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Volumn 49, Issue 47, 2010, Pages 10089-10097

Photosensitivities of rhodopsin mutants with a displaced counterion

Author keywords

[No Author keywords available]

Indexed keywords

ABSORPTION BAND; BOVINE RHODOPSIN; COUNTERIONS; COVALENTLY BOUND; HIGH PROBABILITY; MOLAR EXTINCTION COEFFICIENT; MONOCHROMATIC LIGHT; NATURAL LIGHT; OSCILLATOR STRENGTHS; PHOTON ABSORPTIONS; PROTEIN MOIETY; SCHIFF-BASE; VISUAL PIGMENTS; WAVE NUMBERS; WILD TYPES;

EID: 78649506250     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi101020p     Document Type: Article
Times cited : (4)

References (40)
  • 2
    • 34247859268 scopus 로고    scopus 로고
    • Mechanism of G-protein activation by rhodopsin
    • Shichida, Y. and Morizumi, T. (2006) Mechanism of G-protein activation by rhodopsin Photochem. Photobiol. 83, 70-75
    • (2006) Photochem. Photobiol. , vol.83 , pp. 70-75
    • Shichida, Y.1    Morizumi, T.2
  • 3
    • 78049436281 scopus 로고    scopus 로고
    • Multiple functions of Schiff base counterion in rhodopsins
    • Tsutsui, K. and Shichida, Y. (2010) Multiple functions of Schiff base counterion in rhodopsins Photochem. Photobiol. Sci. 9, 1426-1434
    • (2010) Photochem. Photobiol. Sci. , vol.9 , pp. 1426-1434
    • Tsutsui, K.1    Shichida, Y.2
  • 4
    • 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
  • 5
    • 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
  • 6
    • 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
  • 7
    • 34249666129 scopus 로고    scopus 로고
    • Photoisomerization efficiency in UV-absorbing visual pigments: Protein-directed isomerization of an unprotonated retinal Schiff base
    • Tsutsui, K., Imai, H., and Shichida, Y. (2007) Photoisomerization efficiency in UV-absorbing visual pigments: Protein-directed isomerization of an unprotonated retinal Schiff base Biochemistry 46, 6437-6445
    • (2007) Biochemistry , vol.46 , pp. 6437-6445
    • Tsutsui, K.1    Imai, H.2    Shichida, Y.3
  • 8
    • 53749087534 scopus 로고    scopus 로고
    • E113 is required for the efficient photoisomerization of the unprotonated chromophore in a UV-absorbing visual pigment
    • Tsutsui, K., Imai, H., and Shichida, Y. (2008) E113 is required for the efficient photoisomerization of the unprotonated chromophore in a UV-absorbing visual pigment Biochemistry 47, 10829-10833
    • (2008) Biochemistry , vol.47 , pp. 10829-10833
    • Tsutsui, K.1    Imai, H.2    Shichida, Y.3
  • 10
    • 0028125886 scopus 로고
    • Rhodopsin mutation G90D and a molecular mechanism for congenital night blindness
    • Rao, V. R., Cohen, G. B., and Oprian, D. D. (1994) Rhodopsin mutation G90D and a molecular mechanism for congenital night blindness Nature 367, 639-642
    • (1994) Nature , vol.367 , pp. 639-642
    • Rao, V.R.1    Cohen, G.B.2    Oprian, D.D.3
  • 11
    • 0032943572 scopus 로고    scopus 로고
    • A novel mutation within the rhodopsin gene (Thr-94-Ile) causing autosomal dominant congenital stationary night blindness
    • al-Jandal, N., Farrar, G. J., Kiang, A. S., Humphries, M. M., Bannon, N., Findlay, J. B., Humphries, P., and Kenna, P. F. (1999) A novel mutation within the rhodopsin gene (Thr-94-Ile) causing autosomal dominant congenital stationary night blindness Hum. Mutat. 13, 75-81
    • (1999) Hum. Mutat. , vol.13 , pp. 75-81
    • Al-Jandal, N.1    Farrar, G.J.2    Kiang, A.S.3    Humphries, M.M.4    Bannon, N.5    Findlay, J.B.6    Humphries, P.7    Kenna, P.F.8
  • 12
    • 0026475571 scopus 로고
    • Changing the location of the Schiff base counterion in rhodopsin
    • Zhukovsky, E. A., Robinson, P. R., and Oprian, D. D. (1992) Changing the location of the Schiff base counterion in rhodopsin Biochemistry 31, 10400-10405
    • (1992) Biochemistry , vol.31 , pp. 10400-10405
    • Zhukovsky, E.A.1    Robinson, P.R.2    Oprian, D.D.3
  • 13
    • 0027462158 scopus 로고
    • Movement of the retinylidene Schiff base counterion in rhodopsin by one helix turn reverses the pH dependence of the metarhodopsin i to metarhodopsin II transition
    • Zvyaga, T. A., Min, K. C., Beck, M., and Sakmar, T. P. (1993) Movement of the retinylidene Schiff base counterion in rhodopsin by one helix turn reverses the pH dependence of the metarhodopsin I to metarhodopsin II transition J. Biol. Chem. 268, 4661-4667
    • (1993) J. Biol. Chem. , vol.268 , pp. 4661-4667
    • Zvyaga, T.A.1    Min, K.C.2    Beck, M.3    Sakmar, T.P.4
  • 14
    • 0027248024 scopus 로고
    • Heterozygous missense mutation in the rhodopsin gene as a cause of congenital stationary night blindness
    • Dryja, T. P., Berson, E. L., Rao, V. R., and Oprian, D. D. (1993) Heterozygous missense mutation in the rhodopsin gene as a cause of congenital stationary night blindness Nat. Genet. 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
  • 16
    • 0034089001 scopus 로고    scopus 로고
    • Analysis of amino acid residues in rhodopsin and cone visual pigments that determine their molecular properties
    • Imai, H., Terakita, A., and Shichida, Y. (2000) Analysis of amino acid residues in rhodopsin and cone visual pigments that determine their molecular properties Methods Enzymol. 315, 293-312
    • (2000) Methods Enzymol. , vol.315 , pp. 293-312
    • Imai, H.1    Terakita, A.2    Shichida, Y.3
  • 17
    • 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
  • 18
    • 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. (1988) The nature of the primary photochemical events in rhodopsin and isorhodopsin Biophys. J. 53, 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
  • 19
    • 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
  • 20
    • 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
  • 21
    • 0029972979 scopus 로고    scopus 로고
    • Characterization of the mutant visual pigment responsible for congenital night blindness: A biochemical and Fourier-transform infrared spectroscopy study
    • Zvyaga, T. A., Fahmy, K., Siebert, F., and Sakmar, T. P. (1996) Characterization of the mutant visual pigment responsible for congenital night blindness: A biochemical and Fourier-transform infrared spectroscopy study Biochemistry 35, 7536-7545
    • (1996) Biochemistry , vol.35 , pp. 7536-7545
    • Zvyaga, T.A.1    Fahmy, K.2    Siebert, F.3    Sakmar, T.P.4
  • 22
    • 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
  • 23
    • 0037743559 scopus 로고    scopus 로고
    • Opsin activation as a cause of congenital night blindness
    • Jin, S., Cornwall, M. C., and Oprian, D. D. (2003) Opsin activation as a cause of congenital night blindness Nat. Neurosci. 6, 731-735
    • (2003) Nat. Neurosci. , vol.6 , pp. 731-735
    • Jin, S.1    Cornwall, M.C.2    Oprian, D.D.3
  • 25
    • 20444371505 scopus 로고    scopus 로고
    • Breaking the covalent bond: A pigment property that contributes to desensitization in cones
    • Kefalov, V. J., Estevez, M. E., Kono, M., Goletz, P. W., Crouch, R. K., Cornwall, M. C., and Yau, K. W. (2005) Breaking the covalent bond: A pigment property that contributes to desensitization in cones Neuron 46, 879-890
    • (2005) Neuron , vol.46 , pp. 879-890
    • Kefalov, V.J.1    Estevez, M.E.2    Kono, M.3    Goletz, P.W.4    Crouch, R.K.5    Cornwall, M.C.6    Yau, K.W.7
  • 26
    • 0028128646 scopus 로고
    • Characterization of rhodopsin-transducin interaction: A mutant rhodopsin photoproduct with a protonated Schiff base activates transducin
    • Zvyaga, T. A., Fahmy, K., and Sakmar, T. P. (1994) Characterization of rhodopsin-transducin interaction: A mutant rhodopsin photoproduct with a protonated Schiff base activates transducin Biochemistry 33, 9753-9761 (Pubitemid 24272936)
    • (1994) Biochemistry , vol.33 , Issue.32 , pp. 9753-9761
    • Zvyaga, T.A.1    Fahmy, K.2    Sakmar, T.P.3
  • 27
    • 0037458628 scopus 로고    scopus 로고
    • Unusual thermal and conformational properties of the rhodopsin congenital night blindness mutant Thr-94 → Ile
    • Ramon, E., del Valle, L. J., and Garriga, P. (2003) Unusual thermal and conformational properties of the rhodopsin congenital night blindness mutant Thr-94 → Ile J. Biol. Chem. 278, 6427-6432
    • (2003) J. Biol. Chem. , vol.278 , pp. 6427-6432
    • Ramon, E.1    Del Valle, L.J.2    Garriga, P.3
  • 28
    • 0000254592 scopus 로고
    • The shape of a three-dimensional binding site of rhodopsin based on molecular modeling analysis of isomeric and other visual pigment analogs. Bioorganic studies of visual pigments. 11
    • Liu, R. S. H. and Mirzadegan, T. (1988) The shape of a three-dimensional binding site of rhodopsin based on molecular modeling analysis of isomeric and other visual pigment analogs. Bioorganic studies of visual pigments. 11 J. Am. Chem. Soc. 110, 8617-8623
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 8617-8623
    • Liu, R.S.H.1    Mirzadegan, T.2
  • 29
    • 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
  • 30
    • 0020195682 scopus 로고
    • Quantum efficiency and photosensitivity of the rhodopsin equilibrium metarhodopsin conversion in crayfish photoreceptors
    • Cronin, T. W. and Goldsmith, T. H. (1982) Quantum efficiency and photosensitivity of the rhodopsin equilibrium metarhodopsin conversion in crayfish photoreceptors Photochem. Photobiol. 36, 447-454
    • (1982) Photochem. Photobiol. , vol.36 , pp. 447-454
    • Cronin, T.W.1    Goldsmith, T.H.2
  • 31
    • 0023376803 scopus 로고
    • Quantum efficiencies of the reversible photoreaction of octopus rhodopsin
    • Dixon, S. F. and Cooper, A. (1987) Quantum efficiencies of the reversible photoreaction of octopus rhodopsin Photochem. Photobiol. 46, 115-119
    • (1987) Photochem. Photobiol. , vol.46 , pp. 115-119
    • Dixon, S.F.1    Cooper, A.2
  • 33
    • 0017253455 scopus 로고
    • Studies on cephalopod rhodopsin: Photoisomerization of the chromophore
    • Suzuki, T., Uji, K., and Kito, Y. (1976) Studies on cephalopod rhodopsin: Photoisomerization of the chromophore Biochim. Biophys. Acta 428, 321-338
    • (1976) Biochim. Biophys. Acta , vol.428 , pp. 321-338
    • Suzuki, T.1    Uji, K.2    Kito, Y.3
  • 34
    • 0018165044 scopus 로고
    • Characteristics of Drosophila rhodopsin in wild-type and norpA vision transduction mutants
    • Ostroy, S. E. (1978) Characteristics of Drosophila rhodopsin in wild-type and norpA vision transduction mutants J. Gen. Physiol. 72, 717-732
    • (1978) J. Gen. Physiol. , vol.72 , pp. 717-732
    • Ostroy, S.E.1
  • 35
    • 0005918232 scopus 로고
    • Lumi- and meta-rhodopsins of squid and octopus
    • Kropf, A., Brown, P. K., and Hubbard, R. (1959) Lumi- and meta-rhodopsins of squid and octopus Nature 183, 446-448
    • (1959) Nature , vol.183 , pp. 446-448
    • Kropf, A.1    Brown, P.K.2    Hubbard, R.3
  • 36
    • 0343553129 scopus 로고
    • Vertebrate lumi- and meta-rhodopsins
    • Hubbard, R., Brown, P. K., and Kropf, A. (1959) Vertebrate lumi- and meta-rhodopsins Nature 183, 442-446
    • (1959) Nature , vol.183 , pp. 442-446
    • Hubbard, R.1    Brown, P.K.2    Kropf, A.3
  • 37
    • 0034700314 scopus 로고    scopus 로고
    • Characterization of the primary photointermediates of Drosophila rhodopsin
    • Vought, B. W., Salcedo, E., Chadwell, L. V., Britt, S. G., Birge, R. R., and Knox, B. E. (2000) Characterization of the primary photointermediates of Drosophila rhodopsin Biochemistry 39, 14128-14137
    • (2000) Biochemistry , vol.39 , pp. 14128-14137
    • Vought, B.W.1    Salcedo, E.2    Chadwell, L.V.3    Britt, S.G.4    Birge, R.R.5    Knox, B.E.6
  • 38
    • 0033621078 scopus 로고    scopus 로고
    • Photochemistry of the primary event in short-wavelength visual opsins at low temperature
    • Vought, B. W., Dukkipatti, A., Max, M., Knox, B. E., and Birge, R. R. (1999) Photochemistry of the primary event in short-wavelength visual opsins at low temperature Biochemistry 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
  • 39
    • 43749109187 scopus 로고    scopus 로고
    • Crystal structure of squid rhodopsin
    • Murakami, M. and Kouyama, T. (2008) Crystal structure of squid rhodopsin Nature 453, 363-367
    • (2008) Nature , vol.453 , pp. 363-367
    • Murakami, M.1    Kouyama, T.2
  • 40


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