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Volumn 9, Issue 11, 2010, Pages 1426-1434

Multiple functions of Schiff base counterion in rhodopsins

Author keywords

[No Author keywords available]

Indexed keywords

BOVINAE; VERTEBRATA;

EID: 78049436281     PISSN: 1474905X     EISSN: 14749092     Source Type: Journal    
DOI: 10.1039/c0pp00134a     Document Type: Article
Times cited : (19)

References (85)
  • 2
    • 0001287274 scopus 로고
    • Studies on rhodopsin. VIII. Retinylidenemethylamine, an indicator yellow analogue
    • G. A. Pitt F. D. Collins R. A. Morton P. Stok Studies on rhodopsin. VIII. Retinylidenemethylamine, an indicator yellow analogue Biochem. J. 1955 59 122 128
    • (1955) Biochem. J. , vol.59 , pp. 122-128
    • Pitt, G.A.1    Collins, F.D.2    Morton, R.A.3    Stok, P.4
  • 3
    • 0033622140 scopus 로고    scopus 로고
    • a of the protonated Schiff base of visual pigments
    • a of the protonated Schiff base of visual pigments Methods Enzymol. 2000 315 196 207
    • (2000) Methods Enzymol. , vol.315 , pp. 196-207
    • Ebrey, T.G.1
  • 4
    • 0000388260 scopus 로고
    • The mechanism of bleaching rhodopsin
    • A. Kropf R. Hubbard The mechanism of bleaching rhodopsin Ann. N. Y. Acad. Sci. 1958 74 266 280
    • (1958) Ann. N. Y. Acad. Sci. , vol.74 , pp. 266-280
    • Kropf, A.1    Hubbard, R.2
  • 5
    • 0024362631 scopus 로고
    • Effect of carboxylic acid side chains on the absorption maximum of visual pigments
    • E. A. Zhukovsky D. D. Oprian Effect of carboxylic acid side chains on the absorption maximum of visual pigments Science 1989 246 928 930
    • (1989) Science , vol.246 , pp. 928-930
    • Zhukovsky, E.A.1    Oprian, D.D.2
  • 6
    • 0343177634 scopus 로고
    • Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin
    • T. P. Sakmar R. R. Franke H. G. Khorana Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin Proc. Natl. Acad. Sci. U. S. A. 1989 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
  • 7
    • 0025162902 scopus 로고
    • Determinants of visual pigment absorbance: Identification of the retinylidene Schiff's base counterion in bovine rhodopsin
    • J. Nathans Determinants of visual pigment absorbance: Identification of the retinylidene Schiff's base counterion in bovine rhodopsin Biochemistry 1990 29 9746 9752
    • (1990) Biochemistry , vol.29 , pp. 9746-9752
    • Nathans, J.1
  • 8
    • 0026750971 scopus 로고
    • Resonance Raman microprobe spectroscopy of rhodopsin mutants: Effect of substitutions in the third transmembrane helix
    • S. W. Lin T. P. Sakmar R. R. Franke H. G. Khorana R. A. Mathies Resonance Raman microprobe spectroscopy of rhodopsin mutants: Effect of substitutions in the third transmembrane helix Biochemistry 1992 31 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
  • 11
    • 84989691688 scopus 로고
    • Energetics of protonation-deprotonation of the chromophore in retinal proteins
    • Y. Beppu T. Kakitani F. Tokunaga Energetics of protonation-deprotonation of the chromophore in retinal proteins Photochem. Photobiol. 1992 56 1113 1117
    • (1992) Photochem. Photobiol. , vol.56 , pp. 1113-1117
    • Beppu, Y.1    Kakitani, T.2    Tokunaga, F.3
  • 12
    • 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. 1993 115 3772 3773
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 3772-3773
    • Gat, Y.1    Sheves, M.2
  • 16
    • 0032546920 scopus 로고    scopus 로고
    • Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution
    • H. Luecke H. T. Richter J. K. Lanyi Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution Science 1998 280 1934 1937
    • (1998) Science , vol.280 , pp. 1934-1937
    • Luecke, H.1    Richter, H.T.2    Lanyi, J.K.3
  • 17
    • 1642398852 scopus 로고    scopus 로고
    • The nature of the complex counterion of the chromophore in rhodopsin
    • M. Sugahara V. Buss P. Entel J. Hafner The nature of the complex counterion of the chromophore in rhodopsin J. Phys. Chem. B 2004 108 3673 3680
    • (2004) J. Phys. Chem. B , vol.108 , pp. 3673-3680
    • Sugahara, M.1    Buss, V.2    Entel, P.3    Hafner, J.4
  • 18
    • 0042768527 scopus 로고    scopus 로고
    • Thr94 and Wat2b effect protonation of the retinal chromophore in rhodopsin
    • V. Buss M. Sugihara P. Entel J. Hafner Thr94 and Wat2b effect protonation of the retinal chromophore in rhodopsin Angew. Chem., Int. Ed. 2003 42 3245 3247
    • (2003) Angew. Chem., Int. Ed. , vol.42 , pp. 3245-3247
    • Buss, V.1    Sugihara, M.2    Entel, P.3    Hafner, J.4
  • 21
    • 0037133528 scopus 로고    scopus 로고
    • Function of extracellular loop 2 in rhodopsin: Glutamic acid 181 modulates stability and absorption wavelength of metarhodopsin II
    • E. C. Y. Yan M. A. Kazmi S. De B. S. W. Chang C. Seibert E. P. Marin R. A. Mathies T. P. Sakmar Function of extracellular loop 2 in rhodopsin: Glutamic acid 181 modulates stability and absorption wavelength of metarhodopsin II Biochemistry 2002 41 3620 3627
    • (2002) Biochemistry , vol.41 , pp. 3620-3627
    • Yan, E.C.Y.1    Kazmi, M.A.2    De, S.3    Chang, B.S.W.4    Seibert, C.5    Marin, E.P.6    Mathies, R.A.7    Sakmar, T.P.8
  • 22
    • 0033621078 scopus 로고    scopus 로고
    • Photochemistry of the primary event in short-wavelength visual opsins at low temperature
    • B. W. Vought A. Dukkipatti M. Max B. E. Knox R. R. Birge Photochemistry of the primary event in short-wavelength visual opsins at low temperature Biochemistry 1999 38 11287 11297
    • (1999) Biochemistry , vol.38 , pp. 11287-11297
    • Vought, B.W.1    Dukkipatti, A.2    Max, M.3    Knox, B.E.4    Birge, R.R.5
  • 23
    • 0347948267 scopus 로고    scopus 로고
    • Exploring the opsin shift with ab initio methods: Geometry and counterion effects on the electronic spectrum of retinal
    • M. Schreiber V. Buss M. Sugihara Exploring the opsin shift with ab initio methods: Geometry and counterion effects on the electronic spectrum of retinal J. Chem. Phys. 2003 119 12045 12048
    • (2003) J. Chem. Phys. , vol.119 , pp. 12045-12048
    • Schreiber, M.1    Buss, V.2    Sugihara, M.3
  • 24
    • 52049114905 scopus 로고    scopus 로고
    • Three-layer ONIOM studies of the dark state of rhodopsin: The protonation state of Glu181, 2008
    • K. F. Hall T. Vreven M. J. Frisch M. J. Bearpark Three-layer ONIOM studies of the dark state of rhodopsin: The protonation state of Glu181, 2008 J. Mol. Biol. 2008 383 106 121
    • (2008) J. Mol. Biol. , vol.383 , pp. 106-121
    • Hall, K.F.1    Vreven, T.2    Frisch, M.J.3    Bearpark, M.J.4
  • 27
    • 70350322971 scopus 로고    scopus 로고
    • 6-s-cis conformation and polar binding pocket of the retinal chromophore in the photoactivated state of rhodopsin
    • S. Ahuja M. Eilers A. Hirshfeld E. C. Y. Yan M. Ziliox T. P. Sakmar M. Sheves S. O. Smith 6-s-cis conformation and polar binding pocket of the retinal chromophore in the photoactivated state of rhodopsin J. Am. Chem. Soc. 2009 131 15160 15169
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 15160-15169
    • Ahuja, S.1    Eilers, M.2    Hirshfeld, A.3    Yan, E.C.Y.4    Ziliox, M.5    Sakmar, T.P.6    Sheves, M.7    Smith, S.O.8
  • 28
    • 67849111388 scopus 로고    scopus 로고
    • Glutamic acid 181 is uncharged in dark-adapted visual rhodopsin
    • S. Sekharan V. Buss Glutamic acid 181 is uncharged in dark-adapted visual rhodopsin J. Am. Chem. Soc. 2008 130 17220 17221
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 17220-17221
    • Sekharan, S.1    Buss, V.2
  • 30
    • 0034687783 scopus 로고    scopus 로고
    • Highly conserved glutamic acid in the extracellular IV-V loop in rhodopsins acts as the counterion in retinochrome, a member of the rhodopsin family
    • A. Terakita T. Yamashita Y. Shichida Highly conserved glutamic acid in the extracellular IV-V loop in rhodopsins acts as the counterion in retinochrome, a member of the rhodopsin family Proc. Natl. Acad. Sci. U. S. A. 2000 97 14263 14267
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 14263-14267
    • Terakita, A.1    Yamashita, T.2    Shichida, Y.3
  • 31
    • 34547264066 scopus 로고    scopus 로고
    • Photointermediates of the rhodopsin S186A mutant as a probe of the hydrogen-bond network in the chromophore pocket and the mechanism of counterion switch
    • E. C. Y. Yan J. Epps J. W. Lewis I. Szundi A. Bhagat T. P. Sakmar D. S. Kliger Photointermediates of the rhodopsin S186A mutant as a probe of the hydrogen-bond network in the chromophore pocket and the mechanism of counterion switch J. Phys. Chem. C 2007 111 8843 8848
    • (2007) J. Phys. Chem. C , vol.111 , pp. 8843-8848
    • Yan, E.C.Y.1    Epps, J.2    Lewis, J.W.3    Szundi, I.4    Bhagat, A.5    Sakmar, T.P.6    Kliger, D.S.7
  • 32
    • 44649152217 scopus 로고    scopus 로고
    • Structural impact of the E113Q counterion mutation on the activation and deactivation pathways of the G protein-coupled receptor rhodopsin
    • J. Standfuss E. Zaitseva M. Mahalingam R. Vogel Structural impact of the E113Q counterion mutation on the activation and deactivation pathways of the G protein-coupled receptor rhodopsin J. Mol. Biol. 2008 380 145 157
    • (2008) J. Mol. Biol. , vol.380 , pp. 145-157
    • Standfuss, J.1    Zaitseva, E.2    Mahalingam, M.3    Vogel, R.4
  • 33
    • 53749087534 scopus 로고    scopus 로고
    • E113 is required for the efficient photoisomerization of the unprotonated chromophore in a UV-absorbing visual pigment
    • K. Tsutsui H. Imai Y. Shichida E113 is required for the efficient photoisomerization of the unprotonated chromophore in a UV-absorbing visual pigment Biochemistry 2008 47 10829 10833
    • (2008) Biochemistry , vol.47 , pp. 10829-10833
    • Tsutsui, K.1    Imai, H.2    Shichida, Y.3
  • 34
    • 33745029510 scopus 로고    scopus 로고
    • Vertebrate opsins belonging to different classes vary in constitutively active properties resulting from salt-bridge mutations
    • B. Nickle S. E. Wilkie J. A. Cowing D. M. Hunt P. R. Robinson Vertebrate opsins belonging to different classes vary in constitutively active properties resulting from salt-bridge mutations Biochemistry 2006 45 7307 7313
    • (2006) Biochemistry , vol.45 , pp. 7307-7313
    • Nickle, B.1    Wilkie, S.E.2    Cowing, J.A.3    Hunt, D.M.4    Robinson, P.R.5
  • 35
    • 0343580431 scopus 로고    scopus 로고
    • A comparison of the efficiency of G protein activation by ligand-free and light-activated forms of rhodopsin
    • T. J. Melia C. W. Cowan J. K. Angleson T. G. Wensel A comparison of the efficiency of G protein activation by ligand-free and light-activated forms of rhodopsin Biophys. J. 1997 73 3182 3191
    • (1997) Biophys. J. , vol.73 , pp. 3182-3191
    • Melia, T.J.1    Cowan, C.W.2    Angleson, J.K.3    Wensel, T.G.4
  • 37
    • 0028125886 scopus 로고
    • Rhodopsin mutation G90D and a molecular mechanism for congenital night blindness
    • V. R. Rao G. B. Cohen D. D. Oprian Rhodopsin mutation G90D and a molecular mechanism for congenital night blindness Nature 1994 367 639 642
    • (1994) Nature , vol.367 , pp. 639-642
    • Rao, V.R.1    Cohen, G.B.2    Oprian, D.D.3
  • 38
    • 0037465429 scopus 로고    scopus 로고
    • Characterization of rhodopsin congenital night blindness mutant T94I
    • A. K. Gross V. R. Rao D. D. Oprian Characterization of rhodopsin congenital night blindness mutant T94I Biochemistry 2003 42 2009 2015
    • (2003) Biochemistry , vol.42 , pp. 2009-2015
    • Gross, A.K.1    Rao, V.R.2    Oprian, D.D.3
  • 39
    • 0027248024 scopus 로고
    • Heterozygous missense mutation in the rhodopsin gene as a cause of congenital stationary night blindness
    • T. P. Dryja E. L. Berson V. R. Rao D. D. Oprian Heterozygous missense mutation in the rhodopsin gene as a cause of congenital stationary night blindness Nat. Genet. 1993 4 280 283
    • (1993) Nat. Genet. , vol.4 , pp. 280-283
    • Dryja, T.P.1    Berson, E.L.2    Rao, V.R.3    Oprian, D.D.4
  • 40
    • 0029993990 scopus 로고    scopus 로고
    • Activating mutations of rhodopsin and other G protein-coupled receptors
    • V. R. Rao D. D. Oprian Activating mutations of rhodopsin and other G protein-coupled receptors Annu. Rev. Biophys. Biomol. Struct. 1996 25 287 314
    • (1996) Annu. Rev. Biophys. Biomol. Struct. , vol.25 , pp. 287-314
    • Rao, V.R.1    Oprian, D.D.2
  • 42
    • 29344435298 scopus 로고    scopus 로고
    • Constitutive activity of a UV cone opsin
    • M. Kono Constitutive activity of a UV cone opsin FEBS Lett. 2006 580 229 232
    • (2006) FEBS Lett. , vol.580 , pp. 229-232
    • Kono, M.1
  • 43
    • 0037465424 scopus 로고    scopus 로고
    • Slow binding of retinal to rhodopsin mutants G90D and T94D
    • A. K. Gross G. Xie D. D. Oprian Slow binding of retinal to rhodopsin mutants G90D and T94D Biochemistry 2003 42 2002 2008
    • (2003) Biochemistry , vol.42 , pp. 2002-2008
    • Gross, A.K.1    Xie, G.2    Oprian, D.D.3
  • 44
    • 0242494305 scopus 로고    scopus 로고
    • Assessing structural elements that influence Schiff base stability: Mutants E113Q and D190N destabilize rhodopsin through different mechanisms
    • J. M. Janz D. L. Farrens Assessing structural elements that influence Schiff base stability: Mutants E113Q and D190N destabilize rhodopsin through different mechanisms Vision Res. 2003 43 2991 3002
    • (2003) Vision Res. , vol.43 , pp. 2991-3002
    • Janz, J.M.1    Farrens, D.L.2
  • 45
    • 34249666129 scopus 로고    scopus 로고
    • Photoisomerization efficiency in UV-absorbing visual pigments: Protein-directed isomerization of an unprotonated retinal Schiff base
    • K. Tsutsui H. Imai Y. Shichida Photoisomerization efficiency in UV-absorbing visual pigments: Protein-directed isomerization of an unprotonated retinal Schiff base Biochemistry 2007 46 6437 6445
    • (2007) Biochemistry , vol.46 , pp. 6437-6445
    • Tsutsui, K.1    Imai, H.2    Shichida, Y.3
  • 46
    • 11244264401 scopus 로고    scopus 로고
    • Role of the retinal hydrogen bond network in rhodopsin Schiff base stability and hydrolysis
    • J. M. Janz D. L. Farrens Role of the retinal hydrogen bond network in rhodopsin Schiff base stability and hydrolysis J. Biol. Chem. 2004 279 55886 55894
    • (2004) J. Biol. Chem. , vol.279 , pp. 55886-55894
    • Janz, J.M.1    Farrens, D.L.2
  • 48
    • 0014406466 scopus 로고
    • Absorption spectrum of rhodopsin denatured with acid
    • Y. Kito T. Suzuki M. Azuma Y. Sekoguti Absorption spectrum of rhodopsin denatured with acid Nature 1968 218 955 957
    • (1968) Nature , vol.218 , pp. 955-957
    • Kito, Y.1    Suzuki, T.2    Azuma, M.3    Sekoguti, Y.4
  • 51
    • 33846065828 scopus 로고    scopus 로고
    • Origin of spectral tuning in rhodopsin-It is not the binding pocket
    • S. Sekharan M. Sugihara V. Buss Origin of spectral tuning in rhodopsin-It is not the binding pocket Angew. Chem., Int. Ed. 2007 46 269 271
    • (2007) Angew. Chem., Int. Ed. , vol.46 , pp. 269-271
    • Sekharan, S.1    Sugihara, M.2    Buss, V.3
  • 52
    • 11144239039 scopus 로고    scopus 로고
    • Structure, initial excited-state relaxation, and energy storage of rhodopsin resolved at the multiconfigurational perturbation theory level
    • T. Andruniów N. Ferré M. Olivucci Structure, initial excited-state relaxation, and energy storage of rhodopsin resolved at the multiconfigurational perturbation theory level Proc. Natl. Acad. Sci. U. S. A. 2004 101 17908 17913
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 17908-17913
    • Andruniów, T.1    Ferré, N.2    Olivucci, M.3
  • 54
    • 0001092509 scopus 로고
    • A comprehensive investigation of the mechanism and photophysics of isomerization of a protonated and unprotonated Schiff base of 11-cis-retinal
    • R. S. Becker K. Freedman A comprehensive investigation of the mechanism and photophysics of isomerization of a protonated and unprotonated Schiff base of 11-cis-retinal J. Am. Chem. Soc. 1985 107 1477 1485
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 1477-1485
    • Becker, R.S.1    Freedman, K.2
  • 55
    • 0035923444 scopus 로고    scopus 로고
    • Wavelength dependent cis-trans isomerization in vision
    • J. E. Kim M. J. Tauber R. A. Mathies Wavelength dependent cis-trans isomerization in vision Biochemistry 2001 40 13774 13778
    • (2001) Biochemistry , vol.40 , pp. 13774-13778
    • Kim, J.E.1    Tauber, M.J.2    Mathies, R.A.3
  • 56
    • 0037188415 scopus 로고    scopus 로고
    • Spectral tuning in the mammalian short-wavelength sensitive cone pigments
    • J. I. Fasick M. L. Applebury D. D. Oprian Spectral tuning in the mammalian short-wavelength sensitive cone pigments Biochemistry 2002 41 6860 6865
    • (2002) Biochemistry , vol.41 , pp. 6860-6865
    • Fasick, J.I.1    Applebury, M.L.2    Oprian, D.D.3
  • 57
    • 0037031247 scopus 로고    scopus 로고
    • Phototransduction by vertebrate ultraviolet visual pigments: Protonation of the retinylidene Schiff base following photobleaching
    • A. Dukkipati A. Kusnetzow K. R. Babu L. Ramos D. Singh B. E. Knox R. R. Birge Phototransduction by vertebrate ultraviolet visual pigments: Protonation of the retinylidene Schiff base following photobleaching Biochemistry 2002 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
  • 58
    • 0024081391 scopus 로고
    • The visual process: Photophysics and photoisomerization of model visual pigments and the primary reaction
    • R. S. Becker The visual process: Photophysics and photoisomerization of model visual pigments and the primary reaction Photochem. Photobiol. 1988 48 369 399
    • (1988) Photochem. Photobiol. , vol.48 , pp. 369-399
    • Becker, R.S.1
  • 59
    • 0025303725 scopus 로고
    • Nature of the primary photochemical events in rhodopsin and bacteriorhodopsin
    • R. R. Birge Nature of the primary photochemical events in rhodopsin and bacteriorhodopsin Biochim. Biophys. Acta, Bioenerg. 1990 1016 293 327
    • (1990) Biochim. Biophys. Acta, Bioenerg. , vol.1016 , pp. 293-327
    • Birge, R.R.1
  • 60
    • 12944335314 scopus 로고    scopus 로고
    • Ultraviolet pigments in birds evolved from violet pigments by a single amino acid change
    • S. Yokoyama F. B. Radlwimmer N. S. Blow Ultraviolet pigments in birds evolved from violet pigments by a single amino acid change Proc. Natl. Acad. Sci. U. S. A. 2000 97 7366 7371
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 7366-7371
    • Yokoyama, S.1    Radlwimmer, F.B.2    Blow, N.S.3
  • 61
    • 0027303125 scopus 로고
    • Protein catalysis of the retinal subpicosecond photoisomerization in the primary process of bacteriorhodopsin photosynthesis
    • L. Song M. A. El-Sayed J. K. Lanyi Protein catalysis of the retinal subpicosecond photoisomerization in the primary process of bacteriorhodopsin photosynthesis Science 1993 261 891 894
    • (1993) Science , vol.261 , pp. 891-894
    • Song, L.1    El-Sayed, M.A.2    Lanyi, J.K.3
  • 64
    • 10444237332 scopus 로고    scopus 로고
    • Counterion controlled photoisomerization of retinal chromophore models: A computational investigation
    • A. Cembran F. Bernardi M. Olivucci M. Garavelli Counterion controlled photoisomerization of retinal chromophore models: A computational investigation J. Am. Chem. Soc. 2004 126 16018 16037
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 16018-16037
    • Cembran, A.1    Bernardi, F.2    Olivucci, M.3    Garavelli, M.4
  • 65
    • 11444267304 scopus 로고    scopus 로고
    • How the counterion affects ground- and excited-state properties of the rhodopsin chromophore
    • J. Hufen M. Sugihara V. Buss How the counterion affects ground- and excited-state properties of the rhodopsin chromophore J. Phys. Chem. B 2004 108 20419 20426
    • (2004) J. Phys. Chem. B , vol.108 , pp. 20419-20426
    • Hufen, J.1    Sugihara, M.2    Buss, V.3
  • 66
    • 18244373415 scopus 로고    scopus 로고
    • The retinal chromophore/chloride ion pair: Structure of the photoisomerization path and interplay of charge transfer and covalent states
    • A. Cembran F. Bernardi M. Olivucci M. Garavelli 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. 2005 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
  • 67
    • 0028017506 scopus 로고
    • Identification of glutamic acid 113 as the Schiff base proton acceptor in the metarhodopsin II photointermediate of rhodopsin
    • F. Jäger K. Fahmy T. P. Sakmar F. Siebert Identification of glutamic acid 113 as the Schiff base proton acceptor in the metarhodopsin II photointermediate of rhodopsin Biochemistry 1994 33 10878 10882
    • (1994) Biochemistry , vol.33 , pp. 10878-10882
    • Jäger, F.1    Fahmy, K.2    Sakmar, T.P.3    Siebert, F.4
  • 68
    • 25444483072 scopus 로고    scopus 로고
    • Molecular properties of rod and cone visual pigments from purified chicken cone pigments to mouse rhodopsin in situ
    • H. Imai S. Kuwayama A. Onishi T. Morizumi O. Chisaka Y. Shichida Molecular properties of rod and cone visual pigments from purified chicken cone pigments to mouse rhodopsin in situ Photochem. Photobiol. Sci. 2005 4 667 674
    • (2005) Photochem. Photobiol. Sci. , vol.4 , pp. 667-674
    • Imai, H.1    Kuwayama, S.2    Onishi, A.3    Morizumi, T.4    Chisaka, O.5    Shichida, Y.6
  • 69
    • 0742305686 scopus 로고    scopus 로고
    • Vertebrate ultraviolet visual pigments: Protonation of the retinylidene Schiff base and a counterion switch during photoactivation
    • A. K. Kusnetzow A. Dukkipati K. R. Babu L. Ramos B. E. Knox R. R. Birge Vertebrate ultraviolet visual pigments: Protonation of the retinylidene Schiff base and a counterion switch during photoactivation Proc. Natl. Acad. Sci. U. S. A. 2004 101 941 946
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 941-946
    • Kusnetzow, A.K.1    Dukkipati, A.2    Babu, K.R.3    Ramos, L.4    Knox, B.E.5    Birge, R.R.6
  • 71
    • 0035923434 scopus 로고    scopus 로고
    • Regulation of phototransduction in short-wavelength cone visual pigments via the retinylidene schiff base counterion
    • DOI 10.1021/bi015584b
    • K. R. Babu A. Dukkipati R. R. Birge B. E. Knox Regulation of phototransduction in short-wavelength cone visual pigments via the retinylidene Schiff base counterion Biochemistry 2001 40 13760 13766 (Pubitemid 33078844)
    • (2001) Biochemistry , vol.40 , Issue.46 , pp. 13760-13766
    • Babu, K.R.1    Dukkipati, A.2    Birge, R.R.3    Knox, B.E.4
  • 73
    • 43749109187 scopus 로고    scopus 로고
    • Crystal structure of squid rhodopsin
    • M. Murakami T. Kouyama Crystal structure of squid rhodopsin Nature 2008 453 363 367
    • (2008) Nature , vol.453 , pp. 363-367
    • Murakami, M.1    Kouyama, T.2
  • 74
    • 75749136028 scopus 로고    scopus 로고
    • Photochemistry of visual pigment in a G(q) protein-coupled receptor (GPCR)-Insights from structural and spectral tuning studies on squid rhodopsin
    • S. Sekharan A. Altun K. Morokuma Photochemistry of visual pigment in a G(q) protein-coupled receptor (GPCR)-Insights from structural and spectral tuning studies on squid rhodopsin Chem.-Eur. J. 2010 16 1744 1749
    • (2010) Chem.-Eur. J. , vol.16 , pp. 1744-1749
    • Sekharan, S.1    Altun, A.2    Morokuma, K.3
  • 75
    • 77749267675 scopus 로고    scopus 로고
    • Drawing the retinal out of its comfort zone: An ONIOM(QM/MM) study of mutant squid rhodopsin
    • S. Sekharan K. Morokuma Drawing the retinal out of its comfort zone: An ONIOM(QM/MM) study of mutant squid rhodopsin J. Phys. Chem. Lett. 2010 1 668 672
    • (2010) J. Phys. Chem. Lett. , vol.1 , pp. 668-672
    • Sekharan, S.1    Morokuma, K.2
  • 76
    • 68949143130 scopus 로고    scopus 로고
    • The magnitude of the light-induced conformational change in different rhodopsins correlates with their ability to activate G proteins
    • H. Tsukamoto D. L. Farrens M. Koyanagi A. Terakita The magnitude of the light-induced conformational change in different rhodopsins correlates with their ability to activate G proteins J. Biol. Chem. 2009 284 20676 20683
    • (2009) J. Biol. Chem. , vol.284 , pp. 20676-20683
    • Tsukamoto, H.1    Farrens, D.L.2    Koyanagi, M.3    Terakita, A.4
  • 77
    • 42449108772 scopus 로고    scopus 로고
    • Expression and comparative characterization of Gq-coupled invertebrate visual pigments and melanopsin
    • A. Terakita H. Tsukamoto M. Koyanagi M. Sugahara T. Yamashita Y. Shichida Expression and comparative characterization of Gq-coupled invertebrate visual pigments and melanopsin J. Neurochem. 2008 105 883 890
    • (2008) J. Neurochem. , vol.105 , pp. 883-890
    • Terakita, A.1    Tsukamoto, H.2    Koyanagi, M.3    Sugahara, M.4    Yamashita, T.5    Shichida, Y.6
  • 78
    • 0030566797 scopus 로고    scopus 로고
    • Ultraviolet resonance Raman evidence for the absence of tyrosinate in octopus rhodopsin and the participation of Trp residues in the transition to acid metarhodopsin
    • S. Hashimoto H. Takeuchi M. Nakagawa M. Tsuda Ultraviolet resonance Raman evidence for the absence of tyrosinate in octopus rhodopsin and the participation of Trp residues in the transition to acid metarhodopsin FEBS Lett. 1996 398 239 242
    • (1996) FEBS Lett. , vol.398 , pp. 239-242
    • Hashimoto, S.1    Takeuchi, H.2    Nakagawa, M.3    Tsuda, M.4
  • 79
    • 0033028464 scopus 로고    scopus 로고
    • How vertebrate and invertebrate visual pigments differ in their mechanism of photoactivation
    • M. Nakagawa T. Iwasa S. Kikkawa M. Tsuda T. G. Ebrey How vertebrate and invertebrate visual pigments differ in their mechanism of photoactivation Proc. Natl. Acad. Sci. U. S. A. 1999 96 6189 6192
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 6189-6192
    • Nakagawa, M.1    Iwasa, T.2    Kikkawa, S.3    Tsuda, M.4    Ebrey, T.G.5
  • 80
    • 0000002767 scopus 로고    scopus 로고
    • Invertebrate visual pigments, in
    • D. G. Stavenga, W. J. DeGrip and E. N. Pugh Jr, Elsevier, Amsterdam, 55-90
    • W. Gärtner, Invertebrate visual pigments, in Molecular Mechanisms in Visual Transduction, ed., D. G. Stavenga, W. J. DeGrip, and, E. N. Pugh Jr, Elsevier, Amsterdam, 2000, vol. 3, ch. 7, pp. 55-90
    • (2000) Molecular Mechanisms in Visual Transduction, Ed.
    • Gärtner, W.1
  • 82
    • 4344581120 scopus 로고    scopus 로고
    • The retinal conformation and its environment in rhodopsin in light of a new 2.2 Å crystal structure
    • T. Okada M. Sugihara A. N. Bondar M. Elstner P. Entel V. Buss The retinal conformation and its environment in rhodopsin in light of a new 2.2 Å crystal structure J. Mol. Biol. 2004 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
  • 83
    • 52149109504 scopus 로고    scopus 로고
    • Gq-coupled rhodopsin subfamily composed of invertebrate visual pigment and melanopsin
    • M. Koyanagi A. Terakita Gq-coupled rhodopsin subfamily composed of invertebrate visual pigment and melanopsin Photochem. Photobiol. 2008 84 1024 1030
    • (2008) Photochem. Photobiol. , vol.84 , pp. 1024-1030
    • Koyanagi, M.1    Terakita, A.2


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