메뉴 건너뛰기




Volumn 51, Issue 20, 2012, Pages 4117-4125

Rapid release of retinal from a cone visual pigment following photoactivation

Author keywords

[No Author keywords available]

Indexed keywords

ARRHENIUS ACTIVATION ENERGY; COUNTERIONS; DOUBLE MUTANTS; HOMOLOGY MODELING; KINETIC ISOTOPES; KINETIC MEASUREMENT; NONCOVALENT BINDING; PH DEPENDENCE; PH-DEPENDENT; PHOTO-ACTIVATED; PHOTOACTIVATION; PROTONATED SCHIFF BASE; RAPID RELEASE; RELEASE KINETICS; RELEASE RATE; SCHIFF-BASE; SINGLE MUTANT; TRANSMEMBRANE REGIONS; UV VISIBLE ABSORPTION SPECTRUM; VISUAL CYCLE; VISUAL PIGMENTS;

EID: 84861354678     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi201522h     Document Type: Article
Times cited : (38)

References (68)
  • 1
    • 0002846875 scopus 로고    scopus 로고
    • 1st ed. pp, Sinauer Associates, Inc. Sunderland, MA.
    • Rodieck, R. W. (1998) The First Steps in Seeing, 1st ed., pp 562, Sinauer Associates, Inc., Sunderland, MA.
    • (1998) The First Steps in Seeing , pp. 562
    • Rodieck, R.W.1
  • 2
    • 2942617209 scopus 로고    scopus 로고
    • Dark adaptation and the retinoid cycle of vision
    • Lamb, T. D. and Pugh, E. N. (2004) Dark adaptation and the retinoid cycle of vision Prog. Retinal Eye Res. 23, 307-380
    • (2004) Prog. Retinal Eye Res. , vol.23 , pp. 307-380
    • Lamb, T.D.1    Pugh, E.N.2
  • 3
    • 33846596863 scopus 로고    scopus 로고
    • Phototransduction, dark adaptation, and rhodopsin regeneration: The proctor lecture
    • Lamb, T. D. and Pugh, E. N. (2006) Phototransduction, dark adaptation, and rhodopsin regeneration: The proctor lecture Invest. Ophthalmol. Visual Sci. 47, 5137-5152
    • (2006) Invest. Ophthalmol. Visual Sci. , vol.47 , pp. 5137-5152
    • Lamb, T.D.1    Pugh, E.N.2
  • 4
    • 77956844684 scopus 로고    scopus 로고
    • Dark light, rod saturation, and the absolute and incremental sensitivity of mouse cone vision
    • Naarendorp, F., Esdaille, T. M., Banden, S. M., Andrews-Labenski, J., Gross, O. P., and Pugh, E. N. (2010) Dark light, rod saturation, and the absolute and incremental sensitivity of mouse cone vision J. Neurosci. 30, 12495-12507
    • (2010) J. Neurosci. , vol.30 , pp. 12495-12507
    • Naarendorp, F.1    Esdaille, T.M.2    Banden, S.M.3    Andrews-Labenski, J.4    Gross, O.P.5    Pugh, E.N.6
  • 6
    • 33645535034 scopus 로고    scopus 로고
    • G protein-coupled receptor rhodopsin
    • Palczewski, K. (2006) G protein-coupled receptor rhodopsin Annu. Rev. Biochem. 75, 743-767
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 743-767
    • Palczewski, K.1
  • 7
    • 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
    • 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
  • 10
    • 47049130668 scopus 로고    scopus 로고
    • Crystal structure of the ligand-free G-protein-coupled receptor opsin
    • Park, J. H., Scheerer, P., Hofmann, K. P., Choe, H.-W., and Ernst, O. P. (2008) Crystal structure of the ligand-free G-protein-coupled receptor opsin Nature 454, 183-187
    • (2008) Nature , vol.454 , pp. 183-187
    • Park, J.H.1    Scheerer, P.2    Hofmann, K.P.3    Choe, H.-W.4    Ernst, O.P.5
  • 12
    • 5044235587 scopus 로고    scopus 로고
    • Electron crystallography reveals the structure of metarhodopsin i
    • Ruprecht, J. J., Mielke, T., Vogel, R., Villa, C., and Schertler, G. F. X. (2004) Electron crystallography reveals the structure of metarhodopsin I EMBO J. 23, 3609-3620
    • (2004) EMBO J. , vol.23 , pp. 3609-3620
    • Ruprecht, J.J.1    Mielke, T.2    Vogel, R.3    Villa, C.4    Schertler, G.F.X.5
  • 13
    • 77952906089 scopus 로고    scopus 로고
    • Structure and Activation of the Visual Pigment Rhodopsin
    • Smith, S. O. (2010) Structure and Activation of the Visual Pigment Rhodopsin Annu. Rev. Biophys. 39, 1-23
    • (2010) Annu. Rev. Biophys. , vol.39 , pp. 1-23
    • Smith, S.O.1
  • 14
    • 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
  • 15
    • 27744493897 scopus 로고    scopus 로고
    • Structural observation of the primary isomerization in vision with femtosecond-stimulated Raman
    • Kukura, P., McCamant, D. W., Yoon, S., Wandschneider, D. B., and Mathies, R. A. (2005) Structural observation of the primary isomerization in vision with femtosecond-stimulated Raman Science 310, 1006-1009
    • (2005) Science , vol.310 , pp. 1006-1009
    • Kukura, P.1    McCamant, D.W.2    Yoon, S.3    Wandschneider, D.B.4    Mathies, R.A.5
  • 16
    • 0028519152 scopus 로고
    • Vibrationally coherent photochemistry in the femtosecond primary event of vision
    • Wang, Q., Schoenlein, R. W., Peteanu, L. A., Mathies, R. A., and Shank, C. V. (1994) Vibrationally coherent photochemistry in the femtosecond primary event of vision Science 266, 422-424
    • (1994) Science , vol.266 , pp. 422-424
    • Wang, Q.1    Schoenlein, R.W.2    Peteanu, L.A.3    Mathies, R.A.4    Shank, C.V.5
  • 17
    • 34250340151 scopus 로고    scopus 로고
    • Photoisomerization mechanism of rhodopsin and 9-cis-rhodopsin revealed by X-ray crystallography
    • Nakamichi, H., Buss, V., and Okada, T. (2007) Photoisomerization mechanism of rhodopsin and 9-cis-rhodopsin revealed by X-ray crystallography Biophys. J. 92, L106-L108
    • (2007) Biophys. J. , vol.92
    • Nakamichi, H.1    Buss, V.2    Okada, T.3
  • 18
    • 42449139192 scopus 로고    scopus 로고
    • Crystallizing thinking about the β2-adrenergic receptor
    • Shukla, A. K., Sun, J.-P., and Lefkowitz, R. J. (2008) Crystallizing thinking about the β2-adrenergic receptor Mol. Pharmacol. 73, 1333-1338
    • (2008) Mol. Pharmacol. , vol.73 , pp. 1333-1338
    • Shukla, A.K.1    Sun, J.-P.2    Lefkowitz, R.J.3
  • 20
  • 21
    • 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
  • 25
    • 79958711363 scopus 로고    scopus 로고
    • Activation of visual pigments by light and heat
    • Luo, D.-G., Yue, W. W. S., Ala-Laurila, P., and Yau, K.-W. (2011) Activation of visual pigments by light and heat Science 332, 1307-1312
    • (2011) Science , vol.332 , pp. 1307-1312
    • Luo, D.-G.1    Yue, W.W.S.2    Ala-Laurila, P.3    Yau, K.-W.4
  • 26
    • 0141894860 scopus 로고    scopus 로고
    • Role of visual pigment properties in rod and cone phototransduction
    • Kefalov, V., Fu, Y., Marsh-Armstrong, N., and Yau, K.-W. (2003) Role of visual pigment properties in rod and cone phototransduction Nature 425, 526-531
    • (2003) Nature , vol.425 , pp. 526-531
    • Kefalov, V.1    Fu, Y.2    Marsh-Armstrong, N.3    Yau, K.-W.4
  • 28
    • 0014411230 scopus 로고
    • Molecular basis of visual excitation
    • Wald, G. (1968) Molecular basis of visual excitation Science 162, 230-239
    • (1968) Science , vol.162 , pp. 230-239
    • Wald, G.1
  • 29
    • 0021265905 scopus 로고
    • Pathways in the hydrolysis of vertebrate rhodopsin
    • Blazynski, C. and Ostroy, S. E. (1984) Pathways in the hydrolysis of vertebrate rhodopsin Vision Res. 24, 459-470
    • (1984) Vision Res. , vol.24 , pp. 459-470
    • Blazynski, C.1    Ostroy, S.E.2
  • 32
    • 77951932145 scopus 로고    scopus 로고
    • Lessons from Photoreceptors: Turning off G-Protein Signaling in Living Cells
    • Burns, M. E. and Pugh, E. N. (2010) Lessons from Photoreceptors: Turning Off G-Protein Signaling in Living Cells Physiology 25, 72-84
    • (2010) Physiology , vol.25 , pp. 72-84
    • Burns, M.E.1    Pugh, E.N.2
  • 34
    • 25444483072 scopus 로고    scopus 로고
    • Molecular properties of rod and cone visual pigments from purified chicken cone pigments to mouse rhodopsin in situ
    • Imai, H., Kuwayama, S., Onishi, A., Morizumi, T., Chisaka, O., and Shichida, Y. (2005) Molecular properties of rod and cone visual pigments from purified chicken cone pigments to mouse rhodopsin in situ Photochem. Photobiol. Sci. 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
  • 35
    • 0025972460 scopus 로고
    • Response properties of cones from the retina of the tiger salamander
    • Perry, R. J. and McNaughton, P. A. (1991) Response properties of cones from the retina of the tiger salamander J. Physiol. 433, 561-587
    • (1991) J. Physiol. , vol.433 , pp. 561-587
    • Perry, R.J.1    McNaughton, P.A.2
  • 36
    • 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
  • 37
    • 0028027080 scopus 로고
    • Is chicken green-sensitive cone visual pigment a rhodopsin-like pigment? A comparative study of the molecular properties between chicken green and rhodopsin
    • Shichida, Y., Imai, H., Imamoto, Y., Fukada, Y., and Yoshizawa, T. (1994) Is chicken green-sensitive cone visual pigment a rhodopsin-like pigment? A comparative study of the molecular properties between chicken green and rhodopsin Biochemistry 33, 9040-9044
    • (1994) Biochemistry , vol.33 , pp. 9040-9044
    • Shichida, Y.1    Imai, H.2    Imamoto, Y.3    Fukada, Y.4    Yoshizawa, T.5
  • 38
    • 0035923434 scopus 로고    scopus 로고
    • Regulation of phototransduction in short-wavelength cone visual pigments via the retinylidene Schiff base counterion
    • Babu, K. R., Dukkipati, A., Birge, R. R., and Knox, B. E. (2001) Regulation of phototransduction in short-wavelength cone visual pigments via the retinylidene Schiff base counterion Biochemistry 40, 13760-13766
    • (2001) Biochemistry , vol.40 , pp. 13760-13766
    • Babu, K.R.1    Dukkipati, A.2    Birge, R.R.3    Knox, B.E.4
  • 39
    • 0742305686 scopus 로고    scopus 로고
    • Vertebrate ultraviolet visual pigments: Protonation of the retinylidene Schiff base and a counterion switch during photoactivation
    • Kusnetzow, A. K., Dukkipati, A., Babu, K. R., Ramos, L., Knox, B. E., and Birge, R. R. (2004) Vertebrate ultraviolet visual pigments: protonation of the retinylidene Schiff base and a counterion switch during photoactivation Proc. Natl. Acad. Sci. U.S.A. 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
  • 40
    • 0037168497 scopus 로고    scopus 로고
    • Conserved proline residue at position 189 in cone visual pigments as a determinant of molecular properties different from rhodopsins
    • Kuwayama, S., Imai, H., Hirano, T., Terakita, A., and Shichida, Y. (2002) Conserved proline residue at position 189 in cone visual pigments as a determinant of molecular properties different from rhodopsins Biochemistry 41, 15245-15252
    • (2002) Biochemistry , vol.41 , pp. 15245-15252
    • Kuwayama, S.1    Imai, H.2    Hirano, T.3    Terakita, A.4    Shichida, Y.5
  • 41
    • 0028957661 scopus 로고
    • Structure and function in rhodopsin. Measurement of the rate of metarhodopsin II decay by fluorescence spectroscopy
    • Farrens, D. L. and Khorana, H. G. (1995) Structure and function in rhodopsin. Measurement of the rate of metarhodopsin II decay by fluorescence spectroscopy J. Biol. Chem. 270, 5073-5076
    • (1995) J. Biol. Chem. , vol.270 , pp. 5073-5076
    • Farrens, D.L.1    Khorana, H.G.2
  • 42
    • 0038037706 scopus 로고    scopus 로고
    • Stability of dark state rhodopsin is mediated by a conserved ion pair in intradiscal loop E-2
    • Janz, J. M., Fay, J. F., and Farrens, D. L. (2003) Stability of dark state rhodopsin is mediated by a conserved ion pair in intradiscal loop E-2 J. Biol. Chem. 278, 16982-16991
    • (2003) J. Biol. Chem. , vol.278 , pp. 16982-16991
    • Janz, J.M.1    Fay, J.F.2    Farrens, D.L.3
  • 44
    • 79952255473 scopus 로고    scopus 로고
    • Glutamic Acid 181 Is Negatively Charged in the Bathorhodopsin Photointermediate of Visual Rhodopsin
    • Sandberg, M. N., Amora, T. L., Ramos, L. S., Chen, M.-H., Knox, B. E., and Birge, R. R. (2011) Glutamic Acid 181 Is Negatively Charged in the Bathorhodopsin Photointermediate of Visual Rhodopsin J. Am. Chem. Soc. 133, 2808-2811
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 2808-2811
    • Sandberg, M.N.1    Amora, T.L.2    Ramos, L.S.3    Chen, M.-H.4    Knox, B.E.5    Birge, R.R.6
  • 45
    • 34248193896 scopus 로고    scopus 로고
    • Regulation of photoactivation in vertebrate short wavelength visual pigments: Protonation of the retinylidene Schiff base and a counterion switch
    • Ramos, L. S., Chen, M.-H., Knox, B. E., and Birge, R. R. (2007) Regulation of photoactivation in vertebrate short wavelength visual pigments: Protonation of the retinylidene Schiff base and a counterion switch Biochemistry 46, 5330-5340
    • (2007) Biochemistry , vol.46 , pp. 5330-5340
    • Ramos, L.S.1    Chen, M.-H.2    Knox, B.E.3    Birge, R.R.4
  • 46
    • 0032144874 scopus 로고    scopus 로고
    • Cloning and expression of a Xenopus short wavelength cone pigment
    • Starace, D. M. and Knox, B. E. (1998) Cloning and expression of a Xenopus short wavelength cone pigment Exp. Eye Res. 67, 209-220
    • (1998) Exp. Eye Res. , vol.67 , pp. 209-220
    • Starace, D.M.1    Knox, B.E.2
  • 47
    • 0031031146 scopus 로고    scopus 로고
    • Activation of transducin by a Xenopus short wavelength visual pigment
    • Starace, D. M. and Knox, B. E. (1997) Activation of transducin by a Xenopus short wavelength visual pigment J. Biol. Chem. 272, 1095-1100
    • (1997) J. Biol. Chem. , vol.272 , pp. 1095-1100
    • Starace, D.M.1    Knox, B.E.2
  • 48
    • 0035909830 scopus 로고    scopus 로고
    • Serine 85 in Transmembrane Helix 2 of Short-Wavelength Visual Pigments Interacts with the Retinylidene Schiff Base Counterion
    • Dukkipati, A., Vought, B. W., Singh, D., Birge, R. R., and Knox, B. E. (2001) Serine 85 in Transmembrane Helix 2 of Short-Wavelength Visual Pigments Interacts with the Retinylidene Schiff Base Counterion Biochemistry 40, 15098-15108
    • (2001) Biochemistry , vol.40 , pp. 15098-15108
    • Dukkipati, A.1    Vought, B.W.2    Singh, D.3    Birge, R.R.4    Knox, B.E.5
  • 49
    • 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
  • 50
    • 0028128646 scopus 로고
    • Characterization of rhodopsin-transducin interaction: A mutant rhodopsin photoproduct with a protonated Schiff base activates transducin
    • Zvyaga, T., Fahmy, K., and Sakmar, T. (1994) Characterization of rhodopsin-transducin interaction: A mutant rhodopsin photoproduct with a protonated Schiff base activates transducin Biochemistry 33, 9753-9761
    • (1994) Biochemistry , vol.33 , pp. 9753-9761
    • Zvyaga, T.1    Fahmy, K.2    Sakmar, T.3
  • 51
    • 0017171319 scopus 로고
    • Visual-pigment spectra: Implications of the protonation of the retinal Schiff base
    • Honig, B., Greenberg, A., Dinur, U., and Ebrey, T. (1976) Visual-pigment spectra: Implications of the protonation of the retinal Schiff base Biochemistry 15, 4593-4599
    • (1976) Biochemistry , vol.15 , pp. 4593-4599
    • Honig, B.1    Greenberg, A.2    Dinur, U.3    Ebrey, T.4
  • 52
    • 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
  • 53
    • 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
  • 54
    • 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
  • 55
    • 33645019091 scopus 로고    scopus 로고
    • Late stages of visual pigment photolysis in situ: Cones vs. rods
    • Golobokova, E. Y. and Govardovskii, V. I. (2006) Late stages of visual pigment photolysis in situ: Cones vs. rods Vision Res. 46, 2287-2297
    • (2006) Vision Res. , vol.46 , pp. 2287-2297
    • Golobokova, E.Y.1    Govardovskii, V.I.2
  • 58
    • 0029128883 scopus 로고
    • Difference in molecular properties between chicken green and rhodopsin as related to the functional difference between cone and rod photoreceptor cells
    • Imai, H., Imamoto, Y., Yoshizawa, T., and Shichida, Y. (1995) Difference in molecular properties between chicken green and rhodopsin as related to the functional difference between cone and rod photoreceptor cells Biochemistry 34, 10525-10531
    • (1995) Biochemistry , vol.34 , pp. 10525-10531
    • Imai, H.1    Imamoto, Y.2    Yoshizawa, T.3    Shichida, Y.4
  • 59
    • 84944496908 scopus 로고
    • Rod/cone rivalry in pigment regeneration
    • Rushton, W. A. (1968) Rod/cone rivalry in pigment regeneration J. Physiol. 198, 219-236
    • (1968) J. Physiol. , vol.198 , pp. 219-236
    • Rushton, W.A.1
  • 60
    • 0001448722 scopus 로고
    • Mechanism of retinal Schiff base formation and hydrolysis in relation to visual pigment photolysis and regeneration: Resonance Raman spectroscopy of a tetrahedral carbinolamine intermediate and oxygen-18 labeling of retinal at the metarhodopsin stage in photoreceptor membranes
    • Cooper, A., Dixon, S., Nutley, M., and Robb, J. (1987) Mechanism of retinal Schiff base formation and hydrolysis in relation to visual pigment photolysis and regeneration: Resonance Raman spectroscopy of a tetrahedral carbinolamine intermediate and oxygen-18 labeling of retinal at the metarhodopsin stage in photoreceptor membranes J. Am. Chem. Soc. 109, 7254-7263
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 7254-7263
    • Cooper, A.1    Dixon, S.2    Nutley, M.3    Robb, J.4
  • 62
    • 3242687856 scopus 로고    scopus 로고
    • Formation of Meta III during the decay of activated rhodopsin proceeds via Meta i and not via Meta II
    • Vogel, R., Siebert, F., Zhang, X.-Y., Fan, G., and Sheves, M. (2004) Formation of Meta III during the decay of activated rhodopsin proceeds via Meta I and not via Meta II Biochemistry 43, 9457-9466
    • (2004) Biochemistry , vol.43 , pp. 9457-9466
    • Vogel, R.1    Siebert, F.2    Zhang, X.-Y.3    Fan, G.4    Sheves, M.5
  • 63
    • 11244264401 scopus 로고    scopus 로고
    • Role of the retinal hydrogen bond network in rhodopsin Schiff base stability and hydrolysis
    • Janz, J. M. and Farrens, D. L. (2004) Role of the retinal hydrogen bond network in rhodopsin Schiff base stability and hydrolysis J. Biol. Chem. 279, 55886-55894
    • (2004) J. Biol. Chem. , vol.279 , pp. 55886-55894
    • Janz, J.M.1    Farrens, D.L.2
  • 64
    • 0016289846 scopus 로고
    • Resonance Raman spectroscopy of rhodopsin in retinal disk membranes
    • Oseroff, A. R. and Callendar, 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    Callendar, R.H.2
  • 65
    • 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
  • 66
    • 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
  • 67
    • 0242494305 scopus 로고    scopus 로고
    • Assessing structural elements that influence Schiff base stability: Mutants E113Q and D190N destabilize rhodopsin through different mechanisms
    • Janz, J. M. and Farrens, D. L. (2003) Assessing structural elements that influence Schiff base stability: Mutants E113Q and D190N destabilize rhodopsin through different mechanisms Vision Res. 43, 2991-3002
    • (2003) Vision Res. , vol.43 , pp. 2991-3002
    • Janz, J.M.1    Farrens, D.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.