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Volumn 46, Issue 21, 2007, Pages 6437-6445

Photoisomerization efficiency in UV-absorbing visual pigments: Protein-directed isomerization of an unprotonated retinal Schiff base

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINITY; CHROMOPHORES; PH; PHOTOISOMERIZATION; PROTEINS; ULTRAVIOLET RADIATION;

EID: 34249666129     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7003763     Document Type: Article
Times cited : (37)

References (51)
  • 1
    • 37049065785 scopus 로고
    • Pre-lumirhodopsin and the bleaching of visual pigments
    • Yoshizawa, T., and Wald, G. (1963) Pre-lumirhodopsin and the bleaching of visual pigments, Nature 197, 1279-1286.
    • (1963) Nature , vol.197 , pp. 1279-1286
    • Yoshizawa, T.1    Wald, G.2
  • 3
    • 0026091595 scopus 로고
    • The first step in vision: Femtosecond isomerization of rhodopsin
    • Schoenlein, R. W., Peteanu, L. A., Mathies, R. A., and Shank, C. V. (1991) The first step in vision: femtosecond isomerization of rhodopsin, Science 254, 412-415.
    • (1991) Science , vol.254 , pp. 412-415
    • Schoenlein, R.W.1    Peteanu, L.A.2    Mathies, R.A.3    Shank, C.V.4
  • 4
    • 0032412196 scopus 로고    scopus 로고
    • Visual pigment: G-protein-coupled receptor for light signals
    • Shichida, Y., and Imai, H. (1998) Visual pigment: G-protein-coupled receptor for light signals, Cell. Mol. Life Sci. 54, 1299-1315.
    • (1998) Cell. Mol. Life Sci , vol.54 , pp. 1299-1315
    • Shichida, Y.1    Imai, H.2
  • 5
    • 0026665777 scopus 로고
    • Primary structures of chicken cone visual pigments: Vertebrate rhodopsins have evolved out of cone visual pigments
    • Okano, T., Kojima, D., Fukada, Y., Shichida, Y., and Yoshizawa, T. (1992) Primary structures of chicken cone visual pigments: vertebrate rhodopsins have evolved out of cone visual pigments, Proc. Natl. Acad. Sci. U.S.A. 89, 5932-5936.
    • (1992) Proc. Natl. Acad. Sci. U.S.A , vol.89 , pp. 5932-5936
    • Okano, T.1    Kojima, D.2    Fukada, Y.3    Shichida, Y.4    Yoshizawa, T.5
  • 6
    • 0034002482 scopus 로고    scopus 로고
    • Molecular evolution of vertebrate visual pigments
    • Yokoyama, S. (2000) Molecular evolution of vertebrate visual pigments, Prog. Retinal Eye Res. 19, 385-419.
    • (2000) Prog. Retinal Eye Res , vol.19 , pp. 385-419
    • Yokoyama, S.1
  • 8
    • 0028351942 scopus 로고
    • An analysis of two spectral properties of vertebrate visual pigments
    • Harosi, F. I. (1994) An analysis of two spectral properties of vertebrate visual pigments, Vision Res. 34, 1359-1367.
    • (1994) Vision Res , vol.34 , pp. 1359-1367
    • Harosi, F.I.1
  • 9
    • 84986776518 scopus 로고
    • Tunable laser resonance Raman spectroscopy of the visual process. I: The spectrom of rhodopsin
    • Lewis, A., Fager, R. S., and Abrahamson, E. W. (1973) Tunable laser resonance Raman spectroscopy of the visual process. I: The spectrom of rhodopsin, J. Raman Spectrosc. 1, 465-470.
    • (1973) J. Raman Spectrosc , vol.1 , pp. 465-470
    • Lewis, A.1    Fager, R.S.2    Abrahamson, E.W.3
  • 10
    • 0016289846 scopus 로고
    • Resonance Raman spectroscopy of rhodopsin in retinal disk membranes
    • Oseroff, A. R., and Callender, R. H. (1974) Resonance Raman spectroscopy of rhodopsin in retinal disk membranes, Biochemistry 13, 4243-4248.
    • (1974) Biochemistry , vol.13 , pp. 4243-4248
    • Oseroff, A.R.1    Callender, R.H.2
  • 11
    • 0037188415 scopus 로고    scopus 로고
    • Spectral tuning in the mammalian short-wavelength sensitive cone pigments
    • Fasick, J. I., Applebury, M. L., and Oprian, D. D. (2002) Spectral tuning in the mammalian short-wavelength sensitive cone pigments, Biochemistry 41, 6860-6865.
    • (2002) Biochemistry , vol.41 , pp. 6860-6865
    • Fasick, J.I.1    Applebury, M.L.2    Oprian, D.D.3
  • 12
    • 0037031247 scopus 로고    scopus 로고
    • Phototransduction by vertebrate ultraviolet visual pigments: Protonation of the retinylidene Schiff base following photobleaching
    • Dukkipati, A., Kusnetzow, A., Babu, K. R., Ramos, L., Singh, D., Knox, B. E., and Birge, R. R. (2002) Phototransduction by vertebrate ultraviolet visual pigments: protonation of the retinylidene Schiff base following photobleaching, Biochemistry 41, 9842-9851.
    • (2002) Biochemistry , vol.41 , pp. 9842-9851
    • Dukkipati, A.1    Kusnetzow, A.2    Babu, K.R.3    Ramos, L.4    Singh, D.5    Knox, B.E.6    Birge, R.R.7
  • 13
    • 0031986508 scopus 로고    scopus 로고
    • Functional characterization of visual and nonvisual pigments of American chameleon (Anolis carolinensis)
    • Kawamura, S., and Yokoyama, S. (1998) Functional characterization of visual and nonvisual pigments of American chameleon (Anolis carolinensis), Vision Res. 38, 37-44.
    • (1998) Vision Res , vol.38 , pp. 37-44
    • Kawamura, S.1    Yokoyama, S.2
  • 14
    • 0032548795 scopus 로고    scopus 로고
    • Regeneration of ultraviolet pigments of vertebrates
    • Yokoyama, S., Radlwimmer, F. B., and Kawamura, S. (1998) Regeneration of ultraviolet pigments of vertebrates, FEBS Lett. 423, 155-158.
    • (1998) FEBS Lett , vol.423 , pp. 155-158
    • Yokoyama, S.1    Radlwimmer, F.B.2    Kawamura, S.3
  • 15
    • 0032519470 scopus 로고    scopus 로고
    • The molecular basis for UV vision in birds: Spectral characteristics, cDNA sequence and retinal localization of the UV-sensitive visual pigment of the budgerigar (Melopsittacus undulatus)
    • Wilkie, S. E., Vissers, P. M., Das, D., Degrip, W. J., Bowmaker, J. K., and Hunt, D. M. (1998) The molecular basis for UV vision in birds: spectral characteristics, cDNA sequence and retinal localization of the UV-sensitive visual pigment of the budgerigar (Melopsittacus undulatus), Biochem. J. 330 (Part 1), 541-547.
    • (1998) Biochem. J , vol.330 , Issue.PART 1 , pp. 541-547
    • Wilkie, S.E.1    Vissers, P.M.2    Das, D.3    Degrip, W.J.4    Bowmaker, J.K.5    Hunt, D.M.6
  • 16
    • 0024081391 scopus 로고
    • The visual process: Photophysics and photoisomerization of model visual pigments and the primary reaction
    • Becker, R. S. (1988) The visual process: photophysics and photoisomerization of model visual pigments and the primary reaction, Photochem. Photobiol. 48, 369-399.
    • (1988) Photochem. Photobiol , vol.48 , pp. 369-399
    • Becker, R.S.1
  • 17
    • 0025303725 scopus 로고
    • Nature of the primary photochemical events in rhodopsin and bacteriorhodopsin
    • Birge, R. R. (1990) Nature of the primary photochemical events in rhodopsin and bacteriorhodopsin, Biochim. Biophys. Acta 1016, 293-327.
    • (1990) Biochim. Biophys. Acta , vol.1016 , pp. 293-327
    • Birge, R.R.1
  • 18
    • 0035923444 scopus 로고    scopus 로고
    • Wavelength dependent cis-trans isomerization in vision
    • Kim, J. E., Tauber, M. J., and Mathies, R. A. (2001) Wavelength dependent cis-trans isomerization in vision, Biochemistry 40, 13774-13778.
    • (2001) Biochemistry , vol.40 , pp. 13774-13778
    • Kim, J.E.1    Tauber, M.J.2    Mathies, R.A.3
  • 19
    • 0014272718 scopus 로고
    • The photosensitivities of visual pigments in the presence of hydroxylamine
    • Dannali, H. J. (1968) The photosensitivities of visual pigments in the presence of hydroxylamine, Vision Res. 8, 339-358.
    • (1968) Vision Res , vol.8 , pp. 339-358
    • Dannali, H.J.1
  • 20
    • 0001092509 scopus 로고
    • Comprehensive investigation of the mechanism and photophysics of isomerization of a protonated and unprotonated Schiff base of 11-cis-retinal
    • Becker, R. S., and Freedman, K. (1985) Comprehensive investigation of the mechanism and photophysics of isomerization of a protonated and unprotonated Schiff base of 11-cis-retinal, J. Am. Chem. Soc. 107, 1477-1485.
    • (1985) J. Am. Chem. Soc , vol.107 , pp. 1477-1485
    • Becker, R.S.1    Freedman, K.2
  • 22
    • 0344736728 scopus 로고    scopus 로고
    • The molecular basis for the high photosensitivity of rhodopsin
    • Liu, R. S., and Colmenares, L. U. (2003) The molecular basis for the high photosensitivity of rhodopsin, Proc. Natl. Acad. Sci. U.S.A. 100, 14639-14644.
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 14639-14644
    • Liu, R.S.1    Colmenares, L.U.2
  • 23
    • 0024362631 scopus 로고
    • Effect of carboxylic acid side chains on the absorption maximum of visual pigments
    • Zhukovsky, E. A., and Oprian, D. D. (1989) Effect of carboxylic acid side chains on the absorption maximum of visual pigments, Science 246, 928-930.
    • (1989) Science , vol.246 , pp. 928-930
    • Zhukovsky, E.A.1    Oprian, D.D.2
  • 24
    • 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. (1989) Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin, Proc. Natl. Acad. Sci. U.S.A. 86, 8309-8313.
    • (1989) Proc. Natl. Acad. Sci. U.S.A , vol.86 , pp. 8309-8313
    • Sakmar, T.P.1    Franke, R.R.2    Khorana, H.G.3
  • 25
    • 0025162902 scopus 로고
    • Determinants of visual pigment absorbance: Identification of the retinylidene Schiff's base counterion in bovine rhodopsin
    • Nathans, J. (1990) Determinants of visual pigment absorbance: identification of the retinylidene Schiff's base counterion in bovine rhodopsin, Biochemistry 29, 9746-9752.
    • (1990) Biochemistry , vol.29 , pp. 9746-9752
    • Nathans, J.1
  • 27
    • 0025012994 scopus 로고
    • Determinants of visual pigment absorbance: Role of charged amino acids in the putative transmembrane segments
    • Nathans, J. (1990) Determinants of visual pigment absorbance: role of charged amino acids in the putative transmembrane segments, Biochemistry 29, 937-942.
    • (1990) Biochemistry , vol.29 , pp. 937-942
    • Nathans, J.1
  • 28
    • 28844498515 scopus 로고    scopus 로고
    • Generation of knockin mice carrying third cones with spectral sensitivity different from S and L cones
    • Onishi, A., Hasegawa, J., Imai, H., Chisaka, O., Ueda, Y., Honda, Y., Tachibana, M., and Shichida, Y. (2005) Generation of knockin mice carrying third cones with spectral sensitivity different from S and L cones, Zool. Sci. 22, 1145-1156.
    • (2005) Zool. Sci , vol.22 , pp. 1145-1156
    • Onishi, A.1    Hasegawa, J.2    Imai, H.3    Chisaka, O.4    Ueda, Y.5    Honda, Y.6    Tachibana, M.7    Shichida, Y.8
  • 29
    • 0026352455 scopus 로고
    • Design, chemical synthesis, and expression of genes for the three human color vision pigments
    • Oprian, D. D., Asenjo, A. B., Lee, N., and Pelletier, S. L. (1991) Design, chemical synthesis, and expression of genes for the three human color vision pigments, Biochemistry 30, 11367-11372.
    • (1991) Biochemistry , vol.30 , pp. 11367-11372
    • Oprian, D.D.1    Asenjo, A.B.2    Lee, N.3    Pelletier, S.L.4
  • 30
    • 0030908617 scopus 로고    scopus 로고
    • Water and peptide backbone structure in the active center of bovine rhodopsin
    • Nagata, T., Terakita, A., Kandori, H., Kojima, D., Shichida, Y., and Maeda, A. (1997) Water and peptide backbone structure in the active center of bovine rhodopsin, Biochemistry 36, 6164-6170.
    • (1997) Biochemistry , vol.36 , pp. 6164-6170
    • Nagata, T.1    Terakita, A.2    Kandori, H.3    Kojima, D.4    Shichida, Y.5    Maeda, A.6
  • 32
    • 0023850352 scopus 로고
    • SR alpha promoter: An efficient and versatile mammalian cDNA expression system composed of the simian virus 40 early promoter and the R-U5 segment of human T-cell leukemia vims type 1 long terminal repeat
    • Takebe, Y., Seiki, M., Fujisawa, J., Hoy, P., Yokota, K., Arai, K., Yoshida, M., and Arai, N. (1988) SR alpha promoter: an efficient and versatile mammalian cDNA expression system composed of the simian virus 40 early promoter and the R-U5 segment of human T-cell leukemia vims type 1 long terminal repeat, Mol. Cell. Biol. 8, 466-472.
    • (1988) Mol. Cell. Biol , vol.8 , pp. 466-472
    • Takebe, Y.1    Seiki, M.2    Fujisawa, J.3    Hoy, P.4    Yokota, K.5    Arai, K.6    Yoshida, M.7    Arai, N.8
  • 35
    • 0030461341 scopus 로고    scopus 로고
    • Chromophore configuration of iodopsin and its photoproducts formed at low temperatures
    • Imamoto, Y., Yoshizawa, T., and Shichida, Y. (1996) Chromophore configuration of iodopsin and its photoproducts formed at low temperatures, Biochemistry 35, 14599-14607.
    • (1996) Biochemistry , vol.35 , pp. 14599-14607
    • Imamoto, Y.1    Yoshizawa, T.2    Shichida, Y.3
  • 36
    • 25444453372 scopus 로고
    • High-performance liquid chromatographic and spectroscopic characterization of stereoisomeric retinaloximes Improvements in resolution and implications of the method
    • Tsukida, K., Ito, M., Tanaka, T., and Yagi, I. (1985) High-performance liquid chromatographic and spectroscopic characterization of stereoisomeric retinaloximes Improvements in resolution and implications of the method, J. Chromatogr. 331, 265-272.
    • (1985) J. Chromatogr , vol.331 , pp. 265-272
    • Tsukida, K.1    Ito, M.2    Tanaka, T.3    Yagi, I.4
  • 37
    • 0025090614 scopus 로고
    • On retention of chromophore configuration of rhodopsin isomers derived from three dicis retinal isomers
    • Trehan, A., Liu, R. S. H., Shichida, Y., Imamoto, Y., Nakamura, K., and Yoshizawa, T. (1990) On retention of chromophore configuration of rhodopsin isomers derived from three dicis retinal isomers, Bioorg. Chem. 18, 30-40.
    • (1990) Bioorg. Chem , vol.18 , pp. 30-40
    • Trehan, A.1    Liu, R.S.H.2    Shichida, Y.3    Imamoto, Y.4    Nakamura, K.5    Yoshizawa, T.6
  • 38
    • 0033533398 scopus 로고    scopus 로고
    • Spectral tuning in the human blue cone pigment
    • Fasick, J. I., Lee, N., and Oprian, D. D. (1999) Spectral tuning in the human blue cone pigment, Biochemistry 38, 11593-11596.
    • (1999) Biochemistry , vol.38 , pp. 11593-11596
    • Fasick, J.I.1    Lee, N.2    Oprian, D.D.3
  • 39
    • 0000073823 scopus 로고
    • The molar extinction of rhodopsin
    • Wald, G., and Brown, P. K. (1953) The molar extinction of rhodopsin, J. Gen. Physiol. 37, 189-200.
    • (1953) J. Gen. Physiol , vol.37 , pp. 189-200
    • Wald, G.1    Brown, P.K.2
  • 40
    • 0037465429 scopus 로고    scopus 로고
    • Characterization of rhodopsin congenital night blindness mutant T94I
    • Gross, A. K., Rao, V. R., and Oprian, D. D. (2003) Characterization of rhodopsin congenital night blindness mutant T94I, Biochemistry 42, 2009-2015.
    • (2003) Biochemistry , vol.42 , pp. 2009-2015
    • Gross, A.K.1    Rao, V.R.2    Oprian, D.D.3
  • 41
    • 0034711712 scopus 로고    scopus 로고
    • pH dependence of photolysis intermediates in the photoactivation of rhodopsin mutant E113Q
    • Lewis, J. W., Szundi, I., Fu, W. Y., Sakmar, T. P., and Kliger, D. S. (2000) pH dependence of photolysis intermediates in the photoactivation of rhodopsin mutant E113Q, Biochemistry 39, 599-606.
    • (2000) Biochemistry , vol.39 , pp. 599-606
    • Lewis, J.W.1    Szundi, I.2    Fu, W.Y.3    Sakmar, T.P.4    Kliger, D.S.5
  • 42
    • 0027820508 scopus 로고
    • Light-dependent transducin activation by an ultraviolet-absorbing rhodopsin mutant
    • Fahmy, K., and Sakmar, T. P. (1993) Light-dependent transducin activation by an ultraviolet-absorbing rhodopsin mutant, Biochemistry 32, 9165-9171.
    • (1993) Biochemistry , vol.32 , pp. 9165-9171
    • Fahmy, K.1    Sakmar, T.P.2
  • 43
    • 0030174901 scopus 로고    scopus 로고
    • Fluorescence properties of protonated and unprotonated Schiff bases of retinal at room temperature
    • Bachilo, S. M., Bondarev, S. L., and Gillbro, T. (1996) Fluorescence properties of protonated and unprotonated Schiff bases of retinal at room temperature, J. Photochem. Photobiol. B 34, 39-46.
    • (1996) J. Photochem. Photobiol. B , vol.34 , pp. 39-46
    • Bachilo, S.M.1    Bondarev, S.L.2    Gillbro, T.3
  • 44
    • 0001718556 scopus 로고
    • Retinal has a highly dipolar vertically excited singlet state: Implications for vision
    • Mathies, R., and Stryer, L. (1976) Retinal has a highly dipolar vertically excited singlet state: implications for vision, Proc. Natl. Acad. Sci. U.S.A. 73, 2169-2173.
    • (1976) Proc. Natl. Acad. Sci. U.S.A , vol.73 , pp. 2169-2173
    • Mathies, R.1    Stryer, L.2
  • 45
    • 11444267304 scopus 로고    scopus 로고
    • How the counterion affects ground- and excited-state properties of the rhodopsin chromophore
    • Hufen, J., Sugihara, M., and Buss, V. (2004) How the counterion affects ground- and excited-state properties of the rhodopsin chromophore, J. Phys. Chem. B 108, 20419-20426.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 20419-20426
    • Hufen, J.1    Sugihara, M.2    Buss, V.3
  • 46
    • 23244431748 scopus 로고    scopus 로고
    • Probing the ultrafast charge translocation of photoexcited retinal in bacteriorhodopsin
    • Schenkl, S., van Mourik, F., van der Zwan, G., Haacke, S., and Chergui, M. (2005) Probing the ultrafast charge translocation of photoexcited retinal in bacteriorhodopsin, Science 309, 917-920.
    • (2005) Science , vol.309 , pp. 917-920
    • Schenkl, S.1    van Mourik, F.2    van der Zwan, G.3    Haacke, S.4    Chergui, M.5
  • 47
    • 0022687552 scopus 로고
    • Investigation into the spectroscopy and photoisomerization of a series of poly (ethylene glycol) peptide Schiff bases of 11-cis retinal
    • Freedman, K., Becker, R. S., Hannak, D., and Bayer, E. (1986) Investigation into the spectroscopy and photoisomerization of a series of poly (ethylene glycol) peptide Schiff bases of 11-cis retinal, Photochem. Photobiol. 43, 291-295.
    • (1986) Photochem. Photobiol , vol.43 , pp. 291-295
    • Freedman, K.1    Becker, R.S.2    Hannak, D.3    Bayer, E.4
  • 48
    • 4344581120 scopus 로고    scopus 로고
    • The retinal conformation and its environment in rhodopsin in light of a new 2.2 Å crystal structure
    • Okada, T., Sugihara, M., Bondar, A. N., Elstner, M., Entel, P., and Buss, V. (2004) The retinal conformation and its environment in rhodopsin in light of a new 2.2 Å crystal structure, J. Mol. Biol. 342, 571-583.
    • (2004) J. Mol. Biol , vol.342 , pp. 571-583
    • Okada, T.1    Sugihara, M.2    Bondar, A.N.3    Elstner, M.4    Entel, P.5    Buss, V.6
  • 49
    • 0030471282 scopus 로고    scopus 로고
    • Retinal analog study of the role of steric interactions in the excited state isomerization dynamics of rhodopsin
    • Kochendoerfer, G. G., Verdegem, P. J., van der Hoef, I., Lugtenburg, J., and Mathies, R. A. (1996) Retinal analog study of the role of steric interactions in the excited state isomerization dynamics of rhodopsin, Biochemistry 35, 16230-16240.
    • (1996) Biochemistry , vol.35 , pp. 16230-16240
    • Kochendoerfer, G.G.1    Verdegem, P.J.2    van der Hoef, I.3    Lugtenburg, J.4    Mathies, R.A.5
  • 50
    • 18244373415 scopus 로고    scopus 로고
    • The retinal chromophore/chloride ion pair: Structure of the photoisomerization path and interplay of charge transfer and covalent states
    • Cembran, A., Bernardi, F., Olivucci, M., and Garavelli, M. (2005) The retinal chromophore/chloride ion pair: structure of the photoisomerization path and interplay of charge transfer and covalent states, Proc. Natl. Acad. Sci. U.S.A. 102, 6255-6260.
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 6255-6260
    • Cembran, A.1    Bernardi, F.2    Olivucci, M.3    Garavelli, M.4
  • 51
    • 0030008653 scopus 로고    scopus 로고
    • Multiple visual pigments in a photoreceptor of the salamander retina
    • Makino, C. L., and Dodd, R. L. (1996) Multiple visual pigments in a photoreceptor of the salamander retina, J. Gen. Physiol. 108, 27-34.
    • (1996) J. Gen. Physiol , vol.108 , pp. 27-34
    • Makino, C.L.1    Dodd, R.L.2


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