메뉴 건너뛰기




Volumn 224, Issue , 1999, Pages 102-123

Photoactivation of rhodopsin: Interplay between protein and chromophore

Author keywords

[No Author keywords available]

Indexed keywords

LIGAND; OPSIN; RETINAL; WATER;

EID: 0033250273     PISSN: None     EISSN: None     Source Type: Book Series    
DOI: None     Document Type: Article
Times cited : (6)

References (42)
  • 1
    • 0023005751 scopus 로고
    • Study of the shape of the binding site of bovine opsin using 10-substituted retinal isomers
    • Asato AE, Denny M, Matsumoto H et al 1986 Study of the shape of the binding site of bovine opsin using 10-substituted retinal isomers. Biochemistry 25:7021-7026
    • (1986) Biochemistry , vol.25 , pp. 7021-7026
    • Asato, A.E.1    Denny, M.2    Matsumoto, H.3
  • 2
    • 0001699495 scopus 로고    scopus 로고
    • Structural characterization and binding sites of G-protein-coupled receptors
    • Beck-Sickinger AG 1996 Structural characterization and binding sites of G-protein-coupled receptors. Drug Discov Today 1:502-513
    • (1996) Drug Discov Today , vol.1 , pp. 502-513
    • Beck-Sickinger, A.G.1
  • 3
    • 0012347344 scopus 로고    scopus 로고
    • Energy storage in the primary photoproduct of vision
    • Bifone A, DeGroot HJM, Buda F 1997 Energy storage in the primary photoproduct of vision. J Phys Chem B 101:2954-2958
    • (1997) J Phys Chem B , vol.101 , pp. 2954-2958
    • Bifone, A.1    DeGroot, H.J.M.2    Buda, F.3
  • 4
    • 0344972891 scopus 로고    scopus 로고
    • 13 bond of the retinal chromophore in rhodopsin - Semiempirical and nonempirical calculations of chiroptical data
    • 13 bond of the retinal chromophore in rhodopsin - semiempirical and nonempirical calculations of chiroptical data. Angew Chem Int Ed Engl 37:1893-1895
    • (1998) Angew Chem Int Ed Engl , vol.37 , pp. 1893-1895
    • Buss, V.1    Kolster, K.2    Terstegen, F.3    Vahrenhorst, R.4
  • 7
    • 0024102514 scopus 로고
    • Photoexcitation of rhodopsin: Conformation changes in the chromophore, protein and associated lipids as determined by FTIR difference spectroscopy
    • DeGrip WJ, Gray D, Gillespie J et al 1988 Photoexcitation of rhodopsin: conformation changes in the chromophore, protein and associated lipids as determined by FTIR difference spectroscopy. Photochem Photobiol 48:497-504
    • (1988) Photochem Photobiol , vol.48 , pp. 497-504
    • DeGrip, W.J.1    Gray, D.2    Gillespie, J.3
  • 8
    • 0346690458 scopus 로고
    • Structure and molecular mechanism of bovine rhodopsin: Evidence for the participation of a H-bonded network in spectral tuning and signal transduction
    • Tokunaga F (ed) The Taniguchi Foundation, Osaka, Japan
    • DeGrip WJ, DeCaluwé GLJ, Pistorius AMA et al 1993 Structure and molecular mechanism of bovine rhodopsin: evidence for the participation of a H-bonded network in spectral tuning and signal transduction. In: Tokunaga F (ed) Molecular mechanism of generation of electric signals in sensory cells. The Taniguchi Foundation, Osaka, Japan, p 26-40
    • (1993) Molecular Mechanism of Generation of Electric Signals in Sensory Cells , pp. 26-40
    • DeGrip, W.J.1    DeCaluwé, G.L.J.2    Pistorius, A.M.A.3
  • 9
    • 0032032913 scopus 로고    scopus 로고
    • Selective detergent-extraction from mixed detergent/lipid/protein micelles, using cyclodextrin inclusion compounds: A novel generic approach for the preparation of proteoliposomes
    • DeGrip WJ, VanOostrum J, Bovee-Geurts PHM 1998 Selective detergent-extraction from mixed detergent/lipid/protein micelles, using cyclodextrin inclusion compounds: a novel generic approach for the preparation of proteoliposomes. Biochem J 330:667-674
    • (1998) Biochem J , vol.330 , pp. 667-674
    • DeGrip, W.J.1    Vanoostrum, J.2    Bovee-Geurts, P.H.M.3
  • 10
    • 0032508695 scopus 로고    scopus 로고
    • Tyrosine structural changes detected during the photoactivation of rhodopsin
    • DeLange F, Klaassen CHW, Wallace-Williams SE et al 1998a Tyrosine structural changes detected during the photoactivation of rhodopsin. J Biol Chem 273:23735-23739
    • (1998) J Biol Chem , vol.273 , pp. 23735-23739
    • DeLange, F.1    Klaassen, C.H.W.2    Wallace-Williams, S.E.3
  • 11
    • 0032477819 scopus 로고    scopus 로고
    • An additional methyl group at the 10-position of retinal dramatically slows down the kinetics of the rhodopsin photocascade
    • DeLange F, Bovee-Geurts PHM, VanOostrum J et al 1998b An additional methyl group at the 10-position of retinal dramatically slows down the kinetics of the rhodopsin photocascade. Biochemistry 37:1411-1420
    • (1998) Biochemistry , vol.37 , pp. 1411-1420
    • DeLange, F.1    Bovee-Geurts, P.H.M.2    Vanoostrum, J.3
  • 12
    • 0030759375 scopus 로고    scopus 로고
    • Direct determination of a molecular torsional angle in the membrane protein rhodopsin by solid-state NMR
    • Feng XM, Verdegem PJE, Lee YK et al 1997 Direct determination of a molecular torsional angle in the membrane protein rhodopsin by solid-state NMR. J Am Chem Soc 119:6853-6857
    • (1997) J Am Chem Soc , vol.119 , pp. 6853-6857
    • Feng, X.M.1    Verdegem, P.J.E.2    Lee, Y.K.3
  • 13
    • 0024200660 scopus 로고
    • The photoreaction of vacuum-dried rhodopsin at low temperature: Evidence for charge stabilization by water
    • Ganter UM, Schmid ED, Siebert F 1988 The photoreaction of vacuum-dried rhodopsin at low temperature: evidence for charge stabilization by water. J Photochem Photobiol B Biol 2:417-426
    • (1988) J Photochem Photobiol B Biol , vol.2 , pp. 417-426
    • Ganter, U.M.1    Schmid, E.D.2    Siebert, F.3
  • 14
    • 0000116680 scopus 로고
    • Crystal structure of the visual chromophores 11-cis and all-trans retinal
    • Gilardi R, Sperling W, Karle IL, Karle J 1971 Crystal structure of the visual chromophores 11-cis and all-trans retinal. Nature 222:187-188
    • (1971) Nature , vol.222 , pp. 187-188
    • Gilardi, R.1    Sperling, W.2    Karle, I.L.3    Karle, J.4
  • 15
    • 0028916739 scopus 로고
    • NMR constraints on the location of the retinal chromophore m rhodopsin and bathorhodopsin
    • Han M, Smith SO 1995 NMR constraints on the location of the retinal chromophore m rhodopsin and bathorhodopsin. Biochemistry 34:1425-1432
    • (1995) Biochemistry , vol.34 , pp. 1425-1432
    • Han, M.1    Smith, S.O.2
  • 16
    • 0029730779 scopus 로고    scopus 로고
    • Functional interaction of transmembrane helices 3 and 6 in rhodopsin. Replacement of phenylalanine 261 by alanine causes reversion of phenotype of a glycine 121 replacement mutant
    • Han M, Lin SW, Minkova M, Smith SO, Sakmar TP 1996 Functional interaction of transmembrane helices 3 and 6 in rhodopsin. Replacement of phenylalanine 261 by alanine causes reversion of phenotype of a glycine 121 replacement mutant. J Biol Chem 271:32337-32342
    • (1996) J Biol Chem , vol.271 , pp. 32337-32342
    • Han, M.1    Lin, S.W.2    Minkova, M.3    Smith, S.O.4    Sakmar, T.P.5
  • 17
    • 0032474444 scopus 로고    scopus 로고
    • Constitutive activation of opsin by mutation of methionine 257 on transmembrane helix 6
    • Han M, Smith SO, Sakmar TP 1998 Constitutive activation of opsin by mutation of methionine 257 on transmembrane helix 6. Biochemistry 37:8253-8261
    • (1998) Biochemistry , vol.37 , pp. 8253-8261
    • Han, M.1    Smith, S.O.2    Sakmar, T.P.3
  • 18
    • 0026522293 scopus 로고
    • Rhodopsin and phototransduction: A model system for G protein-linked receptors
    • Hargrave PA, McDowell JH 1992 Rhodopsin and phototransduction: a model system for G protein-linked receptors. FASEB J 6:2323-2331
    • (1992) FASEB J , vol.6 , pp. 2323-2331
    • Hargrave, P.A.1    McDowell, J.H.2
  • 20
    • 0028559773 scopus 로고
    • Synergy in the spectral tuning of retinal pigments: Complete accounting of the opsin shift in bacteriorhodopsin
    • Hu JG, Griffin RG, Herzfeld J 1994 Synergy in the spectral tuning of retinal pigments: complete accounting of the opsin shift in bacteriorhodopsin. Proc Nad Acad Sci USA 91:8880-8884
    • (1994) Proc Nad Acad Sci USA , vol.91 , pp. 8880-8884
    • Hu, J.G.1    Griffin, R.G.2    Herzfeld, J.3
  • 21
    • 0029073041 scopus 로고
    • Histidine tagging both allows convenient single-step purification of bovine rhodopsin and exerts ionic strength-dependent effects on its photochemistry
    • Janssen JJM, Bovee-Geurts PHM, Merkx M, DeGrip WJ 1995 Histidine tagging both allows convenient single-step purification of bovine rhodopsin and exerts ionic strength-dependent effects on its photochemistry. J Biol Chem 270:11222-11229
    • (1995) J Biol Chem , vol.270 , pp. 11222-11229
    • Janssen, J.J.M.1    Bovee-Geurts, P.H.M.2    Merkx, M.3    DeGrip, W.J.4
  • 22
    • 0032003882 scopus 로고    scopus 로고
    • Deuterium substitution effect on the excited-state dynamics of rhodopsin
    • Kakitani T, Akiyama R, Hatano Y et al 1998 Deuterium substitution effect on the excited-state dynamics of rhodopsin. J Phys Chem B 102:1334-1339
    • (1998) J Phys Chem B , vol.102 , pp. 1334-1339
    • Kakitani, T.1    Akiyama, R.2    Hatano, Y.3
  • 23
    • 85005697420 scopus 로고
    • Ultrafast spectroscopy of rhodopsins - Photochemistry at its best!
    • Kochendoerfer GG, Mathies RA 1995 Ultrafast spectroscopy of rhodopsins - photochemistry at its best! Isr J Chem 35:211-226
    • (1995) Isr J Chem , vol.35 , pp. 211-226
    • Kochendoerfer, G.G.1    Mathies, R.A.2
  • 24
    • 0027365358 scopus 로고
    • Water structural changes in lumirhodopsin, metarhodopsin I, and metarhodopsin II upon photolysis of bovine rhodopsin: Analysis by Fourier transform infrared spectroscopy
    • Maeda A, Ohkita YJ, Sasaki J, Shichida Y, Yoshizawa T 1993 Water structural changes in lumirhodopsin, metarhodopsin I, and metarhodopsin II upon photolysis of bovine rhodopsin: analysis by Fourier transform infrared spectroscopy. Biochemistry 32:12033-12038
    • (1993) Biochemistry , vol.32 , pp. 12033-12038
    • Maeda, A.1    Ohkita, Y.J.2    Sasaki, J.3    Shichida, Y.4    Yoshizawa, T.5
  • 25
    • 0023097381 scopus 로고
    • 13C-NMR study of carbons C-5 and C-12 of the chromophore of bovine rhodopsin. Evidence for a 6-S-cis conformation with negative-charge perturbation near C-12
    • 13C-NMR study of carbons C-5 and C-12 of the chromophore of bovine rhodopsin. Evidence for a 6-S-cis conformation with negative-charge perturbation near C-12. Eur J Biochem 163:9-14
    • (1987) Eur J Biochem , vol.163 , pp. 9-14
    • Mollevanger, L.C.P.J.1    Kentgens, A.P.M.2    Pardoen, J.A.3
  • 27
    • 0028272258 scopus 로고
    • Rhodopsin's secondary structure revisited: Assignment of structural elements
    • Pistorius AMA, DeGrip WJ 1994 Rhodopsin's secondary structure revisited: assignment of structural elements. Biochem Biophys Res Commun 198:1040-1045
    • (1994) Biochem Biophys Res Commun , vol.198 , pp. 1040-1045
    • Pistorius, A.M.A.1    DeGrip, W.J.2
  • 28
    • 0030998038 scopus 로고    scopus 로고
    • The transmembrane 7-α-bundle of rhodopsin: Distance geometry calculations with hydrogen bonding constraints
    • Pogozheva ID, Lomize AL, Mosberg HI 1997 The transmembrane 7-α-bundle of rhodopsin: distance geometry calculations with hydrogen bonding constraints. Biophys J 72:1963-1985
    • (1997) Biophys J , vol.72 , pp. 1963-1985
    • Pogozheva, I.D.1    Lomize, A.L.2    Mosberg, H.I.3
  • 29
    • 0027364707 scopus 로고
    • Fourier transform infrared difference spectroscopy of rhodopsin mutants: Light activation of rhodopsin causes hydrogen-bonding changes in residue aspartic acid-83 during meta II formation
    • Rath P, DeCaluwé GLJ, Bovee-Geurts PHM, DeGrip WJ, Rothschild KJ 1993 Fourier transform infrared difference spectroscopy of rhodopsin mutants: light activation of rhodopsin causes hydrogen-bonding changes in residue aspartic acid-83 during meta II formation. Biochemistry 32:10277-10282
    • (1993) Biochemistry , vol.32 , pp. 10277-10282
    • Rath, P.1    DeCaluwé, G.L.J.2    Bovee-Geurts, P.H.M.3    DeGrip, W.J.4    Rothschild, K.J.5
  • 30
    • 0343177634 scopus 로고
    • Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin
    • Sakmar TP, Franke RR, Khorana HG 1989 Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin. Proc Natl Acad Sci USA 86-8309-8313
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 8309-8313
    • Sakmar, T.P.1    Franke, R.R.2    Khorana, H.G.3
  • 31
    • 0026761151 scopus 로고
    • Isolation and prominent characteristics of an L-lysine hyperproducing strain of Corynebacterium glutamicum
    • Schrumpf B, Eggeling L, Sahm H 1992 Isolation and prominent characteristics of an L-lysine hyperproducing strain of Corynebacterium glutamicum. Appl Microbiol Biotechnol 37:566-571
    • (1992) Appl Microbiol Biotechnol , vol.37 , pp. 566-571
    • Schrumpf, B.1    Eggeling, L.2    Sahm, H.3
  • 32
  • 37
    • 0014428724 scopus 로고
    • The molecular basis of visual excitation
    • Wald G 1968 The molecular basis of visual excitation. Nature 219:800-807
    • (1968) Nature , vol.219 , pp. 800-807
    • Wald, G.1
  • 38
    • 0031669472 scopus 로고    scopus 로고
    • Structure of the G-protein-coupled receptor, rhodopsin: A domain approach
    • Yeagle PL, Albert AD 1998 Structure of the G-protein-coupled receptor, rhodopsin: a domain approach. Biochem Soc Trans 26:520-531
    • (1998) Biochem Soc Trans , vol.26 , pp. 520-531
    • Yeagle, P.L.1    Albert, A.D.2
  • 39
    • 0028835362 scopus 로고
    • Amino acid replacements and wavelength absorption of visual pigments in vertebrates
    • Yokoyama S 1995 Amino acid replacements and wavelength absorption of visual pigments in vertebrates. Mol Biol Evol 12:53-61
    • (1995) Mol Biol Evol , vol.12 , pp. 53-61
    • Yokoyama, S.1
  • 40
    • 0342792386 scopus 로고    scopus 로고
    • The behaviour of visual pigments at low temperatures
    • Dartnall HJA (ed) Springer-Verlag, Berlin
    • Yoshizawa T 1972 The behaviour of visual pigments at low temperatures. In: Dartnall HJA (ed) Photochemistry of vision, vol 5. Springer-Verlag, Berlin (Handbook of sensory physiologv vol 7/1) p 146-179
    • (1972) Photochemistry of Vision , vol.5
    • Yoshizawa, T.1
  • 41
    • 0342792386 scopus 로고    scopus 로고
    • Yoshizawa T 1972 The behaviour of visual pigments at low temperatures. In: Dartnall HJA (ed) Photochemistry of vision, vol 5. Springer-Verlag, Berlin (Handbook of sensory physiologv vol 7/1) p 146-179
    • Handbook of Sensory Physiologv , vol.7 , Issue.1 , pp. 146-179
  • 42
    • 0024362631 scopus 로고
    • Effect of carboxylic acid side chains on the absorption maximum of visual pigments
    • Zhukovsky EA, Oprian DD 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.