzymology , pp. 593-604
    • Chabre, M.1    Worcester, D.L.2
  • 75
    • 0020006157 scopus 로고
    • Linear dichroism studies in the visible, UV, and IR on oriented rod suspensions
    • Packer L. (Ed), Academic Press, New York
    • Chabre M., Breton J., Michel-Villaz M., and Saibil H. Linear dichroism studies in the visible, UV, and IR on oriented rod suspensions. In: Packer L. (Ed). Methods in Enzymology (1982), Academic Press, New York 605-616
    • (1982) Methods in Enzymology , pp. 605-616
    • Chabre, M.1    Breton, J.2    Michel-Villaz, M.3    Saibil, H.4
  • 77
    • 0018851718 scopus 로고
    • Surface-induced lamellar orientation of multilayer membrane arrays: Theoretical analysis and a new method with applica-tions to purple membrane fragments
    • Clark N.A., Rothschild K.J., Luippold D.A., and Simon B.A. Surface-induced lamellar orientation of multilayer membrane arrays: Theoretical analysis and a new method with applica-tions to purple membrane fragments. Biophys. J. 31 (1980) 65-96
    • (1980) Biophys. J. , vol.31 , pp. 65-96
    • Clark, N.A.1    Rothschild, K.J.2    Luippold, D.A.3    Simon, B.A.4
  • 78
    • 0018386110 scopus 로고
    • Energies of rhodopsin and isorhodopsin
    • Cooper A. Energies of rhodopsin and isorhodopsin. FEBS Lett 100 (1979) 382-384
    • (1979) FEBS Lett , vol.100 , pp. 382-384
    • Cooper, A.1
  • 79
    • 0018567294 scopus 로고
    • Energy uptake in the first step of visual excitation
    • Cooper A. Energy uptake in the first step of visual excitation. Nature 282 (1979) 531-533
    • (1979) Nature , vol.282 , pp. 531-533
    • Cooper, A.1
  • 80
    • 0021441921 scopus 로고
    • Theory and design of a tunable pulsed dye laser cryogenic photocalorimeter
    • Cooper T.M., Schmidt H.H., Murray L.P., and Birge R.R. Theory and design of a tunable pulsed dye laser cryogenic photocalorimeter. Rev. Sci. Instrm. 55 (1984) 896-904
    • (1984) Rev. Sci. Instrm. , vol.55 , pp. 896-904
    • Cooper, T.M.1    Schmidt, H.H.2    Murray, L.P.3    Birge, R.R.4
  • 81
    • 0028314521 scopus 로고
    • Deuterium solid-state nuclear magnetic resonance studies of methyl group dynamics in bacteriorhodopsin and retinal model compounds: evidence for a 6-s-transchromophore in the protein
    • Copié V., McDermott A.E., Beshah K., Williams J.C., Spijker-Assink M., Gebhard R., Lugtenburg J.L., Herzfeld J., and Griffm R.G. Deuterium solid-state nuclear magnetic resonance studies of methyl group dynamics in bacteriorhodopsin and retinal model compounds: evidence for a 6-s-transchromophore in the protein. Biochemistry 33 (1994) 3280-3286
    • (1994) Biochemistry , vol.33 , pp. 3280-3286
    • Copié, V.1    McDermott, A.E.2    Beshah, K.3    Williams, J.C.4    Spijker-Assink, M.5    Gebhard, R.6    Lugtenburg, J.L.7    Herzfeld, J.8    Griffm, R.G.9
  • 83
    • 1342263269 scopus 로고
    • Isorhodopsin II: Artificial photosensitive pigment formed from 9, 13-dicis retinal
    • Crouch R., Purvin V., Nakanishi K., and Ebrey T. Isorhodopsin II: Artificial photosensitive pigment formed from 9, 13-dicis retinal. Proc. Natl. Acad. Sci. USA 72 (1975) 1538-1542
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 1538-1542
    • Crouch, R.1    Purvin, V.2    Nakanishi, K.3    Ebrey, T.4
  • 85
    • 0000827010 scopus 로고
    • Independent photocycles of the spectrally distinct forms of bacteriorhodopsin
    • Dancshazy Z., Govindjee R., and Ebrey T.G. Independent photocycles of the spectrally distinct forms of bacteriorhodopsin. Proc. Natl. Acad. Sci. USA 85 (1988) 6358-6361
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 6358-6361
    • Dancshazy, Z.1    Govindjee, R.2    Ebrey, T.G.3
  • 86
    • 0001682751 scopus 로고
    • Photosensitivity
    • Dartnall H.J.A. (Ed), Springer-Verlag, Heidelberg
    • Dartnall H.J.A. Photosensitivity. In: Dartnall H.J.A. (Ed). Handbook of sensory physiology (1972), Springer-Verlag, Heidelberg 122-145
    • (1972) Handbook of sensory physiology , pp. 122-145
    • Dartnall, H.J.A.1
  • 87
    • 84995087467 scopus 로고
    • Spectroscopy of polyenes III. Absorption and emission spectral investigation of polyene Schiff bases and protonated Schiff bases related to visual pigments
    • Das P.K., Kogan G., and Becker R.S. Spectroscopy of polyenes III. Absorption and emission spectral investigation of polyene Schiff bases and protonated Schiff bases related to visual pigments. Photochem. Photobiol. 30 (1979) 689-695
    • (1979) Photochem. Photobiol. , vol.30 , pp. 689-695
    • Das, P.K.1    Kogan, G.2    Becker, R.S.3
  • 89
    • 0024102514 scopus 로고
    • Photoexcitation of rhodopsin: conformation changes in the chromophore, protein and associated lipids as determined by FTIR difference spectroscopy
    • DeGrip W.J., Gray D., Gillespie J., Bovee P.H.M., Van den Berg E.M.M., Lugtenburg J., and Rothschild K.J. Photoexcitation of rhodopsin: conformation changes in the chromophore, protein and associated lipids as determined by FTIR difference spectroscopy. Photochem. Photo-biol. 48 (1988) 497-504
    • (1988) Photochem. Photo-biol. , vol.48 , pp. 497-504
    • DeGrip, W.J.1    Gray, D.2    Gillespie, J.3    Bovee, P.H.M.4    Van den Berg, E.M.M.5    Lugtenburg, J.6    Rothschild, K.J.7
  • 90
    • 0023658614 scopus 로고
    • A study of the Schiff base mode in bovine rhodopsin and bathorhodopsin
    • Deng H., and Callender R.H. A study of the Schiff base mode in bovine rhodopsin and bathorhodopsin. Biochemistry 26 (1987) 7418-7426
    • (1987) Biochemistry , vol.26 , pp. 7418-7426
    • Deng, H.1    Callender, R.H.2
  • 93
    • 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/de
    • Deng H., Haung L., Callender R., and Ebrey T. 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/de. Biophys. J. 66 (1994) 1129-1136
    • (1994) Biophys. J. , vol.66 , pp. 1129-1136
    • Deng, H.1    Haung, L.2    Callender, R.3    Ebrey, T.4
  • 95
    • 0001357710 scopus 로고
    • Kinetic resonance Raman studies reveal different conformational states of bacteriorhodospin
    • Diller R., and Stockburger M. Kinetic resonance Raman studies reveal different conformational states of bacteriorhodospin. Biochemistry 27 (1988) 7641-7651
    • (1988) Biochemistry , vol.27 , pp. 7641-7651
    • Diller, R.1    Stockburger, M.2
  • 99
    • 84985448079 scopus 로고
    • Analysis of primary photochemical processes in bacteriorhodopsin
    • Dinur U., Honig B., and Ottolenghi M. Analysis of primary photochemical processes in bacteriorhodopsin. Photochem. Photobiol. 33 (1981) 523-527
    • (1981) Photochem. Photobiol. , vol.33 , pp. 523-527
    • Dinur, U.1    Honig, B.2    Ottolenghi, M.3
  • 100
    • 5844377779 scopus 로고
    • Quantum yield and extinction measurements in strongly overlapping reactant and photoproduct absorption bands II. Bathointermediate formation inbacteriorhodopsin photocycle at room temperature
    • Dioumaev A.K., Savroansky V.V., Tkachemko N.V., and Chukharev V.I. Quantum yield and extinction measurements in strongly overlapping reactant and photoproduct absorption bands II. Bathointermediate formation inbacteriorhodopsin photocycle at room temperature. J. Photochem. Photobiol B. 3 (1989) 397-410
    • (1989) J. Photochem. Photobiol B. , vol.3 , pp. 397-410
    • Dioumaev, A.K.1    Savroansky, V.V.2    Tkachemko, N.V.3    Chukharev, V.I.4
  • 101
    • 0001649161 scopus 로고
    • Excited-state reaction dynamics of bacteri-orhodopsin studied by femtosecond spectroscopy
    • Dobler J., Zinth W., Kaiser W., and Oesterhelt D. Excited-state reaction dynamics of bacteri-orhodopsin studied by femtosecond spectroscopy. Chem. Phys. Lett. 144 (1988) 215-220
    • (1988) Chem. Phys. Lett. , vol.144 , pp. 215-220
    • Dobler, J.1    Zinth, W.2    Kaiser, W.3    Oesterhelt, D.4
  • 102
    • 33751500154 scopus 로고
    • Picosecond time-resolved resonance raman spectroscopy of bacteriorhodopsin's J, K, and KL intermediates
    • Doig S.J., Reid P.J., and Mathies R.A. Picosecond time-resolved resonance raman spectroscopy of bacteriorhodopsin's J, K, and KL intermediates. J. Phys. Chem. 95 (1991) 6372-6379
    • (1991) J. Phys. Chem. , vol.95 , pp. 6372-6379
    • Doig, S.J.1    Reid, P.J.2    Mathies, R.A.3
  • 103
    • 0023054728 scopus 로고
    • Fourier transform infrared difference spectroscopy of bacteriorhodopsin and its photoproducts regenerated with deuterated tyrosine
    • Dollinger G., Eisenstein L., Lin S.-L., Nakanishi K., and Termini J. Fourier transform infrared difference spectroscopy of bacteriorhodopsin and its photoproducts regenerated with deuterated tyrosine. Biochemistry 25 (1986) 6524-6533
    • (1986) Biochemistry , vol.25 , pp. 6524-6533
    • Dollinger, G.1    Eisenstein, L.2    Lin, S.-L.3    Nakanishi, K.4    Termini, J.5
  • 104
    • 0342546940 scopus 로고
    • The role of tyrosine in the proton pump of bacteriorhodopsin
    • Ebrey T.G., Frauenfelder H., Honig B., and Nakanishi K. (Eds), University of Illinois Press
    • Dollinger G., Eisenstein L., Lin S.L., Nakanishi K., and Termini J. The role of tyrosine in the proton pump of bacteriorhodopsin. In: Ebrey T.G., Frauenfelder H., Honig B., and Nakanishi K. (Eds). Biophysical studies of retinal proteins (1987), University of Illinois Press 120-125
    • (1987) Biophysical studies of retinal proteins , pp. 120-125
    • Dollinger, G.1    Eisenstein, L.2    Lin, S.L.3    Nakanishi, K.4    Termini, J.5
  • 106
  • 108
    • 0027752269 scopus 로고
    • Femtosecond time-resolved fluorescence spectroscopy of bacteri-orhodopsin: direct observation of the excited state dynamics in the primary step of the proton
    • Du M., and Fleming G.R. Femtosecond time-resolved fluorescence spectroscopy of bacteri-orhodopsin: direct observation of the excited state dynamics in the primary step of the proton. Biophys. Chem. 48 (1993) 101-111
    • (1993) Biophys. Chem. , vol.48 , pp. 101-111
    • Du, M.1    Fleming, G.R.2
  • 109
    • 0025080570 scopus 로고
    • Ultraviolet-visible transient spectroscopy of bacteriorhdopsin mutants. Evidence for two forms of tyrosine-185 → phenylalanine
    • Dunach M., Berkowitz S., Marti T., He Y.-W., Subramanian S., Khorana H.G., and Rothschild K.J. Ultraviolet-visible transient spectroscopy of bacteriorhdopsin mutants. Evidence for two forms of tyrosine-185 → phenylalanine. J. Biol. Chem. 265 28 (1990) 16978-16984
    • (1990) J. Biol. Chem. , vol.265 , Issue.28 , pp. 16978-16984
    • Dunach, M.1    Berkowitz, S.2    Marti, T.3    He, Y.-W.4    Subramanian, S.5    Khorana, H.G.6    Rothschild, K.J.7
  • 110
    • 0023040477 scopus 로고
    • Orientation of the bacteriorhodopsin chromophore probed by polarized fourier transform infrared difference spec-troscopy
    • Earnest T.N., Roepe P., Braiman M.S., Gillespie J., and Rothschild K.J. Orientation of the bacteriorhodopsin chromophore probed by polarized fourier transform infrared difference spec-troscopy. Biochemistry 25 (1986) 7793-7798
    • (1986) Biochemistry , vol.25 , pp. 7793-7798
    • Earnest, T.N.1    Roepe, P.2    Braiman, M.S.3    Gillespie, J.4    Rothschild, K.J.5
  • 111
    • 0002979180 scopus 로고
    • Light energy transduction in bacteriorhodopsin
    • Jackson M.B. (Ed), CRC Press, Boca Raton
    • Ebrey T.G. Light energy transduction in bacteriorhodopsin. In: Jackson M.B. (Ed). Thermo- dynamics of membrane receptors and channels (1993), CRC Press, Boca Raton 353-387
    • (1993) Thermo- dynamics of membrane receptors and channels , pp. 353-387
    • Ebrey, T.G.1
  • 112
    • 0038822849 scopus 로고
    • Spectral and kinetic evidence for the existence of two forms of bathorhodopsin
    • Einterz C.M., Lewis J.W., and Kliger D.S. Spectral and kinetic evidence for the existence of two forms of bathorhodopsin. Proc. Natl. Acad. Sci. USA 84 (1987) 3699-3703
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3699-3703
    • Einterz, C.M.1    Lewis, J.W.2    Kliger, D.S.3
  • 113
    • 0342546940 scopus 로고
    • Two forms of bathorhodopsin: Laser power dependence
    • Ebrey T.G., Frauenfelder H., Honig B., and Nakanishi K. (Eds), University of Illinois Press
    • Einterz C.M., Lewis J.W., and Kliger D.S. Two forms of bathorhodopsin: Laser power dependence. In: Ebrey T.G., Frauenfelder H., Honig B., and Nakanishi K. (Eds). Biophysical studies of retinal proteins (1987), University of Illinois Press 282-286
    • (1987) Biophysical studies of retinal proteins , pp. 282-286
    • Einterz, C.M.1    Lewis, J.W.2    Kliger, D.S.3
  • 114
    • 0027317955 scopus 로고
    • Resonance Raman and optical transient studies on the light-induced proton pump of bacteriorhodopsin reveal parallel photocycles
    • Eisfeld W., Pusch C., Diller R., Lohrmann R., and Stockburger M. Resonance Raman and optical transient studies on the light-induced proton pump of bacteriorhodopsin reveal parallel photocycles. Biochemistry 32 (1993) 7196-7215
    • (1993) Biochemistry , vol.32 , pp. 7196-7215
    • Eisfeld, W.1    Pusch, C.2    Diller, R.3    Lohrmann, R.4    Stockburger, M.5
  • 115
    • 0018345284 scopus 로고
    • Resonance Raman studies of bathorhodopsin: Evidence for a protonated Schiff base linkage
    • Eyring G., and Mathies R. Resonance Raman studies of bathorhodopsin: Evidence for a protonated Schiff base linkage. Proc. Natl. Acad. Sci. USA 76 (1979) 33-37
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 33-37
    • Eyring, G.1    Mathies, R.2
  • 116
    • 0027820508 scopus 로고
    • Light-dependent transducin activation by an ultraviolet-absorbing rhodopsin mutant
    • Fahmy K., and Sakmar T.P. Light-dependent transducin activation by an ultraviolet-absorbing rhodopsin mutant. Biochemistry 32 (1993) 9165-9171
    • (1993) Biochemistry , vol.32 , pp. 9165-9171
    • Fahmy, K.1    Sakmar, T.P.2
  • 117
    • 0001385068 scopus 로고
    • Photoisomerization in bacteriorhodopsin studied by FTIF., linear dichroism and photoselection experiments combined with quantum chemical theoretical analysis
    • Fahmy K., Siebert F., Großjean M.F., and Tavan P. Photoisomerization in bacteriorhodopsin studied by FTIF., linear dichroism and photoselection experiments combined with quantum chemical theoretical analysis. J. Molec. Struct. 214 (1989) 257-288
    • (1989) J. Molec. Struct. , vol.214 , pp. 257-288
    • Fahmy, K.1    Siebert, F.2    Großjean, M.F.3    Tavan, P.4
  • 118
    • 0025757368 scopus 로고
    • Structural investigation of bacteriorhodopsin and some of its photoproducts by polarized fourier transform infrared spectroscopic methods-differencespec-troscopy and photoselection
    • Fahmy K., Siebert F., and Tavan P. Structural investigation of bacteriorhodopsin and some of its photoproducts by polarized fourier transform infrared spectroscopic methods-differencespec-troscopy and photoselection. Biophys. J. 60 (1991) 989-1001
    • (1991) Biophys. J. , vol.60 , pp. 989-1001
    • Fahmy, K.1    Siebert, F.2    Tavan, P.3
  • 119
    • 33845550093 scopus 로고
    • Evidence for the necessity of double-bond (13-Ene) isomerization in the proton pumping of bacteriorhodopsin
    • Fang J.M., Carriker J.D., Balogh-Nair V., and Nakanishi K. Evidence for the necessity of double-bond (13-Ene) isomerization in the proton pumping of bacteriorhodopsin. J. Am. Chem. Soc. 105 (1983) 5162-5164
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 5162-5164
    • Fang, J.M.1    Carriker, J.D.2    Balogh-Nair, V.3    Nakanishi, K.4
  • 123
    • 26944439297 scopus 로고
    • Rhodopsin activation: A novel view suggested by in vivo Chlamydomonas experiments
    • Foster K.W., and Saranak J. Rhodopsin activation: A novel view suggested by in vivo Chlamydomonas experiments. J. Am. Chem. Soc. 110 (1988) 6588-6589
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 6588-6589
    • Foster, K.W.1    Saranak, J.2
  • 124
    • 0024076241 scopus 로고
    • Autoregulation of rhodopsin synthesis in Chlamydo-monas reinhardtii
    • Foster K.W., Saranak J., and Zarrilli G. Autoregulation of rhodopsin synthesis in Chlamydo-monas reinhardtii. Proc. Natl. Acad. Sci. USA 85 (1988) 6379-6383
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 6379-6383
    • Foster, K.W.1    Saranak, J.2    Zarrilli, G.3
  • 126
    • 0000123518 scopus 로고
    • Comprehensive investigation of the photoisomerization of the protonated and unprotonated Schiff bases of 9-cis, 11 -cis, 13-cis, and all-trans retinal
    • Freedman K., and Becker R.S. Comprehensive investigation of the photoisomerization of the protonated and unprotonated Schiff bases of 9-cis, 11 -cis, 13-cis, and all-trans retinal. J. Am. Chem. Soc. 108 (1986) 1245-1251
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 1245-1251
    • Freedman, K.1    Becker, R.S.2
  • 127
    • 0022687552 scopus 로고
    • Investigation into the spectroscopy and photoisomerization of a series of poly (ethyleneglycol) peptide Schiff bases of 11 -cis retinal
    • Freedman K., Becker R.S., Hannak D., and Bayer E. Investigation into the spectroscopy and photoisomerization of a series of poly (ethyleneglycol) peptide Schiff bases of 11 -cis retinal. Photochem. Photobiol. 43 (1986) 291-295
    • (1986) Photochem. Photobiol. , vol.43 , pp. 291-295
    • Freedman, K.1    Becker, R.S.2    Hannak, D.3    Bayer, E.4
  • 128
    • 0025273351 scopus 로고
    • Comparative study on the chromophore binding sites of rod and red-sensitive cone visual pigments by use of synthetic retinal isomers and analogues
    • Fukuda Y., Okano T., Shichida Y., Yoshizawa T., Trehan A., Mead D., Denny M., Asato A., and Liu R.S.H. Comparative study on the chromophore binding sites of rod and red-sensitive cone visual pigments by use of synthetic retinal isomers and analogues. Biochemistry 29 (1990) 3133-3140
    • (1990) Biochemistry , vol.29 , pp. 3133-3140
    • Fukuda, Y.1    Okano, T.2    Shichida, Y.3    Yoshizawa, T.4    Trehan, A.5    Mead, D.6    Denny, M.7    Asato, A.8    Liu, R.S.H.9
  • 129
    • 0024293241 scopus 로고
    • Rhodopsin-lumirhodopsin phototransition of bovine rhodopsin investigated by Fourier transform infrared difference spectroscopy
    • Ganter U.M., Gartner W., and Siebert F. Rhodopsin-lumirhodopsin phototransition of bovine rhodopsin investigated by Fourier transform infrared difference spectroscopy. Biochemistry 27 (1988) 7480-7488
    • (1988) Biochemistry , vol.27 , pp. 7480-7488
    • Ganter, U.M.1    Gartner, W.2    Siebert, F.3
  • 130
    • 0024200660 scopus 로고
    • The photoreaction of vacuum-dried rhodopsin at low temperature: evidence for charge stabilization by water
    • Ganter U.M., Schmid E.D., and Siebert F. The photoreaction of vacuum-dried rhodopsin at low temperature: evidence for charge stabilization by water. J. Photochem. Photobiol. B. 2 (1988) 417-426
    • (1988) J. Photochem. Photobiol. B. , vol.2 , pp. 417-426
    • Ganter, U.M.1    Schmid, E.D.2    Siebert, F.3
  • 131
    • 0027509599 scopus 로고
    • Quantitative characterization of the structure of rhodopsin in disc membrane by means of fourier transform infrared spectroscopy
    • Garcia-Quintana D., Garriga P., and Manyosa J. Quantitative characterization of the structure of rhodopsin in disc membrane by means of fourier transform infrared spectroscopy. J. Biol. Chem. 268 (1993) 2403-2409
    • (1993) J. Biol. Chem. , vol.268 , pp. 2403-2409
    • Garcia-Quintana, D.1    Garriga, P.2    Manyosa, J.3
  • 132
    • 0026264506 scopus 로고
    • Quantum yield of chapso-solubilized rhodopsin and 3-hydroxy retinal containing bovine opsin
    • Gärtner W., Ullrich D., and Vogt K. Quantum yield of chapso-solubilized rhodopsin and 3-hydroxy retinal containing bovine opsin. Photochem. Photobiol. 54 (1991) 1047-1055
    • (1991) Photochem. Photobiol. , vol.54 , pp. 1047-1055
    • Gärtner, W.1    Ullrich, D.2    Vogt, K.3
  • 133
    • 0000559536 scopus 로고
    • a of the retinal protonated Schiff base in retinal proteins. A study with model compounds
    • a of the retinal protonated Schiff base in retinal proteins. A study with model compounds. J. Am. Chem. Soc. 115 (1993) 3772-3773
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 3772-3773
    • Gat, Y.1    Sheves, M.2
  • 134
    • 0026552909 scopus 로고
    • Participation of bacteriorhodopsin active-site lysine backbone in vibrations associated with retinal photochem-istry
    • Gat Y., Grossjean M., Pinevsky I., Takei H., Rothman Z., Sigrist H., and Lewis A. Participation of bacteriorhodopsin active-site lysine backbone in vibrations associated with retinal photochem-istry. Proc. Natl. Acad. Sci. USA 89 (1992) 2434-2438
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 2434-2438
    • Gat, Y.1    Grossjean, M.2    Pinevsky, I.3    Takei, H.4    Rothman, Z.5    Sigrist, H.6    Lewis, A.7
  • 135
    • 0342546940 scopus 로고
    • Initiation of light-induced proton transfers in bacteriorhodopsin monitored by FTIR difference spectroscopy
    • Ebrey T.G., Frauenfelder H., Honig B., and Nakanishi K. (Eds), University of Illinois Press
    • Gerwert K., and Hess B. Initiation of light-induced proton transfers in bacteriorhodopsin monitored by FTIR difference spectroscopy. In: Ebrey T.G., Frauenfelder H., Honig B., and Nakanishi K. (Eds). Biophysical studies of retinal proteins (1987), University of Illinois Press 144-148
    • (1987) Biophysical studies of retinal proteins , pp. 144-148
    • Gerwert, K.1    Hess, B.2
  • 136
    • 0000311181 scopus 로고
    • Evidence for light-induced 13-cis, 14-s-cis isomerization in bacteri-orhodopsin obtained by FTIR difference spectroscopy using isotopically labelled retinals
    • Gerwert K., and Siebert F. Evidence for light-induced 13-cis, 14-s-cis isomerization in bacteri-orhodopsin obtained by FTIR difference spectroscopy using isotopically labelled retinals. EMBO 5 (1986) 805-811
    • (1986) EMBO , vol.5 , pp. 805-811
    • Gerwert, K.1    Siebert, F.2
  • 137
    • 77957073812 scopus 로고
    • Retinal can regulate global conformational changes of the bacteriorhodopsins in the light-mediated sodium-borohydride-reduced purple membrane
    • Ebrey T.G., Frauenfelder H., Honig B., and Nakanishi K. (Eds), University of Illinois Press
    • Gibson N.J., and Cassim J.Y. Retinal can regulate global conformational changes of the bacteriorhodopsins in the light-mediated sodium-borohydride-reduced purple membrane. In: Ebrey T.G., Frauenfelder H., Honig B., and Nakanishi K. (Eds). Biophysical studies of retinal proteins (1987), University of Illinois Press 71-79
    • (1987) Biophysical studies of retinal proteins , pp. 71-79
    • Gibson, N.J.1    Cassim, J.Y.2
  • 138
    • 0023959207 scopus 로고
    • Analysis of the factors that influence the C=N stretching frequency of polyene schiff bases
    • Gilson H.S.R., Honig B.H., Croteau A., Zarrilli G., and Nakanishi K. Analysis of the factors that influence the C=N stretching frequency of polyene schiff bases. Biophys. J. 53 (1988) 261-269
    • (1988) Biophys. J. , vol.53 , pp. 261-269
    • Gilson, H.S.R.1    Honig, B.H.2    Croteau, A.3    Zarrilli, G.4    Nakanishi, K.5
  • 139
    • 0017062945 scopus 로고
    • On the primary quantum yield in the bacteriorhodopsin photocyle
    • Goldschmidt C.R., Ottolenghi M., and Korenstein R. On the primary quantum yield in the bacteriorhodopsin photocyle. Biophys. J. 16 (1976) 839-843
    • (1976) Biophys. J. , vol.16 , pp. 839-843
    • Goldschmidt, C.R.1    Ottolenghi, M.2    Korenstein, R.3
  • 141
    • 0018897008 scopus 로고
    • The quantum efficiency of proton pumping by the purple membrane of Halobacterium halobium
    • Govindjee R., Ebrey T.G., and Crofts A.R. The quantum efficiency of proton pumping by the purple membrane of Halobacterium halobium. Biophys. J. 30 (1980) 231-240
    • (1980) Biophys. J. , vol.30 , pp. 231-240
    • Govindjee, R.1    Ebrey, T.G.2    Crofts, A.R.3
  • 143
    • 0025034111 scopus 로고
    • Quantum efficiency of the photochemical cycle of bacteriorhodopsin
    • Govindjee R., Balashov S.P., and Ebrey T.G. Quantum efficiency of the photochemical cycle of bacteriorhodopsin. Biophys. J. 58 (1990) 597-608
    • (1990) Biophys. J. , vol.58 , pp. 597-608
    • Govindjee, R.1    Balashov, S.P.2    Ebrey, T.G.3
  • 144
    • 0017769863 scopus 로고
    • Cis-trans isomerization of rhodopsin in picoseconds
    • Green B., Monger T., Alfano R., Anton B., and Callender R.H. Cis-trans isomerization of rhodopsin in picoseconds. Nature 269 (1977) 179-180
    • (1977) Nature , vol.269 , pp. 179-180
    • Green, B.1    Monger, T.2    Alfano, R.3    Anton, B.4    Callender, R.H.5
  • 145
    • 0027218962 scopus 로고
    • Hydrophobie amino acids in the retinal-binding pocket of bacteriorhodopsin
    • Greenhalgh D.A., Farrens D.L., Subramaniam S., and Khorana H.G. Hydrophobie amino acids in the retinal-binding pocket of bacteriorhodopsin. J. Biophys. Chem. 268 (1993) 20305-20311
    • (1993) J. Biophys. Chem. , vol.268 , pp. 20305-20311
    • Greenhalgh, D.A.1    Farrens, D.L.2    Subramaniam, S.3    Khorana, H.G.4
  • 146
    • 0027051284 scopus 로고
    • Effect of introducing different carboxylate-containing side chains at position 85 on chromophore formation and proton transport in bacteriorhodopsin
    • Greenhalgh D.A., Subramaniam S., Alexiev U., Otto H., Heyn M.P., and Khorana H.G. Effect of introducing different carboxylate-containing side chains at position 85 on chromophore formation and proton transport in bacteriorhodopsin. J. Biol. Chem. 267 (1992) 25734-25738
    • (1992) J. Biol. Chem. , vol.267 , pp. 25734-25738
    • Greenhalgh, D.A.1    Subramaniam, S.2    Alexiev, U.3    Otto, H.4    Heyn, M.P.5    Khorana, H.G.6
  • 147
    • 4043061269 scopus 로고
    • A Flash-photolytic investigation of rhodopsin at low temperatures
    • Grellmann K.H., Livingston R., and Pratt D. A Flash-photolytic investigation of rhodopsin at low temperatures. Nature 193 (1962) 1258-1260
    • (1962) Nature , vol.193 , pp. 1258-1260
    • Grellmann, K.H.1    Livingston, R.2    Pratt, D.3
  • 148
    • 0001929587 scopus 로고
    • Picosecond and nanosecond components in bacteriorhodopsin light-induced electric response signal
    • Groma G.I., Ráksi F., Szabó G., and Váró G. Picosecond and nanosecond components in bacteriorhodopsin light-induced electric response signal. Biophys. J. 54 (1988) 77-80
    • (1988) Biophys. J. , vol.54 , pp. 77-80
    • Groma, G.I.1    Ráksi, F.2    Szabó, G.3    Váró, G.4
  • 149
    • 0023645105 scopus 로고
    • Structure-function studies on bacteriorhodopsin: V. effects of amino acid substitutions in the putative helix F
    • Hackett N.R., Stern L.J., Chao B.H., Kronis K.A., and Khorana H.G. Structure-function studies on bacteriorhodopsin: V. effects of amino acid substitutions in the putative helix F. J. Biol. Chem. 269 (1987) 9277-9284
    • (1987) J. Biol. Chem. , vol.269 , pp. 9277-9284
    • Hackett, N.R.1    Stern, L.J.2    Chao, B.H.3    Kronis, K.A.4    Khorana, H.G.5
  • 150
    • 0027199085 scopus 로고
    • Localization of the retinal protonated Schiff base counterion in rhodopsin
    • Han M., DeDecker B.S., and Smith S.O. Localization of the retinal protonated Schiff base counterion in rhodopsin. Biophys. J. 65 (1993) 899-906
    • (1993) Biophys. J. , vol.65 , pp. 899-906
    • Han, M.1    DeDecker, B.S.2    Smith, S.O.3
  • 151
    • 0011247629 scopus 로고
    • On the protein (tyrosine) -chromophore (protonated Schiff base) coupling in bacteriorhodopsin
    • Hanamoto J.H., Dupuis P., and El-Sayed M.A. On the protein (tyrosine) -chromophore (protonated Schiff base) coupling in bacteriorhodopsin. Proc. Natl. Acad. Sci. USA 81 (1984) 7083-7087
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 7083-7087
    • Hanamoto, J.H.1    Dupuis, P.2    El-Sayed, M.A.3
  • 152
    • 0025228428 scopus 로고
    • Ultraviolet resonance raman spectra of bacteriorhodopsin in the light-adapted and dark-adapted states
    • Harada I., Yamagishi T., Uchida K., and Takeuchi H. Ultraviolet resonance raman spectra of bacteriorhodopsin in the light-adapted and dark-adapted states. J. Am. Chem. Soc. 112 (1990) 2443-2445
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 2443-2445
    • Harada, I.1    Yamagishi, T.2    Uchida, K.3    Takeuchi, H.4
  • 153
    • 0021094366 scopus 로고
    • Solid-state nitrogen-15 nuclear magnetic resonance study of the schiff base in bacteriorhodopsin
    • Harbison G.S., Herzfeld J., and Griffin R.G. Solid-state nitrogen-15 nuclear magnetic resonance study of the schiff base in bacteriorhodopsin. Biochemistry 22 (1983) 1-5
    • (1983) Biochemistry , vol.22 , pp. 1-5
    • Harbison, G.S.1    Herzfeld, J.2    Griffin, R.G.3
  • 155
    • 33845280969 scopus 로고
    • Solid-state NMR detection of proton exchange between the bacteriorhodopsin Schiff base and bulk water
    • Harbison G.S., Roberts J.E., Herzfeld J., and Griffin R.G. Solid-state NMR detection of proton exchange between the bacteriorhodopsin Schiff base and bulk water. J. Am. Chem. Soc. 110 (1988) 7221-7223
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 7221-7223
    • Harbison, G.S.1    Roberts, J.E.2    Herzfeld, J.3    Griffin, R.G.4
  • 159
    • 0025300323 scopus 로고
    • Transmembrane location of retinal in bacteriorhodopsin by neutron diffraction
    • Hauss T., Grzesiek S., Otto H., Westerhausen J., and Heyn M.P. Transmembrane location of retinal in bacteriorhodopsin by neutron diffraction. Biochemistry 29 (1990) 4904-4913
    • (1990) Biochemistry , vol.29 , pp. 4904-4913
    • Hauss, T.1    Grzesiek, S.2    Otto, H.3    Westerhausen, J.4    Heyn, M.P.5
  • 160
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson R., Baldwin J.M., and Ceska T.A. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 213 (1990) 899-929
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3
  • 161
    • 0025716272 scopus 로고
    • The structure of bacteriorhodopsin and its relevance to the visual opsins and other seven-helix G-protein coupled receptors
    • Henderson R., Schertler F.R.S., and Schertier G.R.X. The structure of bacteriorhodopsin and its relevance to the visual opsins and other seven-helix G-protein coupled receptors. Phil. Trans. R. Soc. Lond., B. 326 (1990) 379-389
    • (1990) Phil. Trans. R. Soc. Lond., B. , vol.326 , pp. 379-389
    • Henderson, R.1    Schertler, F.R.S.2    Schertier, G.R.X.3
  • 163
    • 0017571694 scopus 로고
    • Transient and linear dichroism studies on bacteriorho-dopsin: Determination of the orientation of the 568 nm all-trans retinal chromophore
    • Heyn M.P., Cherry R.J., and Müller U. Transient and linear dichroism studies on bacteriorho-dopsin: Determination of the orientation of the 568 nm all-trans retinal chromophore. J. Mol. Biol. 117 (1977) 607-620
    • (1977) J. Mol. Biol. , vol.117 , pp. 607-620
    • Heyn, M.P.1    Cherry, R.J.2    Müller, U.3
  • 164
    • 0000217440 scopus 로고
    • Role of water in bacteriorhodopsin's chromophore: reso-nance raman study
    • Hildebrandt P., and Stockburger M. Role of water in bacteriorhodopsin's chromophore: reso-nance raman study. Biochemistry 23 (1984) 5539-5548
    • (1984) Biochemistry , vol.23 , pp. 5539-5548
    • Hildebrandt, P.1    Stockburger, M.2
  • 165
    • 85025567406 scopus 로고
    • Distributed kinetics of the charge movements in bacteriorhodopsin: evidence for conformational substrates
    • Holz M., Lindau M., and Heyn M.P. Distributed kinetics of the charge movements in bacteriorhodopsin: evidence for conformational substrates. Biophys. J. 53 (1988) 623-633
    • (1988) Biophys. J. , vol.53 , pp. 623-633
    • Holz, M.1    Lindau, M.2    Heyn, M.P.3
  • 166
    • 0004064402 scopus 로고
    • Theoretical aspects of photoisomerization in visual pigments and bacteriorhodopsin
    • Alfano R.R. (Ed), Academic Press Inc, New York
    • Honig B. Theoretical aspects of photoisomerization in visual pigments and bacteriorhodopsin. In: Alfano R.R. (Ed). Biological events probed by ultrafast laser spectroscopy (1982), Academic Press Inc, New York 281-296
    • (1982) Biological events probed by ultrafast laser spectroscopy , pp. 281-296
    • Honig, B.1
  • 167
    • 0009643868 scopus 로고
    • Photoisomerization, energy storage, and charge separation: A model for light energy transduction in visual pigments and bacteriorhodopsin
    • Honig B., Ebrey T., Callender R.H., Dinur U., and Ottolenghi M. Photoisomerization, energy storage, and charge separation: A model for light energy transduction in visual pigments and bacteriorhodopsin. Proc. Natl. Acad. Sci. USA 76 (1979) 2503-2507
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 2503-2507
    • Honig, B.1    Ebrey, T.2    Callender, R.H.3    Dinur, U.4    Ottolenghi, M.5
  • 168
    • 0017171319 scopus 로고
    • Visual-pigment spectra: Implications of the protonation of the retinal schiff base
    • Honig B., Greenberg A.D., Dinur U., and Ebrey T.G. Visual-pigment spectra: Implications of the protonation of the retinal schiff base. Biochemistry 15 (1976) 4593-4599
    • (1976) Biochemistry , vol.15 , pp. 4593-4599
    • Honig, B.1    Greenberg, A.D.2    Dinur, U.3    Ebrey, T.G.4
  • 170
    • 0001909239 scopus 로고
    • Theoretical studies of the visual chromophores
    • Honig B., Warshel A., and Karplus M. Theoretical studies of the visual chromophores. Acct. Chem. Res. 8 (1975) 92-100
    • (1975) Acct. Chem. Res. , vol.8 , pp. 92-100
    • Honig, B.1    Warshel, A.2    Karplus, M.3
  • 171
    • 0019319521 scopus 로고
    • Circular dichrosim of cattle rhodopsin and bathorhodopsin at liquid nitrogen temperatures
    • Horiuchi S., Tokunaga F., and Yoshizawa T. Circular dichrosim of cattle rhodopsin and bathorhodopsin at liquid nitrogen temperatures. Biochim. Biophys. Acta 591 (1980) 445-457
    • (1980) Biochim. Biophys. Acta , vol.591 , pp. 445-457
    • Horiuchi, S.1    Tokunaga, F.2    Yoshizawa, T.3
  • 172
    • 77957088358 scopus 로고
    • Synergy in the spectral tuning of retinal pigments-com-plete accounting of the opsin shift in bacteriorhodopsin
    • Hu J., Griffin R.G., and Herzfeld J. Synergy in the spectral tuning of retinal pigments-com-plete accounting of the opsin shift in bacteriorhodopsin. Biophys. J. 66 (1994) A45
    • (1994) Biophys. J. , vol.66
    • Hu, J.1    Griffin, R.G.2    Herzfeld, J.3
  • 173
    • 0028058192 scopus 로고
    • Unbleachable rhodopsin with an 11-cis-locked eight-membered ring retinal: The visual transduc-tion process
    • Hu S., Franklin P.J., Wang J., Chen A.-H., Silva B.E.R., Derguini F., and Nakanishi K. Unbleachable rhodopsin with an 11-cis-locked eight-membered ring retinal: The visual transduc-tion process. Biochemistry 33 (1994) 408-416
    • (1994) Biochemistry , vol.33 , pp. 408-416
    • Hu, S.1    Franklin, P.J.2    Wang, J.3    Chen, A.-H.4    Silva, B.E.R.5    Derguini, F.6    Nakanishi, K.7
  • 174
    • 0024536233 scopus 로고
    • Determination of the absolute orientation of the retinylidene chromophore in purple membrane by a second-harmonic interference technique
    • Huang J.Y., and Lewis A. Determination of the absolute orientation of the retinylidene chromophore in purple membrane by a second-harmonic interference technique. Biophys. J. 55 (1989) 835-842
    • (1989) Biophys. J. , vol.55 , pp. 835-842
    • Huang, J.Y.1    Lewis, A.2
  • 175
    • 0020491413 scopus 로고
    • Orientation of retinal in bacteriorhodopsin as studied by cross-linking using a photosensitive analog of retinal
    • Huang K.-S., Radhakrishnan R., Bayley H., and Khorana H.G. Orientation of retinal in bacteriorhodopsin as studied by cross-linking using a photosensitive analog of retinal. J. Biol. Chem. 257 (1982) 13616-13623
    • (1982) J. Biol. Chem. , vol.257 , pp. 13616-13623
    • Huang, K.-S.1    Radhakrishnan, R.2    Bayley, H.3    Khorana, H.G.4
  • 176
    • 0014027427 scopus 로고
    • The stereoisomerization of 11-cis-retinal
    • Hubbard R. The stereoisomerization of 11-cis-retinal. J. Biol. Chem. 241 (1966) 1814-1818
    • (1966) J. Biol. Chem. , vol.241 , pp. 1814-1818
    • Hubbard, R.1
  • 178
    • 0343117190 scopus 로고
    • Evidence for a common batho intermediate of rhodopsin and isorhodopsin
    • Hug S.J., Lewis J.W., and Kliger D.S. Evidence for a common batho intermediate of rhodopsin and isorhodopsin. J. Am. Chem. Soc. 110 (1988) 1998-1999
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 1998-1999
    • Hug, S.J.1    Lewis, J.W.2    Kliger, D.S.3
  • 179
    • 0017869801 scopus 로고
    • Energy transfer in the purple membrane of Halobacterium halobium
    • Hurley J.B., and Ebrey T.G. Energy transfer in the purple membrane of Halobacterium halobium. Biophys. J. 22 (1978) 49-66
    • (1978) Biophys. J. , vol.22 , pp. 49-66
    • Hurley, J.B.1    Ebrey, T.G.2
  • 180
    • 0017770143 scopus 로고
    • Temperature and wavelength effects on the photochemistry of rhodopsin, isorhodopsin, bacteriorhodopsin, and their photoproducts
    • Hurley J.B., Ebrey T.G., Honig B., and Ottolenghi M. Temperature and wavelength effects on the photochemistry of rhodopsin, isorhodopsin, bacteriorhodopsin, and their photoproducts. Nature 270 (1977) 540-542
    • (1977) Nature , vol.270 , pp. 540-542
    • Hurley, J.B.1    Ebrey, T.G.2    Honig, B.3    Ottolenghi, M.4
  • 181
    • 0001663752 scopus 로고
    • Conformational analysis of the rhodopsin chromophore using bycyclic retinal analogues
    • Ito M., Katsuta Y., Imamoto Y., Shichida Y., and Yoshizawa T. Conformational analysis of the rhodopsin chromophore using bycyclic retinal analogues. Photochem. Photobiol. 56 (1992) 915-919
    • (1992) Photochem. Photobiol. , vol.56 , pp. 915-919
    • Ito, M.1    Katsuta, Y.2    Imamoto, Y.3    Shichida, Y.4    Yoshizawa, T.5
  • 182
    • 84989709945 scopus 로고
    • A novel bacteriorhodopsin analogue with conformationally 6-s-cis fixed retinals
    • Iwasa T., Ito M., and Tokunaga F. A novel bacteriorhodopsin analogue with conformationally 6-s-cis fixed retinals. Photochem. Photobiol. 56 (1992) 921-927
    • (1992) Photochem. Photobiol. , vol.56 , pp. 921-927
    • Iwasa, T.1    Ito, M.2    Tokunaga, F.3
  • 183
    • 0025325371 scopus 로고
    • Effect of genetic modification of tyrosine-185 on the proton pump and the blue-to-purple transition in bacteriorho-dopsin
    • Jang D.-J., El-Sayed M.A., Stern L.J., Mogi T., and Khorana H.G. Effect of genetic modification of tyrosine-185 on the proton pump and the blue-to-purple transition in bacteriorho-dopsin. Proc. Natl. Acad. Sci. USA 87 (1990) 4103-4107
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4103-4107
    • Jang, D.-J.1    El-Sayed, M.A.2    Stern, L.J.3    Mogi, T.4    Khorana, H.G.5
  • 184
    • 0026007784 scopus 로고
    • Binding of a single divalent cation directly correlates with the blue-to-purple transition in bacteriorhodopsin
    • Jonas R., and Ebrey T.G. Binding of a single divalent cation directly correlates with the blue-to-purple transition in bacteriorhodopsin. Proc. Natl. Acad. Sci. USA 88 (1991) 149
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 149
    • Jonas, R.1    Ebrey, T.G.2
  • 185
    • 0000749514 scopus 로고
    • Molecular mechanism for the initial process of visual excitation. II. Theoretical analysis of optical activity in rhodopsin and bathorhodopsin
    • Kakitani T., Kakitani H., and Yomosa S. Molecular mechanism for the initial process of visual excitation. II. Theoretical analysis of optical activity in rhodopsin and bathorhodopsin. J. Phys. Soc. Japan 42 (1977) 996-1004
    • (1977) J. Phys. Soc. Japan , vol.42 , pp. 996-1004
    • Kakitani, T.1    Kakitani, H.2    Yomosa, S.3
  • 186
  • 187
    • 33845552576 scopus 로고
    • Correlation of vibrational frequencies with absorption maxima in polyenes, rhodopsin, bacteriorhodopsin and retinal ana-logues
    • Kakitani H., Kakitani T., Rodman H., Honig B., and Callender R.J. Correlation of vibrational frequencies with absorption maxima in polyenes, rhodopsin, bacteriorhodopsin and retinal ana-logues. J. Phys. Chem. 87 (1983) 3620-3628
    • (1983) J. Phys. Chem. , vol.87 , pp. 3620-3628
    • Kakitani, H.1    Kakitani, T.2    Rodman, H.3    Honig, B.4    Callender, R.J.5
  • 188
    • 84985473388 scopus 로고
    • Branching pathways in the photocycle of bacteriorhodopsin
    • Kalisky O., and Ottolenghi M. Branching pathways in the photocycle of bacteriorhodopsin. Photochem. Photobiol. 35 (1982) 109-115
    • (1982) Photochem. Photobiol. , vol.35 , pp. 109-115
    • Kalisky, O.1    Ottolenghi, M.2
  • 189
    • 0024046232 scopus 로고
    • Dependency of apparent relative quantum yield of isorhodopsin to rhodopsin on the photon density of picosecond laser pulse
    • Kandori H., Matuoka H., Nagai H., Shichida Y., and Yoshizawa T. Dependency of apparent relative quantum yield of isorhodopsin to rhodopsin on the photon density of picosecond laser pulse. Photochem. Photobiol. 48 (1988) 93-97
    • (1988) Photochem. Photobiol. , vol.48 , pp. 93-97
    • Kandori, H.1    Matuoka, H.2    Nagai, H.3    Shichida, Y.4    Yoshizawa, T.5
  • 190
    • 0024617321 scopus 로고
    • Dependency of photon density on primary process of cattle rhodopsin
    • Kandori H., Matuoka S., Shichida Y., and Yoshizawa T. Dependency of photon density on primary process of cattle rhodopsin. Photochem. Photobiol. 49 (1989) 181-184
    • (1989) Photochem. Photobiol. , vol.49 , pp. 181-184
    • Kandori, H.1    Matuoka, S.2    Shichida, Y.3    Yoshizawa, T.4
  • 191
    • 0024375762 scopus 로고
    • Mechanism of isomerization of rhodopsin studied by use of 11-cis-locked rhodopsin analogues excited with a picosecond laser pulse
    • Kandori H., Matuoka S., Shichida Y., Yoshizawa T., Ito M., Tsukida K., Balogh-Nair V., and Nakanishi K. Mechanism of isomerization of rhodopsin studied by use of 11-cis-locked rhodopsin analogues excited with a picosecond laser pulse. Biochemistry 28 (1989) 6460-6467
    • (1989) Biochemistry , vol.28 , pp. 6460-6467
    • Kandori, H.1    Matuoka, S.2    Shichida, Y.3    Yoshizawa, T.4    Ito, M.5    Tsukida, K.6    Balogh-Nair, V.7    Nakanishi, K.8
  • 192
    • 0024729899 scopus 로고
    • Absolute absorption spectra of batho-and photorhodopsins at room temperature
    • Kandori H., Shichida Y., and Yoshizawa T. Absolute absorption spectra of batho-and photorhodopsins at room temperature. Biophys. J. 56 (1989) 453-457
    • (1989) Biophys. J. , vol.56 , pp. 453-457
    • Kandori, H.1    Shichida, Y.2    Yoshizawa, T.3
  • 193
    • 0001362637 scopus 로고
    • Comparative studies of primary photochemical events of two retinal proteins, bacteriorhodopsin and halorhodopsin, by use of subpicosecond time-resolved spectr
    • Kandori H., Yoshihara K., Tomioka H., Sasabe H., and Shichida Y. Comparative studies of primary photochemical events of two retinal proteins, bacteriorhodopsin and halorhodopsin, by use of subpicosecond time-resolved spectr. Chem. Phys. Lett. 211 (1993) 385-391
    • (1993) Chem. Phys. Lett. , vol.211 , pp. 385-391
    • Kandori, H.1    Yoshihara, K.2    Tomioka, H.3    Sasabe, H.4    Shichida, Y.5
  • 194
    • 0019306307 scopus 로고
    • Circadian clock in Limulus brain increases response and decreases noise of retinal photoreceptors
    • Kaplan E., and Barlow Jr. R.B. Circadian clock in Limulus brain increases response and decreases noise of retinal photoreceptors. Nature 286 (1980) 393-395
    • (1980) Nature , vol.286 , pp. 393-395
    • Kaplan, E.1    Barlow Jr., R.B.2
  • 195
    • 0018890191 scopus 로고
    • Photochemical studies of 7-cis-rhodopsin at low temperatures. Nature and properties of the bathointermediate
    • Kawamura S., Miyatani S., Matsumoto H., Yoshizawa T., and Liu R.S.H. Photochemical studies of 7-cis-rhodopsin at low temperatures. Nature and properties of the bathointermediate. Biochemistry 19 (1980) 1549-1553
    • (1980) Biochemistry , vol.19 , pp. 1549-1553
    • Kawamura, S.1    Miyatani, S.2    Matsumoto, H.3    Yoshizawa, T.4    Liu, R.S.H.5
  • 196
    • 0018717528 scopus 로고
    • Orientational changes of the transition dipole moment of retinal chromophore of the disk membrane due to the conversion of rhodopsin to bathorhodopsin and to
    • Kawamura S., Tokunaga F., Yoshizawa T., Sarai A., and Kakitani T. Orientational changes of the transition dipole moment of retinal chromophore of the disk membrane due to the conversion of rhodopsin to bathorhodopsin and to. Vision Res. 19 (1979) 879-884
    • (1979) Vision Res. , vol.19 , pp. 879-884
    • Kawamura, S.1    Tokunaga, F.2    Yoshizawa, T.3    Sarai, A.4    Kakitani, T.5
  • 197
    • 0000910683 scopus 로고
    • Primary charge motions and light-energy transduction in bacteriorhodopsin
    • Keszthelyi L. Primary charge motions and light-energy transduction in bacteriorhodopsin. Biophys. Chem. 29 (1988) 127-136
    • (1988) Biophys. Chem. , vol.29 , pp. 127-136
    • Keszthelyi, L.1
  • 198
    • 8944227986 scopus 로고
    • Electric signals associated with the photocycle of bacteriorhodopsin
    • Keszthelyi L., and Ormos P. Electric signals associated with the photocycle of bacteriorhodopsin. FEBS Lett. 109 (1980) 189-193
    • (1980) FEBS Lett. , vol.109 , pp. 189-193
    • Keszthelyi, L.1    Ormos, P.2
  • 199
    • 0021715502 scopus 로고
    • Evidence for a common batho-intermediate in the bleaching of rhodopsin and isorhodopsin
    • Kliger D.S., Horowitz J.W., Lewis J.W., and Einterz C.M. Evidence for a common batho-intermediate in the bleaching of rhodopsin and isorhodopsin. Vision Res. 24 (1984) 1465-1470
    • (1984) Vision Res. , vol.24 , pp. 1465-1470
    • Kliger, D.S.1    Horowitz, J.W.2    Lewis, J.W.3    Einterz, C.M.4
  • 200
    • 0017809144 scopus 로고
    • Immobilization of bacteriorhodopsin and orientation of its transition moment in purple membrane
    • Korenstein R., and Hess B. Immobilization of bacteriorhodopsin and orientation of its transition moment in purple membrane. FEBS Lett. 89 (1978) 15-20
    • (1978) FEBS Lett. , vol.89 , pp. 15-20
    • Korenstein, R.1    Hess, B.2
  • 202
    • 84989712926 scopus 로고
    • Isomerization of the retinylidene chromo-phore of bacteriorhodopsin in light adaptation: Intrinsic isomerization of the chromophore and its control by the apo
    • Koyama Y., Natasu H., Mukai Y., and Tokunaga F. Isomerization of the retinylidene chromo-phore of bacteriorhodopsin in light adaptation: Intrinsic isomerization of the chromophore and its control by the apo. Photochem. Photobiol. 57 (1993) 732-738
    • (1993) Photochem. Photobiol. , vol.57 , pp. 732-738
    • Koyama, Y.1    Natasu, H.2    Mukai, Y.3    Tokunaga, F.4
  • 203
    • 0000388260 scopus 로고
    • The colors of the visual pigments
    • Kropf A., and Hubbard R. The colors of the visual pigments. Ann. NY Acad. Sci. 74 (1958) 266-280
    • (1958) Ann. NY Acad. Sci. , vol.74 , pp. 266-280
    • Kropf, A.1    Hubbard, R.2
  • 204
    • 0020070177 scopus 로고
    • Trans-cis isomerization of the retinal chromophore of bacteriorho-dopsin during the photocycle
    • Kuschmitz D., and Hess B. Trans-cis isomerization of the retinal chromophore of bacteriorho-dopsin during the photocycle. FEBS Lett. 138 (1982) 137-140
    • (1982) FEBS Lett. , vol.138 , pp. 137-140
    • Kuschmitz, D.1    Hess, B.2
  • 205
    • 0018257782 scopus 로고
    • Light energy conversion in Halobacterium halobium
    • Lanyi J.K. Light energy conversion in Halobacterium halobium. Microbiol. Rev. 42 (1978) 682-712
    • (1978) Microbiol. Rev. , vol.42 , pp. 682-712
    • Lanyi, J.K.1
  • 206
    • 0024378716 scopus 로고
    • The transverse location of the retinal chromophore in the purple membrane by diffusion-enhanced energy transfer
    • Leder R.O., Helgerson S.L., and Thomas D.D. The transverse location of the retinal chromophore in the purple membrane by diffusion-enhanced energy transfer. J. Mol. Biol. 209 (1989) 683-701
    • (1989) J. Mol. Biol. , vol.209 , pp. 683-701
    • Leder, R.O.1    Helgerson, S.L.2    Thomas, D.D.3
  • 208
    • 0026772264 scopus 로고
    • Photointermediates of Visual Pigments
    • Lewis J.W., and Kliger D.S. Photointermediates of Visual Pigments. J. Bioenerg. Biomembr. 24 (1992) 201-210
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 201-210
    • Lewis, J.W.1    Kliger, D.S.2
  • 209
    • 0023161174 scopus 로고
    • The molecular mechanism of visual excitation and its relation to the structure and composition of the rod outer segment
    • Liebman P.A., Parker K.R., and Dratz E.A. The molecular mechanism of visual excitation and its relation to the structure and composition of the rod outer segment. Ann. Rev. Physiol. 49 (1987) 965-991
    • (1987) Ann. Rev. Physiol. , vol.49 , pp. 965-991
    • Liebman, P.A.1    Parker, K.R.2    Dratz, E.A.3
  • 210
    • 0024741970 scopus 로고
    • Orientation of the protonated retinal Schiff base group in bacteriorhodopsin from absorption linear dichroism
    • Lin S.W., and Mathies R.A. Orientation of the protonated retinal Schiff base group in bacteriorhodopsin from absorption linear dichroism. Biophys. J. 56 (1989) 653-660
    • (1989) Biophys. J. , vol.56 , pp. 653-660
    • Lin, S.W.1    Mathies, R.A.2
  • 211
    • 0026750971 scopus 로고
    • Resonance Raman microprobe spectroscopy of rhodopsin mutants: effects of substitutions in the third transmembrane helix
    • Lin S.W., Sakmar T.P., Franke R.R., Khorana H.G., and Mathies R.A. Resonance Raman microprobe spectroscopy of rhodopsin mutants: effects of substitutions in the third transmembrane helix. Biochemistry 31 (1992) 5105-5111
    • (1992) Biochemistry , vol.31 , pp. 5105-5111
    • Lin, S.W.1    Sakmar, T.P.2    Franke, R.R.3    Khorana, H.G.4    Mathies, R.A.5
  • 212
    • 0001383264 scopus 로고
    • The primary process of vision and the structure of bathorhodopsin, a mechanism of photoisomerization of polyenes
    • Liu R.S.H., and Asato A.E. The primary process of vision and the structure of bathorhodopsin, a mechanism of photoisomerization of polyenes. Proc. Natl. Acad. Sci. USA 82 (1985) 259-263
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 259-263
    • Liu, R.S.H.1    Asato, A.E.2
  • 213
    • 0000254592 scopus 로고
    • The shape of a three-dimensional binding site of rhodopsin based on molecular modeling analyses of isomeric and other visual pigment analogues. Bioorganic stu of visual pigments. 11
    • Liu R.S., and Mirzadegan T. The shape of a three-dimensional binding site of rhodopsin based on molecular modeling analyses of isomeric and other visual pigment analogues. Bioorganic stu of visual pigments. 11. J. Am. Chem. Soc. 110 (1988) 8617-8623
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 8617-8623
    • Liu, R.S.1    Mirzadegan, T.2
  • 214
    • 0026232955 scopus 로고
    • Butyl conformational reorganization as a possible explanation for the longitudinal flexability of the binding site of bacteriorhodopsin. The azulene and C-22
    • Liu R.S.H., Liu C.W.X.-Y.L., and Asato A.E. Butyl conformational reorganization as a possible explanation for the longitudinal flexability of the binding site of bacteriorhodopsin. The azulene and C-22. Photochem. Photobiol. 54 (1991) 625-631
    • (1991) Photochem. Photobiol. , vol.54 , pp. 625-631
    • Liu, R.S.H.1    Liu, C.W.X.-Y.L.2    Asato, A.E.3
  • 215
    • 0027306780 scopus 로고
    • The Schiff base bond configuration in bacteriorhodopsin and in model compounds
    • Livnah N., and Sheves M. The Schiff base bond configuration in bacteriorhodopsin and in model compounds. Biochemistry 32 (1993) 7223-7228
    • (1993) Biochemistry , vol.32 , pp. 7223-7228
    • Livnah, N.1    Sheves, M.2
  • 217
    • 0001451202 scopus 로고
    • Resonance Raman studies on the intermediate K-590 in the photocycle of bacteriorhodopsin
    • Lohrmann R., Grieger L., and Stockburger M. Resonance Raman studies on the intermediate K-590 in the photocycle of bacteriorhodopsin. J. Phys. Chem. 95 (1991) 1993-2001
    • (1991) J. Phys. Chem. , vol.95 , pp. 1993-2001
    • Lohrmann, R.1    Grieger, L.2    Stockburger, M.3
  • 218
    • 0011480156 scopus 로고
    • Deprotonation of the Schiffbase of rhodopsin is obligate in the activation of the G protein
    • Longstaff C., Calhoon R.D., and Rando R.R. Deprotonation of the Schiffbase of rhodopsin is obligate in the activation of the G protein. Proc. Natl. Acad. Sci. USA 83 (1986) 4209-4213
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 4209-4213
    • Longstaff, C.1    Calhoon, R.D.2    Rando, R.R.3
  • 219
    • 0023662554 scopus 로고
    • Deprotonation of the Schiff base of bacteriorhodopsin is obligate in light-induced proton pumping
    • Longstaff C., and Rando R.R. Deprotonation of the Schiff base of bacteriorhodopsin is obligate in light-induced proton pumping. Biochemistry 26 (1987) 6107-6113
    • (1987) Biochemistry , vol.26 , pp. 6107-6113
    • Longstaff, C.1    Rando, R.R.2
  • 220
    • 0342546940 scopus 로고
    • Active-site lysine methylation and the mechanisms of action of rhodopsin and bacteriorhodopsin
    • Ebrey T.G., Frauenfelder H., Honig B., and Nakanishi K. (Eds), University of Illinois Press
    • Longstaff C., Seckler B., Calhoon R.D., and Rando R.R. Active-site lysine methylation and the mechanisms of action of rhodopsin and bacteriorhodopsin. In: Ebrey T.G., Frauenfelder H., Honig B., and Nakanishi K. (Eds). Biophysical studies of retinal proteins (1987), University of Illinois Press 64-70
    • (1987) Biophysical studies of retinal proteins , pp. 64-70
    • Longstaff, C.1    Seckler, B.2    Calhoon, R.D.3    Rando, R.R.4
  • 221
    • 0001194341 scopus 로고
    • Factors influencing the C=N stretching frequency in neutral and protonated Schiff's bases
    • Lopez-Garriga J.J., Babcock G.T., and Harrison J.F. Factors influencing the C=N stretching frequency in neutral and protonated Schiff's bases. J. Am. Chem. Soc. 108 (1986) 7241-7251
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 7241-7251
    • Lopez-Garriga, J.J.1    Babcock, G.T.2    Harrison, J.F.3
  • 222
    • 33845376078 scopus 로고
    • Increase in the C=N stretching frequency upon complexation of trans-retinylidene-n-butylamine with general Lewis acids
    • Lopez-Garriga J.J., Babcock G.T., and Harrison J.F. Increase in the C=N stretching frequency upon complexation of trans-retinylidene-n-butylamine with general Lewis acids. J. Am. Chem. Soc. 108 (1986) 7131-7133
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 7131-7133
    • Lopez-Garriga, J.J.1    Babcock, G.T.2    Harrison, J.F.3
  • 223
    • 0024592918 scopus 로고
    • Why are blue visual pigments blue? A resonance raman microprobe study
    • Loppnow G.R., Barry B.A., and Mathies R.A. Why are blue visual pigments blue? A resonance raman microprobe study. Proc. Natl. Acad. Sci. USA 86 (1989) 1515-1518
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 1515-1518
    • Loppnow, G.R.1    Barry, B.A.2    Mathies, R.A.3
  • 226
    • 0023762295 scopus 로고
    • Structure and function of rhodopsins from solid state NMR and resonance Raman spectroscopy of isotopic retinal derivatives
    • Lugtenburg J., Mathies R.A., Griffin R.G., and Herzfeld J. Structure and function of rhodopsins from solid state NMR and resonance Raman spectroscopy of isotopic retinal derivatives. Trends Biochem. Sci. 13 (1988) 388-393
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 388-393
    • Lugtenburg, J.1    Mathies, R.A.2    Griffin, R.G.3    Herzfeld, J.4
  • 228
    • 84989669798 scopus 로고
    • Fourier transform infrared spectral studies on the Schiff base mode of all-trans bacteriorhodopsin and its photointermediates, K and L. Photochem
    • Maeda A., Saski J., Pfefferlé J.-M., Shichida Y., and Yoshizawa T. Fourier transform infrared spectral studies on the Schiff base mode of all-trans bacteriorhodopsin and its photointermediates, K and L. Photochem. Photobiol. 54 (1991) 911-921
    • (1991) Photobiol. , vol.54 , pp. 911-921
    • Maeda, A.1    Saski, J.2    Pfefferlé, J.-M.3    Shichida, Y.4    Yoshizawa, T.5
  • 229
    • 0026602025 scopus 로고
    • Water structural changes in the bacteriorho-dopsin photocycle: analysis by fourier transform infrared spectroscopy
    • Maeda A., Sasaki J., Shichida Y., and Yoshizawa T. Water structural changes in the bacteriorho-dopsin photocycle: analysis by fourier transform infrared spectroscopy. Biochemistry 31 (1992) 462-467
    • (1992) Biochemistry , vol.31 , pp. 462-467
    • Maeda, A.1    Sasaki, J.2    Shichida, Y.3    Yoshizawa, T.4
  • 230
    • 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 spec
    • Maeda A., Sasaki J., Tamazake T., Needleman R., and Lanyi J.K. Interaction of aspartate-85 with a water molecule and the protonated Schiff base in the L intermediate of bacteriorhodopsin: a fourier-transform infrared spec. Biochemistry 33 (1994) 1713-1717
    • (1994) Biochemistry , vol.33 , pp. 1713-1717
    • Maeda, A.1    Sasaki, J.2    Tamazake, T.3    Needleman, R.4    Lanyi, J.K.5
  • 231
    • 0018874368 scopus 로고
    • Bathoproducts of rhodopsin, isorhodopsin I, and isorho-dopsin II
    • Mao B., Ebrey T.G., and Crouch R. Bathoproducts of rhodopsin, isorhodopsin I, and isorho-dopsin II. Biophys. J. 29 (1980) 247-256
    • (1980) Biophys. J. , vol.29 , pp. 247-256
    • Mao, B.1    Ebrey, T.G.2    Crouch, R.3
  • 232
    • 0019499786 scopus 로고
    • Flash photolysis and low temperature photochemistry of bovine rhodopsin with a fixed 11-ene
    • Mao B., Tsuda M., Ebrey T., Akita H., Balogh-Nair V., and Nakanishi K. Flash photolysis and low temperature photochemistry of bovine rhodopsin with a fixed 11-ene. Biophys. J. 35 (1981) 543-546
    • (1981) Biophys. J. , vol.35 , pp. 543-546
    • Mao, B.1    Tsuda, M.2    Ebrey, T.3    Akita, H.4    Balogh-Nair, V.5    Nakanishi, K.6
  • 233
    • 0023359362 scopus 로고
    • Abrupt onset of large scale nonproton ion release in purple membranes caused by increasing pH or ionic strength
    • Marinetti T. Abrupt onset of large scale nonproton ion release in purple membranes caused by increasing pH or ionic strength. Biophys. J. 51 (1987) 875-881
    • (1987) Biophys. J. , vol.51 , pp. 875-881
    • Marinetti, T.1
  • 234
    • 0023374661 scopus 로고
    • Large scale nonproton ion release and bacteriorhodopsin's state of aggregation in lipid vesicles
    • Marinetti T. Large scale nonproton ion release and bacteriorhodopsin's state of aggregation in lipid vesicles. Biophys. J. 52 (1987) 115-121
    • (1987) Biophys. J. , vol.52 , pp. 115-121
    • Marinetti, T.1
  • 235
    • 0020691028 scopus 로고
    • Absolute quantum yields and proof of proton and non-proton transient release and uptake in photoexcited bacteriorhodopsin
    • Marinetti T., and Mauzerall D. Absolute quantum yields and proof of proton and non-proton transient release and uptake in photoexcited bacteriorhodopsin. Proc. Natl. Acad. Sci.USA 80 (1983) 178-180
    • (1983) Proc. Natl. Acad. Sci.USA , vol.80 , pp. 178-180
    • Marinetti, T.1    Mauzerall, D.2
  • 236
    • 0026059269 scopus 로고
    • The retinylidene schiff base counterion in bacteriorhodopsin
    • Marti T., Rösselet S.J.H.O., Heyn M.P., and Khorana H.G. The retinylidene schiff base counterion in bacteriorhodopsin. J. Biol. Chem. 266 (1991) 18674-18683
    • (1991) J. Biol. Chem. , vol.266 , pp. 18674-18683
    • Marti, T.1    Rösselet, S.J.H.O.2    Heyn, M.P.3    Khorana, H.G.4
  • 237
    • 0343622125 scopus 로고
    • Resonance Raman spectroscopy of rhodopsin and bacteriorhodopsin isotopic analogs
    • Packer L. (Ed), Academic Press, New York
    • Mathies R. Resonance Raman spectroscopy of rhodopsin and bacteriorhodopsin isotopic analogs. In: Packer L. (Ed). Methods enzymol (1982), Academic Press, New York 633-643
    • (1982) Methods enzymol , pp. 633-643
    • Mathies, R.1
  • 238
    • 0024279842 scopus 로고
    • Direct observation of the femtosecond excited-state cis-trans isomerization in bacteriorhodopsin
    • Mathies R.A., Brito Cruz C.H., Pollard W.T., and Shank C.V. Direct observation of the femtosecond excited-state cis-trans isomerization in bacteriorhodopsin. Science 240 (1988) 777-779
    • (1988) Science , vol.240 , pp. 777-779
    • Mathies, R.A.1    Brito Cruz, C.H.2    Pollard, W.T.3    Shank, C.V.4
  • 239
    • 0025829307 scopus 로고
    • From femtoseconds to biology: Mechanism of bacteriorhdopsin's light-driven proton pump
    • Mathies R.A., Lin S.W., Ames J.B., and Pollard W.T. From femtoseconds to biology: Mechanism of bacteriorhdopsin's light-driven proton pump. Annu. Rev. Biophys. Biophys. Chem. 20 (1991) 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
  • 240
    • 84968033002 scopus 로고
    • From femtoseconds to biology: mechanism of the light-driven proton pump in bacteriorhodopsin
    • Mathies R.A., Lugtenburg J., and Shank C.V. From femtoseconds to biology: mechanism of the light-driven proton pump in bacteriorhodopsin. SPIE (Biomolecular Spectroscopy) 1057 (1989) 138-145
    • (1989) SPIE (Biomolecular Spectroscopy) , vol.1057 , pp. 138-145
    • Mathies, R.A.1    Lugtenburg, J.2    Shank, C.V.3
  • 241
    • 0025947168 scopus 로고
    • Mechanism of proton pumping in bacteriorhodopsin by solid-state NMR: the protonation state of tyrosine in the light-adapted and M states
    • McDermott A.E., Thompson L.K., Winkel C., Farrar M.R., Pelletier S., Lugtenburg J., Herzfeld J., and Griffin R.G. Mechanism of proton pumping in bacteriorhodopsin by solid-state NMR: the protonation state of tyrosine in the light-adapted and M states. Biochemistry 30 (1991) 8366-8371
    • (1991) Biochemistry , vol.30 , pp. 8366-8371
    • McDermott, A.E.1    Thompson, L.K.2    Winkel, C.3    Farrar, M.R.4    Pelletier, S.5    Lugtenburg, J.6    Herzfeld, J.7    Griffin, R.G.8
  • 242
    • 0024286277 scopus 로고
    • Evidence for light-induced lysine conformational changes during the primary event of the bacteriorhodopsin photocycle
    • McMaster E., and Lewis A. Evidence for light-induced lysine conformational changes during the primary event of the bacteriorhodopsin photocycle. Biochem. Biophys. Res. Comm. 156 (1988) 86-91
    • (1988) Biochem. Biophys. Res. Comm. , vol.156 , pp. 86-91
    • McMaster, E.1    Lewis, A.2
  • 243
    • 0026512964 scopus 로고
    • High-resolution solid state 13C NMR of bacteriorhodop-sin: characterization of [4-13C]asp resonances
    • Metz G., Siebert F., and Engelhard M. High-resolution solid state 13C NMR of bacteriorhodop-sin: characterization of [4-13C]asp resonances. Biochemistry 31 (1992) 455-462
    • (1992) Biochemistry , vol.31 , pp. 455-462
    • Metz, G.1    Siebert, F.2    Engelhard, M.3
  • 244
    • 0022625758 scopus 로고
    • A new approach to understanding the initial step in visual transduction
    • Milder S.J., and Kliger D.S. A new approach to understanding the initial step in visual transduction. Biophys. J. 49 (1986) 567-570
    • (1986) Biophys. J. , vol.49 , pp. 567-570
    • Milder, S.J.1    Kliger, D.S.2
  • 246
    • 0024978461 scopus 로고
    • Structure-function studies on bacteriorhodopsin
    • Mogi T., Marti T., and Khorana H.G. Structure-function studies on bacteriorhodopsin. J. Biol. Chem. 264 (1989) 14197-14201
    • (1989) J. Biol. Chem. , vol.264 , pp. 14197-14201
    • Mogi, T.1    Marti, T.2    Khorana, H.G.3
  • 247
    • 0024978498 scopus 로고
    • Structure-function studies on bacteriorho-dopsin
    • Mogi T., Stern L.J., Chao B., and Khorana H.G. Structure-function studies on bacteriorho-dopsin. J. Biol. Chem. 264 (1989) 14192-14196
    • (1989) J. Biol. Chem. , vol.264 , pp. 14192-14196
    • Mogi, T.1    Stern, L.J.2    Chao, B.3    Khorana, H.G.4
  • 248
  • 250
    • 0018743755 scopus 로고
    • Photochemistry of rhodopsin and isorhodopsin investigated on a picosecond time scale
    • Monger T., Alfano R.R., and Callender R.H. Photochemistry of rhodopsin and isorhodopsin investigated on a picosecond time scale. Biophys. J. 27 (1979) 105-115
    • (1979) Biophys. J. , vol.27 , pp. 105-115
    • Monger, T.1    Alfano, R.R.2    Callender, R.H.3
  • 251
    • 84989685009 scopus 로고
    • Effect of photoselection upon saturation and the dichroic ratio in flash experiments upon effectively immobilized systems
    • Nagle J.F., Bhattacharjee S.M., Parodi L.A., and Lozier R.H. Effect of photoselection upon saturation and the dichroic ratio in flash experiments upon effectively immobilized systems. Photochem. Photobiol. 38 (1983) 331-339
    • (1983) Photochem. Photobiol. , vol.38 , pp. 331-339
    • Nagle, J.F.1    Bhattacharjee, S.M.2    Parodi, L.A.3    Lozier, R.H.4
  • 252
    • 33847086787 scopus 로고
    • An external point-charge model for bacteriorhodopsin to account for its purple color
    • Nakanishi K., Balogh-Nair V., Arnaboldi M., Tsujimoto K., and Honig R. An external point-charge model for bacteriorhodopsin to account for its purple color. J. Am. Chem. Soc. 102 (1980) 7945-7947
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 7945-7947
    • Nakanishi, K.1    Balogh-Nair, V.2    Arnaboldi, M.3    Tsujimoto, K.4    Honig, R.5
  • 253
    • 0025050478 scopus 로고
    • Orientation of retinal of bovine rhodopsin determined by cross-linking using a photoactivatable analog of 11-cis-retinal
    • Nakayama T.A., and Khorana H.G. Orientation of retinal of bovine rhodopsin determined by cross-linking using a photoactivatable analog of 11-cis-retinal. J. Biol. Chem. 265 (1990) 15762-15769
    • (1990) J. Biol. Chem. , vol.265 , pp. 15762-15769
    • Nakayama, T.A.1    Khorana, H.G.2
  • 254
    • 0025162902 scopus 로고
    • Determinants of visual pigment absorbance: identification of the retinylidene schiff 's base counterion-in bovine rhodopsin
    • Nathans J. Determinants of visual pigment absorbance: identification of the retinylidene schiff 's base counterion-in bovine rhodopsin. Biochemistry 29 (1990) 9746-9752
    • (1990) Biochemistry , vol.29 , pp. 9746-9752
    • Nathans, J.1
  • 255
    • 0025012994 scopus 로고
    • Determinants of visual pigment absorbance: Role of charged amino acids in the putative transmembrane segments
    • Nathans J. Determinants of visual pigment absorbance: Role of charged amino acids in the putative transmembrane segments. Biochemistry 29 (1990) 937-942
    • (1990) Biochemistry , vol.29 , pp. 937-942
    • Nathans, J.1
  • 256
    • 0026643593 scopus 로고
    • Rhodopsin: structure, function, and genetics
    • Nathans J. Rhodopsin: structure, function, and genetics. Biochemistry 31 (1992) 4923-4929
    • (1992) Biochemistry , vol.31 , pp. 4923-4929
    • Nathans, J.1
  • 257
    • 84989685275 scopus 로고
    • Structure of bacteriorhodopsin and in situ isomerization of retinal: A molecular dynamics study
    • Nonella M., Windemuth A., and Schulten K. Structure of bacteriorhodopsin and in situ isomerization of retinal: A molecular dynamics study. Photochem. Photobiol. 54 (1991) 937-948
    • (1991) Photochem. Photobiol. , vol.54 , pp. 937-948
    • Nonella, M.1    Windemuth, A.2    Schulten, K.3
  • 258
    • 20544447251 scopus 로고
    • Femtosecond spectroscopy of the first events of the photochemical cycle in bacteriorhodopsin
    • Nuss M.C., Zinth W., Kaiser W., Rolling E., and Oesterhelt D. Femtosecond spectroscopy of the first events of the photochemical cycle in bacteriorhodopsin. Chem. Phys. Lett. 117 (1985) 1-7
    • (1985) Chem. Phys. Lett. , vol.117 , pp. 1-7
    • Nuss, M.C.1    Zinth, W.2    Kaiser, W.3    Rolling, E.4    Oesterhelt, D.5
  • 259
    • 0015886107 scopus 로고
    • Reversible photolysis of the purple complex in the purple membrane of Halobacterium halobium
    • Oesterhelt D., and Hess B. Reversible photolysis of the purple complex in the purple membrane of Halobacterium halobium. Eur. J. Biochem. 37 (1973) 316-326
    • (1973) Eur. J. Biochem. , vol.37 , pp. 316-326
    • Oesterhelt, D.1    Hess, B.2
  • 260
    • 0024501960 scopus 로고
    • Two pumps, one principle: light-driven ion transport in Halobacteria
    • Oesterhelt D., and Tittor J. Two pumps, one principle: light-driven ion transport in Halobacteria. Trends Biochem. Sci. 14 (1989) 57-61
    • (1989) Trends Biochem. Sci. , vol.14 , pp. 57-61
    • Oesterhelt, D.1    Tittor, J.2
  • 261
    • 0000948646 scopus 로고
    • The photocycle of the chloride pump halorhodopsin. II. Quantum yields and a kinetic model
    • Oesterhelt D., Hegemann P., and Tittor J. The photocycle of the chloride pump halorhodopsin. II. Quantum yields and a kinetic model. EMBO J. 4 (1985) 2351-2356
    • (1985) EMBO J. , vol.4 , pp. 2351-2356
    • Oesterhelt, D.1    Hegemann, P.2    Tittor, J.3
  • 262
    • 84989761133 scopus 로고
    • Primary processes in photolysis of octopus rhodopsin
    • Ohtani H., Kobayashi T., Tsuda M., and Ebrey T.G. Primary processes in photolysis of octopus rhodopsin. Biophysical J. 53 (1988) 17-24
    • (1988) Biophysical J. , vol.53 , pp. 17-24
    • Ohtani, H.1    Kobayashi, T.2    Tsuda, M.3    Ebrey, T.G.4
  • 263
    • 0013127874 scopus 로고
    • Coupling of stereochemistry and proton donor-acceptor properties of a schiff base. A model of a light-driven proton pump
    • Orlandi G., and Schulten K. Coupling of stereochemistry and proton donor-acceptor properties of a schiff base. A model of a light-driven proton pump. Chem. Phys. Lett. 64 (1979) 370-374
    • (1979) Chem. Phys. Lett. , vol.64 , pp. 370-374
    • Orlandi, G.1    Schulten, K.2
  • 264
    • 0016289846 scopus 로고
    • Resonance Raman spectroscopy of rhodopsin in retinal disk membranes
    • Oseroff A.R., and Callender R.H. Resonance Raman spectroscopy of rhodopsin in retinal disk membranes. Biochemistry 13 (1974) 2443-4348
    • (1974) Biochemistry , vol.13 , pp. 2443-4348
    • Oseroff, A.R.1    Callender, R.H.2
  • 265
    • 77957028258 scopus 로고
    • Chromophore of bacteriorhodopsin is closer to the cytoplasmic surface of purple membrane
    • Otomo J., Tomioka A., Kinoshita K., Miyata H., Takenaka Y.T.K., and Ikegami A. Chromophore of bacteriorhodopsin is closer to the cytoplasmic surface of purple membrane. Biophys. J. 54 (1988) 57-64
    • (1988) Biophys. J. , vol.54 , pp. 57-64
    • Otomo, J.1    Tomioka, A.2    Kinoshita, K.3    Miyata, H.4    Takenaka, Y.T.K.5    Ikegami, A.6
  • 266
    • 0024835953 scopus 로고
    • Synthetic retinals as probes for the binding site and photoreactions in rhodopsins
    • Ottolenghi M., and Sheves M. Synthetic retinals as probes for the binding site and photoreactions in rhodopsins. J. Membrane Biol. 112 (1989) 193-212
    • (1989) J. Membrane Biol. , vol.112 , pp. 193-212
    • Ottolenghi, M.1    Sheves, M.2
  • 267
    • 0023215761 scopus 로고
    • Assignment of fingerprint vibrations in the resonance raman spectra of rhodopsin, isorhodopsin, and bathorhodopsin: Implications for chromophore structure and
    • Palings I., Pardoen J.A., van den Berg E., Winkle C., Lugtenburg J., and Mathies R.A. Assignment of fingerprint vibrations in the resonance raman spectra of rhodopsin, isorhodopsin, and bathorhodopsin: Implications for chromophore structure and. Biochemistry 26 (1987) 2544-2556
    • (1987) Biochemistry , vol.26 , pp. 2544-2556
    • Palings, I.1    Pardoen, J.A.2    van den Berg, E.3    Winkle, C.4    Lugtenburg, J.5    Mathies, R.A.6
  • 268
    • 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
    • Palings I., van den Berg E.M.M., Lugtenburg J., and Mathies R.A. Complete assignment of the hydrogen out-of-plane wagging vibrations of bathorhodopsin: chromophore structure and energy storage in the primary photoproduct of. Biochemistry 28 (1989) 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
  • 270
    • 0023658619 scopus 로고
    • Resonance Raman spectroscopy of an ultraviolet-sensitive insect rhodopsin
    • Pande C., Deng H., Rath P., Callender H., and Schwemer J. Resonance Raman spectroscopy of an ultraviolet-sensitive insect rhodopsin. Biochemistry 26 (1987) 7426-7430
    • (1987) Biochemistry , vol.26 , pp. 7426-7430
    • Pande, C.1    Deng, H.2    Rath, P.3    Callender, H.4    Schwemer, J.5
  • 271
    • 0025298852 scopus 로고
    • Water molecules and exchangeable hydrogen ions at the active centre of bacteriorhodopsin localized by neutron diffraction. Elements of the proton pathway?
    • Papadopoulos G., Dencher N.A., Zaccai G., and Büldt G. Water molecules and exchangeable hydrogen ions at the active centre of bacteriorhodopsin localized by neutron diffraction. Elements of the proton pathway?. J. Mol Biol. 214 (1990) 15-19
    • (1990) J. Mol Biol. , vol.214 , pp. 15-19
    • Papadopoulos, G.1    Dencher, N.A.2    Zaccai, G.3    Büldt, G.4
  • 272
    • 0024373166 scopus 로고
    • Probes which reflect the distance between the retinal chromophore and membrane surface in bacteriorhodopsin (bR) . Direction of retinal 9-methyl in bR
    • Park M.H., Yamamoto T., and Nakanishi K. Probes which reflect the distance between the retinal chromophore and membrane surface in bacteriorhodopsin (bR) . Direction of retinal 9-methyl in bR. J. Am. Chem. Soc. 111 (1989) 4997-4998
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 4997-4998
    • Park, M.H.1    Yamamoto, T.2    Nakanishi, K.3
  • 277
    • 36549097689 scopus 로고
    • Direct observation of the excited-state cis-trans photoisomerization of bacteriorhodopsin: Multilevel line shape theory for femtosecond dynamic hole burni and its application
    • Pollard W.T., Cruz C.H.B., Shank C.V., and Mathies R.A. Direct observation of the excited-state cis-trans photoisomerization of bacteriorhodopsin: Multilevel line shape theory for femtosecond dynamic hole burni and its application. J. Chem. Phys. 90 (1989) 199-208
    • (1989) J. Chem. Phys. , vol.90 , pp. 199-208
    • Pollard, W.T.1    Cruz, C.H.B.2    Shank, C.V.3    Mathies, R.A.4
  • 278
    • 0015969754 scopus 로고
    • Reconstitution of purple membrane vesicles catalyzing light-driven proton uptake and adenosine triphosphate formation
    • Racker E., and Stoeckenius W. Reconstitution of purple membrane vesicles catalyzing light-driven proton uptake and adenosine triphosphate formation. J. Biol. Chem. 249 (1974) 662-663
    • (1974) J. Biol. Chem. , vol.249 , pp. 662-663
    • Racker, E.1    Stoeckenius, W.2
  • 279
    • 0019532559 scopus 로고
    • The involvement of water at the retinal binding site in rhodopsin and early light-induced intramolecular proton transfer
    • Rafferty C.N., and Shichi H. The involvement of water at the retinal binding site in rhodopsin and early light-induced intramolecular proton transfer. Photochem. Photobiol. 33 (1981) 229-234
    • (1981) Photochem. Photobiol. , vol.33 , pp. 229-234
    • Rafferty, C.N.1    Shichi, H.2
  • 280
    • 0020713773 scopus 로고
    • Events in proton pumping by bacteriorhodopsin
    • Rayfield G.W. Events in proton pumping by bacteriorhodopsin. Biophys. J. 41 (1983) 109-117
    • (1983) Biophys. J. , vol.41 , pp. 109-117
    • Rayfield, G.W.1
  • 281
    • 0012128949 scopus 로고
    • A rhodopsin pigment containing a spin-labeled retinal
    • Renk G.E., Or Y.S., and Crouch R.K. A rhodopsin pigment containing a spin-labeled retinal. J. Am. Chem. Soc. 109 (1987) 6163-6168
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 6163-6168
    • Renk, G.E.1    Or, Y.S.2    Crouch, R.K.3
  • 285
  • 287
    • 0000017956 scopus 로고
    • Quantum yields of the photochromic equilibrium between bacteriorhodopsin and its bathointermediate K. Fempto-and nanosecond optoacoustic spectroscopy
    • Rohr M., Gärtner W., Schweitzer G., Holzwarth A.R., and Braslavsky S.E. Quantum yields of the photochromic equilibrium between bacteriorhodopsin and its bathointermediate K. Fempto-and nanosecond optoacoustic spectroscopy. J. Phys. Chem. 96 (1992) 6055-6061
    • (1992) J. Phys. Chem. , vol.96 , pp. 6055-6061
    • Rohr, M.1    Gärtner, W.2    Schweitzer, G.3    Holzwarth, A.R.4    Braslavsky, S.E.5
  • 288
    • 0000823495 scopus 로고
    • Cis-trans isomerization in the photochemistry of vision
    • Rosenfeld T., Honig B., and Ottolenghi M. Cis-trans isomerization in the photochemistry of vision. Pure Appl. Chem. 49 (1977) 341-351
    • (1977) Pure Appl. Chem. , vol.49 , pp. 341-351
    • Rosenfeld, T.1    Honig, B.2    Ottolenghi, M.3
  • 289
    • 0000823495 scopus 로고
    • On the role of the protein in the photoisomerization of the visual pigment chromophore
    • Rosenfeld T., Honig B., Ottolenghi M., Hurley J.B., and Ebrey T.G. On the role of the protein in the photoisomerization of the visual pigment chromophore. Pure Appl. Chem 49 (1977) 341-351
    • (1977) Pure Appl. Chem , vol.49 , pp. 341-351
    • Rosenfeld, T.1    Honig, B.2    Ottolenghi, M.3    Hurley, J.B.4    Ebrey, T.G.5
  • 290
    • 0026643216 scopus 로고
    • FTIR difference spectroscopy of bacteriorhodopsin: Toward a molecular model
    • Rothschild K.J. FTIR difference spectroscopy of bacteriorhodopsin: Toward a molecular model. J. Bioenerg. Biomembr. 24 (1992) 147-167
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 147-167
    • Rothschild, K.J.1
  • 292
    • 0025075443 scopus 로고
    • Vibrational spectroscopy of bacteriorhodopsin mutants. Evidence for the interaction of aspartic acid 212 with tyrosine 185 and possible role in the proton pum
    • Rothschild K.J., Braiman M.S., He Y.-W., Marti T., and Khorana H.G. Vibrational spectroscopy of bacteriorhodopsin mutants. Evidence for the interaction of aspartic acid 212 with tyrosine 185 and possible role in the proton pum. J. Biol. Chem. 265 28 (1990) 16985-16991
    • (1990) J. Biol. Chem. , vol.265 , Issue.28 , pp. 16985-16991
    • Rothschild, K.J.1    Braiman, M.S.2    He, Y.-W.3    Marti, T.4    Khorana, H.G.5
  • 293
    • 0024960566 scopus 로고
    • Conserved amino acids in F-helix of bacteriorhodopsin form part of a retinal binding pocket
    • Rothschild K.J., Braiman M.S., Mogi T., Stern L.J., and Khorana H.G. Conserved amino acids in F-helix of bacteriorhodopsin form part of a retinal binding pocket. FEBS Lett. 250 (1989) 44S-452
    • (1989) FEBS Lett. , vol.250
    • Rothschild, K.J.1    Braiman, M.S.2    Mogi, T.3    Stern, L.J.4    Khorana, H.G.5
  • 294
    • 0024976553 scopus 로고
    • Vibrational spectroscopy of bacteriorhodopsin mutants: chromophore isomerization perturbs tryptophan-86
    • Rothschild K.J., Gray D., Mogi T., Marti T., Braiman M.S., Stern L.J., and Khorana H.G. Vibrational spectroscopy of bacteriorhodopsin mutants: chromophore isomerization perturbs tryptophan-86. Biochemistry 28 (1989) 7052-7059
    • (1989) Biochemistry , vol.28 , pp. 7052-7059
    • Rothschild, K.J.1    Gray, D.2    Mogi, T.3    Marti, T.4    Braiman, M.S.5    Stern, L.J.6    Khorana, H.G.7
  • 296
    • 0021887888 scopus 로고
    • Fourier transform infrared spectroscopic evidence for the existence of two conformations of the bacteriorhodopsin primary photoproduct at low temperature
    • Rothschild K.J., and Gillespie J. Fourier transform infrared spectroscopic evidence for the existence of two conformations of the bacteriorhodopsin primary photoproduct at low temperature. Biochim. Biophys. Acta 808 (1985) 140-148
    • (1985) Biochim. Biophys. Acta , vol.808 , pp. 140-148
    • Rothschild, K.J.1    Gillespie, J.2
  • 297
    • 0021755238 scopus 로고
    • Fourier transform infrared evidence for Schiff base alteration in the first step of the bacteriorhodopsin photocycle
    • Rothschild K.J., Roepe P., Lugtenburg J., and Pardoen J.A. Fourier transform infrared evidence for Schiff base alteration in the first step of the bacteriorhodopsin photocycle. Biochemistry 23 (1984) 6103-6109
    • (1984) Biochemistry , vol.23 , pp. 6103-6109
    • Rothschild, K.J.1    Roepe, P.2    Lugtenburg, J.3    Pardoen, J.A.4
  • 298
    • 0343177634 scopus 로고
    • Glutamic acid 113 serves as the retinylidene Schiff base counterion in bovine rhodopsin
    • Sakmar T.P., Franke R.R., and Khorana H.G. Glutamic acid 113 serves as the retinylidene Schiff base counterion in bovine rhodopsin. Proc. Natl. Acad. Sci. USA 86 (1989) 8309-8313
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 8309-8313
    • Sakmar, T.P.1    Franke, R.R.2    Khorana, H.G.3
  • 300
    • 0016714583 scopus 로고
    • Conversion of a photon to an electrical signal by sudden polarization in the n-retinylidene visual chromophore
    • Salem S., and Bruckmann P. Conversion of a photon to an electrical signal by sudden polarization in the n-retinylidene visual chromophore. Nature 258 (1975) 526-528
    • (1975) Nature , vol.258 , pp. 526-528
    • Salem, S.1    Bruckmann, P.2
  • 301
    • 0028218956 scopus 로고
    • Environmental effects on the protonation states of active site residues in bacteriorhodopsin
    • Sampogna R.V., and Honig B. Environmental effects on the protonation states of active site residues in bacteriorhodopsin. Biophys. J. 66 (1994) 1341-1352
    • (1994) Biophys. J. , vol.66 , pp. 1341-1352
    • Sampogna, R.V.1    Honig, B.2
  • 302
    • 0342546940 scopus 로고
    • Fourier-transform infrared study of the protonation of retinylidene Schiff base
    • Ebrey T.G., Frauenfelder H., Honig B., and Nakanishi K. (Eds), University of Illinois Press
    • Sandorfy C., Lussier L.S., Thanh H.L., and Vocelle D. Fourier-transform infrared study of the protonation of retinylidene Schiff base. In: Ebrey T.G., Frauenfelder H., Honig B., and Nakanishi K. (Eds). Biophysical studies of retinal proteins (1987), University of Illinois Press 247-251
    • (1987) Biophysical studies of retinal proteins , pp. 247-251
    • Sandorfy, C.1    Lussier, L.S.2    Thanh, H.L.3    Vocelle, D.4
  • 304
    • 0019328814 scopus 로고
    • Existence of two forms of bathorhodopsins
    • Sasaki N., Tokunaga F., and Yoshizawa T. Existence of two forms of bathorhodopsins. FEBS Lett. 114 (1980) 1-3
    • (1980) FEBS Lett. , vol.114 , pp. 1-3
    • Sasaki, N.1    Tokunaga, F.2    Yoshizawa, T.3
  • 305
    • 0019077760 scopus 로고
    • The formation of two forms of bathorhodopsin and their optical properties
    • Sasaki N., Tokunaga F., and Yoshizawa T. The formation of two forms of bathorhodopsin and their optical properties. Photochem. Photobio. 32 (1980) 433-441
    • (1980) Photochem. Photobio. , vol.32 , pp. 433-441
    • Sasaki, N.1    Tokunaga, F.2    Yoshizawa, T.3
  • 306
    • 0025834125 scopus 로고
    • Chromophore motion during the bacteriorhodopsin photocycle: polarized absorption spectroscopy of bacteriorhodopsin and its M-state in bacteriorhodopsin crysta
    • Schertier G.F.X., Lozier R., Michel H., and Oesterhelt D. Chromophore motion during the bacteriorhodopsin photocycle: polarized absorption spectroscopy of bacteriorhodopsin and its M-state in bacteriorhodopsin crysta. EMBO J. 10 (1991) 2253-2261
    • (1991) EMBO J. , vol.10 , pp. 2253-2261
    • Schertier, G.F.X.1    Lozier, R.2    Michel, H.3    Oesterhelt, D.4
  • 307
    • 0027190359 scopus 로고
    • Projection structure of rhodopsin
    • Schertler G.F.X., Villa C., and Henderson R. Projection structure of rhodopsin. Nature 362 (1993) 770-772
    • (1993) Nature , vol.362 , pp. 770-772
    • Schertler, G.F.X.1    Villa, C.2    Henderson, R.3
  • 308
    • 0023219466 scopus 로고
    • Energy storage in the primary photochemical events of rhodopsin and isorhodopsin
    • Schick G.A., Cooper T.M., Holloway R.A., Murray L.P., and Birge R.R. Energy storage in the primary photochemical events of rhodopsin and isorhodopsin. Biochemistry 26 (1987) 2556-2562
    • (1987) Biochemistry , vol.26 , pp. 2556-2562
    • Schick, G.A.1    Cooper, T.M.2    Holloway, R.A.3    Murray, L.P.4    Birge, R.R.5
  • 309
    • 0002650691 scopus 로고
    • Photochemical quantum yield of bacteriorhodopsin from resonance Raman scattering as a probe for photolysis
    • Schneider G., Diller R., and Stockburger M. Photochemical quantum yield of bacteriorhodopsin from resonance Raman scattering as a probe for photolysis. Chem. Phys. 131 (1989) 17-29
    • (1989) Chem. Phys. , vol.131 , pp. 17-29
    • Schneider, G.1    Diller, R.2    Stockburger, M.3
  • 310
    • 0026091595 scopus 로고
    • The first step in vision: femptosecond isomerization of rhodopsin
    • Schoenlein R.W., Peteanu L.A., Mathies R.A., and Shank C.V. The first step in vision: femptosecond isomerization of rhodopsin. Sci. 254 (1991) 412-415
    • (1991) Sci. , vol.254 , pp. 412-415
    • Schoenlein, R.W.1    Peteanu, L.A.2    Mathies, R.A.3    Shank, C.V.4
  • 311
    • 33751384971 scopus 로고
    • Femtosecond dynamics of cis-trans isomerization in a visual pigment analog: isorhodopsin
    • Schoenlein R.W., Peteanu L.A., Wang Q., Mathies R.A., and Shank C.V. Femtosecond dynamics of cis-trans isomerization in a visual pigment analog: isorhodopsin. J. Phys. Chem. 97 (1993) 12087-12092
    • (1993) J. Phys. Chem. , vol.97 , pp. 12087-12092
    • Schoenlein, R.W.1    Peteanu, L.A.2    Wang, Q.3    Mathies, R.A.4    Shank, C.V.5
  • 312
    • 0017879924 scopus 로고
    • A mechanism for the light-driven proton pump of Halobacterium halobium
    • Schulten K., and Tavan P. A mechanism for the light-driven proton pump of Halobacterium halobium. Nature 272 (1978) 85-86
    • (1978) Nature , vol.272 , pp. 85-86
    • Schulten, K.1    Tavan, P.2
  • 313
    • 0021700253 scopus 로고
    • An isomerization model for the pump cycle of bacteriorhodopsin
    • Bolis L., Helmrich E.J.M., and Passow H. (Eds), Alan R. Liss, New York
    • Schulten K., Schulten Z., and Tavan P. An isomerization model for the pump cycle of bacteriorhodopsin. In: Bolis L., Helmrich E.J.M., and Passow H. (Eds). Information and energy transduction in biological membranes (1984), Alan R. Liss, New York 113-131
    • (1984) Information and energy transduction in biological membranes , pp. 113-131
    • Schulten, K.1    Schulten, Z.2    Tavan, P.3
  • 316
    • 0021991970 scopus 로고
    • Primary photochemical event in bacteriorhodopsin: study with artificial pigments
    • Sheves M., Friedman N., and Albeck A. Primary photochemical event in bacteriorhodopsin: study with artificial pigments. Biochemistry 24 (1985) 1260-1265
    • (1985) Biochemistry , vol.24 , pp. 1260-1265
    • Sheves, M.1    Friedman, N.2    Albeck, A.3
  • 317
    • 0022869494 scopus 로고
    • Primary intermediates of photobleaching of rhodopsin
    • Shichida Y. Primary intermediates of photobleaching of rhodopsin. Photobiochem. Photobio-phys. 13 (1986) 287-307
    • (1986) Photobiochem. Photobio-phys. , vol.13 , pp. 287-307
    • Shichida, Y.1
  • 318
    • 77957089659 scopus 로고
    • Changes in the chromophore-opsin interaction in the photobleaching processes of visual pigments
    • Rigaud J.-L. (Ed), John Libbey and Company Ltd, Dourdan, France
    • Shichida Y. Changes in the chromophore-opsin interaction in the photobleaching processes of visual pigments. In: Rigaud J.-L. (Ed). Colloques INSERM (Structures and functions of retinal proteins) (1992), John Libbey and Company Ltd, Dourdan, France 291-294
    • (1992) Colloques INSERM (Structures and functions of retinal proteins) , pp. 291-294
    • Shichida, Y.1
  • 319
    • 0000248079 scopus 로고
    • Absorption spectra of intermediates of bacteriorhodopsin measured by laser photolysis at room temperature
    • Shichida Y., Matuoka S., Hidaka Y., and Yoshizawa T. Absorption spectra of intermediates of bacteriorhodopsin measured by laser photolysis at room temperature. Biochim. Biophys. Acta. 723 (1983) 240-246
    • (1983) Biochim. Biophys. Acta. , vol.723 , pp. 240-246
    • Shichida, Y.1    Matuoka, S.2    Hidaka, Y.3    Yoshizawa, T.4
  • 320
    • 0021169930 scopus 로고
    • Formation of photorhodopsin, a precursor of bathorhodopsin, detected by a picosecond laser photolysis at room temperature
    • Shichida Y., Matuoka S., and Yoshizawa T. Formation of photorhodopsin, a precursor of bathorhodopsin, detected by a picosecond laser photolysis at room temperature. Photobiochem. Photobiophys. 7 (1984) 221-228
    • (1984) Photobiochem. Photobiophys. , vol.7 , pp. 221-228
    • Shichida, Y.1    Matuoka, S.2    Yoshizawa, T.3
  • 321
    • 0018076990 scopus 로고
    • Circular dichroism of squid rhodopsin and its intermediates
    • Shichida Y., Tokunaga F., and Yoshizawa T. Circular dichroism of squid rhodopsin and its intermediates. Biochim. Biophys. Acta 504 (1978) 413-430
    • (1978) Biochim. Biophys. Acta , vol.504 , pp. 413-430
    • Shichida, Y.1    Tokunaga, F.2    Yoshizawa, T.3
  • 322
    • 0021103472 scopus 로고
    • Investigation of the primary photochemistry of bacteriorhodopsin by low temperature Fourier-transform infrared spectroscopy
    • Siebert F., and Mantele W. Investigation of the primary photochemistry of bacteriorhodopsin by low temperature Fourier-transform infrared spectroscopy. Eur. J. Biochem. 130 (1983) 565-573
    • (1983) Eur. J. Biochem. , vol.130 , pp. 565-573
    • Siebert, F.1    Mantele, W.2
  • 323
    • 0025261654 scopus 로고
    • Evidence that the photoelectric response of bacteriorhodopsin occurs in less than 5 picoseconds
    • Simmeth R., and Rayfield G.W. Evidence that the photoelectric response of bacteriorhodopsin occurs in less than 5 picoseconds. Biophys. J. 57 (1990) 1099-1101
    • (1990) Biophys. J. , vol.57 , pp. 1099-1101
    • Simmeth, R.1    Rayfield, G.W.2
  • 324
    • 0000300950 scopus 로고
    • Acta Crystallogr., Sect. B: Struct. Crystallogr
    • Simmons C.J., Liu R.S.M., Denny M., and Seff K. Acta Crystallogr., Sect. B: Struct. Crystallogr. Cryst. Chem. B37 (1981) 2197-2205
    • (1981) Cryst. Chem. , vol.B37 , pp. 2197-2205
    • Simmons, C.J.1    Liu, R.S.M.2    Denny, M.3    Seff, K.4
  • 325
    • 77957062599 scopus 로고
    • Rhodopsins: from ion pumps to specialized photoreceptors
    • Rigaud J.-L. (Ed), John Libbey and Company Ltd., Dourdan, France
    • Skulachev V.P. Rhodopsins: from ion pumps to specialized photoreceptors. In: Rigaud J.-L. (Ed). Colloques INSERM (Structures and functions of retinal proteins) (1992), John Libbey and Company Ltd., Dourdan, France 229-232
    • (1992) Colloques INSERM (Structures and functions of retinal proteins) , pp. 229-232
    • Skulachev, V.P.1
  • 327
    • 0025919682 scopus 로고
    • 13C magic-angle spinning NMR studies of bathorhodopsin, the primary photoproduct of rhodopsin
    • Smith S.O., Courtin J., de Groot H., and Lugtenburg J. 13C magic-angle spinning NMR studies of bathorhodopsin, the primary photoproduct of rhodopsin. Biochemistry 30 (1991) 7409-7415
    • (1991) Biochemistry , vol.30 , pp. 7409-7415
    • Smith, S.O.1    Courtin, J.2    de Groot, H.3    Lugtenburg, J.4
  • 328
    • 0024982103 scopus 로고
    • Structure and protein environment of the retinal chromophore in light-and dark-adapted bacteriorhodopsin studied by solid-state NMR
    • Smith S.O., de Groot H.J.M., Gebhard R., Courtin J.M.L., Lugtenburg J., Herzfeld J., and Griffin R.G. Structure and protein environment of the retinal chromophore in light-and dark-adapted bacteriorhodopsin studied by solid-state NMR. Biochemistry 28 (1989) 8897-8904
    • (1989) Biochemistry , vol.28 , pp. 8897-8904
    • Smith, S.O.1    de Groot, H.J.M.2    Gebhard, R.3    Courtin, J.M.L.4    Lugtenburg, J.5    Herzfeld, J.6    Griffin, R.G.7
  • 329
    • 0342546940 scopus 로고
    • Solid-state NMR studies of bacteriorhodopsin: Recent results on the structure of the Schiff base in the dark-adapted and M412 states
    • Ebrey T.G., Frauenfelder H., Honig B., and Nakanishi K. (Eds), University of Illinois Press
    • Smith S.O., Harbison G.S., Raleigh D.P., Griffin R.G., Winkel C., Pardoen J.A., Lugtenburg J., and Herzfeld J. Solid-state NMR studies of bacteriorhodopsin: Recent results on the structure of the Schiff base in the dark-adapted and M412 states. In: Ebrey T.G., Frauenfelder H., Honig B., and Nakanishi K. (Eds). Biophysical studies of retinal proteins (1987), University of Illinois Press 219-225
    • (1987) Biophysical studies of retinal proteins , pp. 219-225
    • Smith, S.O.1    Harbison, G.S.2    Raleigh, D.P.3    Griffin, R.G.4    Winkel, C.5    Pardoen, J.A.6    Lugtenburg, J.7    Herzfeld, J.8
  • 331
    • 0021848415 scopus 로고
    • Determination of retinal chromophore structure in bacteriorhodopsin with resonance raman spectroscopy
    • Smith S.O., Lugtenburg J., and Mathies R.A. Determination of retinal chromophore structure in bacteriorhodopsin with resonance raman spectroscopy. J. Membrane Biol. 85 (1985) 95-109
    • (1985) J. Membrane Biol. , vol.85 , pp. 95-109
    • Smith, S.O.1    Lugtenburg, J.2    Mathies, R.A.3
  • 336
    • 0000736928 scopus 로고
    • Vibrational analysis of the 13-cis-retinal chromophore in dark-adapted bacteriorhodopsin
    • Smith S.O., Pardoen J.A., Lugtenburg J., and Mathies R.A. Vibrational analysis of the 13-cis-retinal chromophore in dark-adapted bacteriorhodopsin. J. Phys. Chem. 91 (1987) 804-819
    • (1987) J. Phys. Chem. , vol.91 , pp. 804-819
    • Smith, S.O.1    Pardoen, J.A.2    Lugtenburg, J.3    Mathies, R.A.4
  • 337
    • 0027303125 scopus 로고
    • Protein catalysis of the retinal subpicosecond photoisomerization in the primary process of bacteriorhodopsin photosynthesis
    • Song L., El-Sayed M.A., and Lanyi J.K. Protein catalysis of the retinal subpicosecond photoisomerization in the primary process of bacteriorhodopsin photosynthesis. Science 261 (1993) 891-894
    • (1993) Science , vol.261 , pp. 891-894
    • Song, L.1    El-Sayed, M.A.2    Lanyi, J.K.3
  • 338
    • 0343196043 scopus 로고
    • Conformations of 11-cis retinal
    • Langer H. (Ed), Springer-Verlag Inc, New York
    • Sperling W. Conformations of 11-cis retinal. In: Langer H. (Ed). Biochemistry and physiology of visual pigments (1972), Springer-Verlag Inc, New York 19-28
    • (1972) Biochemistry and physiology of visual pigments , pp. 19-28
    • Sperling, W.1
  • 340
    • 0027335795 scopus 로고
    • a of the protonated Schiff base of bovine rhodopsin. A study with artificial pigments
    • a of the protonated Schiff base of bovine rhodopsin. A study with artificial pigments. Biophys. J. 64 (1993) 1499-1502
    • (1993) Biophys. J. , vol.64 , pp. 1499-1502
    • Steinberg, G.1    Ottolenghi, M.2    Sheves, M.3
  • 341
    • 0024978473 scopus 로고
    • Structure-function studies on bacteriorhodopsin
    • Stern L.J., and Khorana H.G. Structure-function studies on bacteriorhodopsin. J. Biol. Chem. 264 (1989) 14202-14208
    • (1989) J. Biol. Chem. , vol.264 , pp. 14202-14208
    • Stern, L.J.1    Khorana, H.G.2
  • 342
    • 0022558381 scopus 로고
    • Cycle GMP cascade in vision
    • Stryer L. Cycle GMP cascade in vision. Ann. Rev. Neurosci. 9 (1986) 87-119
    • (1986) Ann. Rev. Neurosci. , vol.9 , pp. 87-119
    • Stryer, L.1
  • 343
    • 0023373669 scopus 로고
    • The molecules of visual excitation
    • Stryer L. The molecules of visual excitation. Sci. Am. 257 (1987) 42-50
    • (1987) Sci. Am. , vol.257 , pp. 42-50
    • Stryer, L.1
  • 344
    • 0027043105 scopus 로고
    • Aspartic acid 85 in bacteriorhodopsin functions both as proton acceptor and negative counterion to the Schiff base
    • Subramaniam S., Greenhalgh D.A., and Khorana H.G. Aspartic acid 85 in bacteriorhodopsin functions both as proton acceptor and negative counterion to the Schiff base. J. Biol. Chem. 267 (1992) 25730-25733
    • (1992) J. Biol. Chem. , vol.267 , pp. 25730-25733
    • Subramaniam, S.1    Greenhalgh, D.A.2    Khorana, H.G.3
  • 345
    • 0019497625 scopus 로고
    • Primary photochemistry and photoisomerization of retinal at 77K in cattle and squid rhodopsins
    • Suzuki T., and Callender R.H. Primary photochemistry and photoisomerization of retinal at 77K in cattle and squid rhodopsins. Biophys. J. 34 (1981) 261-265
    • (1981) Biophys. J. , vol.34 , pp. 261-265
    • Suzuki, T.1    Callender, R.H.2
  • 348
    • 0028283324 scopus 로고
    • Active site lysine backbone undergoes conformational changes in the bacteriorhodopsin photocycle
    • Takei H., Gat Y., Rothman Z., Lewis A., and Sheves M. Active site lysine backbone undergoes conformational changes in the bacteriorhodopsin photocycle. J. Biol. Chem. 269 (1994) 7387-7389
    • (1994) J. Biol. Chem. , vol.269 , pp. 7387-7389
    • Takei, H.1    Gat, Y.2    Rothman, Z.3    Lewis, A.4    Sheves, M.5
  • 350
    • 77957052847 scopus 로고
    • Stereodynamic coupling of light energy and ion transport in the retinal proteins bacteriorhodopsin and halorhodopsin
    • Tavan P. Stereodynamic coupling of light energy and ion transport in the retinal proteins bacteriorhodopsin and halorhodopsin. Phys. Chem. 92 (1988) 1040-1045
    • (1988) Phys. Chem. , vol.92 , pp. 1040-1045
    • Tavan, P.1
  • 351
    • 0022455356 scopus 로고
    • Evidence for a 13, 14-cis cycle in bacteriorhodopsin
    • Tavan P., and Schulten K. Evidence for a 13, 14-cis cycle in bacteriorhodopsin. Biophys. J. 50 (1986) 81-89
    • (1986) Biophys. J. , vol.50 , pp. 81-89
    • Tavan, P.1    Schulten, K.2
  • 353
    • 0020079867 scopus 로고
    • Transverse location of the retinal chromophore of rhodopsin in rod outer disc membranes
    • Thomas D.D., and Stryer L. Transverse location of the retinal chromophore of rhodopsin in rod outer disc membranes. J. Mol. Biol. 154 (1982) 145-157
    • (1982) J. Mol. Biol. , vol.154 , pp. 145-157
    • Thomas, D.D.1    Stryer, L.2
  • 354
    • 0026733379 scopus 로고
    • Rotational resonance NMR study of the active site structure in bacteriorho-dopsin: conformation of the schiffbase linkage
    • Thompson L.K., McDermott A.E., Raap J., van der Wielen C.M., Lugtenburg J., Herzfeld J., and Griffen R.G. Rotational resonance NMR study of the active site structure in bacteriorho-dopsin: conformation of the schiffbase linkage. Biochemistry 31 (1992) 7931-7938
    • (1992) Biochemistry , vol.31 , pp. 7931-7938
    • Thompson, L.K.1    McDermott, A.E.2    Raap, J.3    van der Wielen, C.M.4    Lugtenburg, J.5    Herzfeld, J.6    Griffen, R.G.7
  • 355
    • 77957032191 scopus 로고
    • Balows A., Trüper H.G., Dworkin M., Harder W., and Schleifer K.-H. (Eds), Springer, Berlin
    • Tindall B.J. In: Balows A., Trüper H.G., Dworkin M., Harder W., and Schleifer K.-H. (Eds). The Prokaryotes: A Handbook on the Biology of Bacteria (1992), Springer, Berlin 769-808
    • (1992) The Prokaryotes: A Handbook on the Biology of Bacteria , pp. 769-808
    • Tindall, B.J.1
  • 356
    • 0025327261 scopus 로고
    • The quantum yield of bacteriorhodopsin
    • Tittor J., and Oesterhelt D. The quantum yield of bacteriorhodopsin. FEBS Lett. 263 (1990) 269-273
    • (1990) FEBS Lett. , vol.263 , pp. 269-273
    • Tittor, J.1    Oesterhelt, D.2
  • 357
    • 4243491025 scopus 로고
    • I. Primary electrogenic processed in bacteriorhodopsin probed by photoelectric measurements with capacitative metal electrodes
    • Trissl H.-W. I. Primary electrogenic processed in bacteriorhodopsin probed by photoelectric measurements with capacitative metal electrodes. Biochim. Biophys. Acta 806 (1985) 124-135
    • (1985) Biochim. Biophys. Acta , vol.806 , pp. 124-135
    • Trissl, H.-W.1
  • 358
    • 0023115506 scopus 로고
    • Rapid charge separation and bathochromic absorption shift of flash-excited bacteriorhodopsin containing 13-cis or all-trans forms of substituted retinals
    • Trissl H.-W., and Gärtner W. Rapid charge separation and bathochromic absorption shift of flash-excited bacteriorhodopsin containing 13-cis or all-trans forms of substituted retinals. Bio-chemistry 26 (1987) 751-758
    • (1987) Bio-chemistry , vol.26 , pp. 751-758
    • Trissl, H.-W.1    Gärtner, W.2
  • 359
    • 38249023291 scopus 로고
    • Reversed picosecond charge displacement from the photoproduct K of bacteriorhodopsin demonstrated photoelectrically
    • Trissl H.-W., Gärtner W., and Leibl W. Reversed picosecond charge displacement from the photoproduct K of bacteriorhodopsin demonstrated photoelectrically. Chem. Phys. Lett. 158 (1989) 515-518
    • (1989) Chem. Phys. Lett. , vol.158 , pp. 515-518
    • Trissl, H.-W.1    Gärtner, W.2    Leibl, W.3
  • 360
    • 0019302483 scopus 로고
    • Light isomerizes the chromophore of bacteriorhodopsin
    • Tsuda M., Glaccum M., Nelson B., and Ebrey T.G. Light isomerizes the chromophore of bacteriorhodopsin. Nature 287 (1980) 351-353
    • (1980) Nature , vol.287 , pp. 351-353
    • Tsuda, M.1    Glaccum, M.2    Nelson, B.3    Ebrey, T.G.4
  • 361
    • 0026447195 scopus 로고
    • Structure determination of the cyclohexene ring of retinal in bacteriorhodopsin by solid-state deuterium NMR
    • Ulrich A.S., Heyn M.P., and Watts A. Structure determination of the cyclohexene ring of retinal in bacteriorhodopsin by solid-state deuterium NMR. Biochemistry 31 (1992) 10390-10399
    • (1992) Biochemistry , vol.31 , pp. 10390-10399
    • Ulrich, A.S.1    Heyn, M.P.2    Watts, A.3
  • 362
    • 0024829219 scopus 로고
    • Orientation of retinal in purple membrane determined by polarized raman spectroscopy
    • Urabe H., Otomo J., and Ikegami A. Orientation of retinal in purple membrane determined by polarized raman spectroscopy. Biophys. J. 56 (1989) 1225-1228
    • (1989) Biophys. J. , vol.56 , pp. 1225-1228
    • Urabe, H.1    Otomo, J.2    Ikegami, A.3
  • 363
    • 0025370049 scopus 로고
    • Subpicosecond resonance Raman spectra of the early intermediates in the photocycle of bacteriorhodopsin
    • van den Berg R., Jang D.-J., Bitting H.C., and El-Sayed M.A. Subpicosecond resonance Raman spectra of the early intermediates in the photocycle of bacteriorhodopsin. Biophys. J. 58 (1990) 135-141
    • (1990) Biophys. J. , vol.58 , pp. 135-141
    • van den Berg, R.1    Jang, D.-J.2    Bitting, H.C.3    El-Sayed, M.A.4
  • 364
    • 33845375680 scopus 로고
    • Retinal analogues with locked 6-7 conformations show that bacteriorhodopsin requires the 6-s-trans conformation of the chromophore
    • van der Steen R., Biesheuvel P.L., Mathies R.A., and Lugtenburg J. Retinal analogues with locked 6-7 conformations show that bacteriorhodopsin requires the 6-s-trans conformation of the chromophore. J. Am. Chem. Soc. 108 (1986) 6410-6411
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 6410-6411
    • van der Steen, R.1    Biesheuvel, P.L.2    Mathies, R.A.3    Lugtenburg, J.4
  • 365
    • 0025723894 scopus 로고
    • Effects of the crystalline structure of purple membrane on the kinetics and energetics of the bacteriorhodopsin photocycle
    • Varo G., and Lanyi J.K. Effects of the crystalline structure of purple membrane on the kinetics and energetics of the bacteriorhodopsin photocycle. Biochem. 30 (1991) 7165-7171
    • (1991) Biochem. , vol.30 , pp. 7165-7171
    • Varo, G.1    Lanyi, J.K.2
  • 366
    • 0025871066 scopus 로고
    • Kinetic and spectroscopic evidence for an irreversible step between deprotonation and reprotonation of the schiff base on the bacteriorhodopsin photocycle
    • Váró G., and Lanyi J.K. Kinetic and spectroscopic evidence for an irreversible step between deprotonation and reprotonation of the schiff base on the bacteriorhodopsin photocycle. Biochem-istry 30 (1991) 5008-5015
    • (1991) Biochem-istry , vol.30 , pp. 5008-5015
    • Váró, G.1    Lanyi, J.K.2
  • 367
    • 0025820289 scopus 로고
    • Thermodynamics and energy coupling in the bacteriorhodopsin photocycle
    • Váró G., and Lanyi J.K. Thermodynamics and energy coupling in the bacteriorhodopsin photocycle. Biochemistry 30 (1991) 5016-5022
    • (1991) Biochemistry , vol.30 , pp. 5016-5022
    • Váró, G.1    Lanyi, J.K.2
  • 368
    • 0028066280 scopus 로고
    • 13C NMR chemical shifts for the chromophores of rhodopsin and bacteriorhodopsin. 1. Theoretical estima-tion of their ring-chain con
    • 13C NMR chemical shifts for the chromophores of rhodopsin and bacteriorhodopsin. 1. Theoretical estima-tion of their ring-chain con. J. Am. Chem. Soc. 116 (1994) 1537-1545
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 1537-1545
    • Wada, M.1    Sakurai, M.2    Inoue, Y.3    Tamura, Y.4    Watanabe, Y.5
  • 369
    • 0015921932 scopus 로고
    • Visual pigments. III. Determination and interpretation of the fluorescence quantum yields of retinals, Schiff bases and protonated Schiff bases
    • Waddell W.H., Schaffer A.M., and Becker R.S. Visual pigments. III. Determination and interpretation of the fluorescence quantum yields of retinals, Schiff bases and protonated Schiff bases. J. Am. Chem. Soc. 95 (1973) 8223-8227
    • (1973) J. Am. Chem. Soc. , vol.95 , pp. 8223-8227
    • Waddell, W.H.1    Schaffer, A.M.2    Becker, R.S.3
  • 370
    • 0014428724 scopus 로고
    • The molecular basis of visual excitation
    • Wald G. The molecular basis of visual excitation. Nature 219 (1968) 800-807
    • (1968) Nature , vol.219 , pp. 800-807
    • Wald, G.1
  • 371
    • 0001604008 scopus 로고
    • The dynamics of the primary event in rhodopsins revisited
    • Warshel A., Chu Z.T., and Hwang J.-K. The dynamics of the primary event in rhodopsins revisited. Chem. Phys. 158 (1991) 303-314
    • (1991) Chem. Phys. , vol.158 , pp. 303-314
    • Warshel, A.1    Chu, Z.T.2    Hwang, J.-K.3
  • 372
    • 0001628475 scopus 로고
    • Anew view of the dynamics of singlet cis-trans photoisomerization
    • Weiss R.M., and Warshel A. Anew view of the dynamics of singlet cis-trans photoisomerization. J. Am. Chem. Soc. 101 (1979) 6131-6133
    • (1979) J. Am. Chem. Soc. , vol.101 , pp. 6131-6133
    • Weiss, R.M.1    Warshel, A.2
  • 373
    • 0025052669 scopus 로고
    • Quantum efficiencies of bacteriorhodopsin photochemical reactions
    • Xie A. Quantum efficiencies of bacteriorhodopsin photochemical reactions. Biophys. J. 58 (1990) 1127-1132
    • (1990) Biophys. J. , vol.58 , pp. 1127-1132
    • Xie, A.1
  • 377
    • 37049065785 scopus 로고
    • Pre-lumirhodopsin and the bleaching of visual pigments
    • Yoshizawa T., and Wald G. Pre-lumirhodopsin and the bleaching of visual pigments. Nature 197 (1963) 1279-1286
    • (1963) Nature , vol.197 , pp. 1279-1286
    • Yoshizawa, T.1    Wald, G.2
  • 378
    • 0021705069 scopus 로고
    • Primary intermediates of rhodopsin studied by low temperature spectrophotometry and laser photolysis
    • Yoshizawa T., Shichida Y., and Matuoka S. Primary intermediates of rhodopsin studied by low temperature spectrophotometry and laser photolysis. Vision. Res. 24 (1984) 1455-1463
    • (1984) Vision. Res. , vol.24 , pp. 1455-1463
    • Yoshizawa, T.1    Shichida, Y.2    Matuoka, S.3
  • 379
    • 77957045636 scopus 로고
    • Two-Photon Spectroscopic and Molecular Orbital Studies of Light-Adapted Bacteriorhodopsin
    • Carnegie-Mellon University
    • Zhang C.-F. Two-Photon Spectroscopic and Molecular Orbital Studies of Light-Adapted Bacteriorhodopsin. Ph.D. (1989), Carnegie-Mellon University
    • (1989) Ph.D.
    • Zhang, C.-F.1
  • 382
    • 0024362631 scopus 로고
    • Effect of carboxylic acid side chains on the absorption maximum of visual pigments
    • Zhukovsky E.A., and Oprian D.D. Effect of carboxylic acid side chains on the absorption maximum of visual pigments. Science 246 (1989) 928-930
    • (1989) Science , vol.246 , pp. 928-930
    • Zhukovsky, E.A.1    Oprian, D.D.2
  • 383
    • 0026475571 scopus 로고
    • Changing the location of the schiff base counterion in rhodopsin
    • Zhukovsky E.A., Robinson P.R., and Oprian D.D. Changing the location of the schiff base counterion in rhodopsin. Biochemistry 31 (1992) 10400-10405
    • (1992) Biochemistry , vol.31 , pp. 10400-10405
    • Zhukovsky, E.A.1    Robinson, P.R.2    Oprian, D.D.3


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