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Volumn 66, Issue 6, 1997, Pages 741-746

Absorbance Changes by Aromatic Amino Acid Side Chains in Early Rhodopsin Photointermediates

Author keywords

[No Author keywords available]

Indexed keywords

BOVINAE;

EID: 0031301708     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1751-1097.1997.tb03218.x     Document Type: Article
Times cited : (6)

References (37)
  • 1
    • 0026091595 scopus 로고
    • The 1st step in vision - Femtosecond isomerization of rhodopsin
    • Schoenlein, R. W., L. A. Peteanu, R. A. Mathies and C. V. Shank (1991) The 1st 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
  • 3
    • 0022869494 scopus 로고
    • Primary intermediates of photobleaching of rhodopsin
    • Shichida, Y. (1986) Primary intermediates of photobleaching of rhodopsin. Photobiochem. Photobiophys. 13, 287-307.
    • (1986) Photobiochem. Photobiophys. , vol.13 , pp. 287-307
    • Shichida, Y.1
  • 4
    • 0025105229 scopus 로고
    • Nanosecond photolysis of rhodopsin: Evidence for a new, blue shifted intermediate
    • Hug, S. J., J. W. Lewis, C. M. Einterz, T. E. Thorgeirsson and D. S. Kliger (1990) Nanosecond photolysis of rhodopsin: evidence for a new, blue shifted intermediate. Biochemistry 29, 1475-1485.
    • (1990) Biochemistry , vol.29 , pp. 1475-1485
    • Hug, S.J.1    Lewis, J.W.2    Einterz, C.M.3    Thorgeirsson, T.E.4    Kliger, D.S.5
  • 7
    • 0028823469 scopus 로고
    • Structural changes in early photolysis intermediates of rhodopsin from time-resolved spectral measurements of artificial pigments sterically hindered along the chromophore chain
    • Lewis, J. W., I. Pinkas, M. Sheves, M. Ottolenghi and D. S. Kliger (1995) Structural changes in early photolysis intermediates of rhodopsin from time-resolved spectral measurements of artificial pigments sterically hindered along the chromophore chain. J. Am. Chem. Soc. 117, 918-923.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 918-923
    • Lewis, J.W.1    Pinkas, I.2    Sheves, M.3    Ottolenghi, M.4    Kliger, D.S.5
  • 8
    • 0024851737 scopus 로고
    • Transition dipole orientations in the early photolysis intermediates of rhodopsin
    • Lewis, J. W., C. M. Einterz, S. J. Hug and D. S. Kliger (1989) Transition dipole orientations in the early photolysis intermediates of rhodopsin. Biophys. J. 56, 1101-1111.
    • (1989) Biophys. J. , vol.56 , pp. 1101-1111
    • Lewis, J.W.1    Einterz, C.M.2    Hug, S.J.3    Kliger, D.S.4
  • 9
    • 0021319736 scopus 로고
    • Sensitive light scattering probe of enzymatic processes in retinal rod photoreceptor membranes
    • Lewis, J. W., J. L. Miller, L. E. Schaechter, D. S. Kliger and E. A. Dratz (1984) Sensitive light scattering probe of enzymatic processes in retinal rod photoreceptor membranes. Proc. Natl. Acad. Sci. USA 81, 743-747.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 743-747
    • Lewis, J.W.1    Miller, J.L.2    Schaechter, L.E.3    Kliger, D.S.4    Dratz, E.A.5
  • 10
    • 0001436112 scopus 로고
    • Microliter flow cell for measurements of irreversible optical absorbance transients
    • Lewis, J. W. and D. S. Kliger (1993) Microliter flow cell for measurements of irreversible optical absorbance transients. Rev. Sci. Instrum. 64, 2828-2833.
    • (1993) Rev. Sci. Instrum. , vol.64 , pp. 2828-2833
    • Lewis, J.W.1    Kliger, D.S.2
  • 11
    • 0346501208 scopus 로고
    • Photographic filter for equalizing spectral output of light sources used with optical multichannel analyzers
    • Lewis, J. W., S. J. Hug and D. S. Kliger (1987) Photographic filter for equalizing spectral output of light sources used with optical multichannel analyzers. Rev. Sci. Instrum. 58, 2342-2344.
    • (1987) Rev. Sci. Instrum. , vol.58 , pp. 2342-2344
    • Lewis, J.W.1    Hug, S.J.2    Kliger, D.S.3
  • 12
    • 0038822849 scopus 로고
    • Spectral and kinetic evidence for the existence of two forms of bathorhodopsin
    • Einterz, C. M., J. W. Lewis and D. S. Kliger (1987) Spectral and kinetic evidence for the existence of two forms of bathorhodopsin. Proc. Natl. Acad. USA 84, 3699-3703.
    • (1987) Proc. Natl. Acad. USA , vol.84 , pp. 3699-3703
    • Einterz, C.M.1    Lewis, J.W.2    Kliger, D.S.3
  • 13
    • 0016504773 scopus 로고
    • Molecular aspects of photoreceptor function
    • Ebrey, T. G. and B. Honig (1975) Molecular aspects of photoreceptor function. Q. Rev. Biophys. 8, 129-184.
    • (1975) Q. Rev. Biophys. , vol.8 , pp. 129-184
    • Ebrey, T.G.1    Honig, B.2
  • 14
    • 0019323521 scopus 로고
    • Tryptophan in bovine rhodopsin: Its content, spectral properties and environment
    • Rafferty, C. N., C. G. Mullenberg and H. Shichi (1980) Tryptophan in bovine rhodopsin: its content, spectral properties and environment. Biochemistry 19, 2145-2151.
    • (1980) Biochemistry , vol.19 , pp. 2145-2151
    • Rafferty, C.N.1    Mullenberg, C.G.2    Shichi, H.3
  • 16
    • 3242770330 scopus 로고
    • Hypochromism in polynucleotides
    • Tinoco, I., Jr. (1960) Hypochromism in polynucleotides. J. Am. Chem. Soc. 82, 4785-4790.
    • (1960) J. Am. Chem. Soc. , vol.82 , pp. 4785-4790
    • Tinoco Jr., I.1
  • 17
    • 0015369740 scopus 로고
    • Ultraviolet chromophore transitions in the rhodopsin spectrum
    • Ebrey, T. G. and B. Honig (1972) Ultraviolet chromophore transitions in the rhodopsin spectrum. Proc. Natl. Acad. Sci. USA 69, 1897-1899.
    • (1972) Proc. Natl. Acad. Sci. USA , vol.69 , pp. 1897-1899
    • Ebrey, T.G.1    Honig, B.2
  • 18
    • 0014346255 scopus 로고
    • N-retinylidene-1-amino-2-propanol: A Schiff base analog for rhodopsin
    • Erickson, J. O. and P. E. Blatz (1968) N-retinylidene-1-amino-2-propanol: a Schiff base analog for rhodopsin. Vision Res. 8, 1367-1375.
    • (1968) Vision Res. , vol.8 , pp. 1367-1375
    • Erickson, J.O.1    Blatz, P.E.2
  • 19
    • 33845378460 scopus 로고
    • Model compounds for the study of spectroscopic properties of visual pigments and bacteriorhodopsin
    • Baasov, T. and M. Sheves (1985) Model compounds for the study of spectroscopic properties of visual pigments and bacteriorhodopsin. J. Am. Chem. Soc. 107, 7524-7533.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 7524-7533
    • Baasov, T.1    Sheves, M.2
  • 20
    • 0029556994 scopus 로고
    • Projection structure of frog rhodopsin in two crystal forms
    • Schertler, G. F. and P. A. Hargrave (1995) Projection structure of frog rhodopsin in two crystal forms. Proc. Natl. Acad. Sci. USA 92, 11578-11582.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11578-11582
    • Schertler, G.F.1    Hargrave, P.A.2
  • 21
    • 0027190359 scopus 로고
    • Projection structure of rhodopsin
    • Schertler, G. F., C. Villa and R. Henderson (1993) Projection structure of rhodopsin. Nature 362, 770-772.
    • (1993) Nature , vol.362 , pp. 770-772
    • Schertler, G.F.1    Villa, C.2    Henderson, R.3
  • 22
    • 0027506471 scopus 로고
    • The probable arrangement of the helices in G protein coupled receptors
    • Baldwin, J. M. (1993) The probable arrangement of the helices in G protein coupled receptors. EMBO J. 12, 1693-1703.
    • (1993) EMBO J. , vol.12 , pp. 1693-1703
    • Baldwin, J.M.1
  • 23
    • 0028227013 scopus 로고
    • Structure and function of receptors coupled to G proteins
    • Baldwin, J. M. (1994) Structure and function of receptors coupled to G proteins. Curr. Opin. Cell Biol. 6, 180-190.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 180-190
    • Baldwin, J.M.1
  • 25
    • 0025050478 scopus 로고
    • Orientation of retinal in bovine rhodopsin determined by cross-linking using a photoactivatable analog of 11-cis-retinal
    • Nakayama, T. A. and H. G. Khorana (1990) Orientation of retinal in bovine rhodopsin determined by cross-linking using a photoactivatable analog of 11-cis-retinal. J. Biol. Chem. 265, 15762-15769.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15762-15769
    • Nakayama, T.A.1    Khorana, H.G.2
  • 26
    • 84995100934 scopus 로고
    • Light-induced perturbation of aromatic residues in bovine rhodopsin and bacteriorhodopsin
    • Rafferty, C. N. (1979) Light-induced perturbation of aromatic residues in bovine rhodopsin and bacteriorhodopsin. Photochem. Photobiol. 29, 109-120.
    • (1979) Photochem. Photobiol. , vol.29 , pp. 109-120
    • Rafferty, C.N.1
  • 27
    • 0015963426 scopus 로고
    • Effects of detergents and high pressure upon the metarhodopsin I ⇋ metarhodopsin II equilibrium
    • Lamola, A. A., T. Yamane and A. Zipp (1974) Effects of detergents and high pressure upon the metarhodopsin I ⇋ metarhodopsin II equilibrium. Biochemistry 13, 738-745.
    • (1974) Biochemistry , vol.13 , pp. 738-745
    • Lamola, A.A.1    Yamane, T.2    Zipp, A.3
  • 28
    • 0029756165 scopus 로고    scopus 로고
    • Specific tryptophan UV-absorbance changes are probes of the transition state of rhodopsin to its active state
    • Lin, S. W. and T. P. Sakmar (1996) Specific tryptophan UV-absorbance changes are probes of the transition state of rhodopsin to its active state. Biochemistry 34, 11149-11159.
    • (1996) Biochemistry , vol.34 , pp. 11149-11159
    • Lin, S.W.1    Sakmar, T.P.2
  • 29
    • 0029907599 scopus 로고    scopus 로고
    • Requirement of rigid body motion of transmembrane helices for light activation of rhodopsin
    • Farrens, D. L., C. Altenbach, K. Yang, W. L. Hubbell and H. G. Khorana (1996) Requirement of rigid body motion of transmembrane helices for light activation of rhodopsin. Science 274, 768-770.
    • (1996) Science , vol.274 , pp. 768-770
    • Farrens, D.L.1    Altenbach, C.2    Yang, K.3    Hubbell, W.L.4    Khorana, H.G.5
  • 30
    • 0029778268 scopus 로고    scopus 로고
    • Rhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F
    • Sheikh, S. P., T. A. Zvyaga, O. Lichtarge, T. P. Sakmar and H. R. Bourne (1996) Rhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F. Nature 383, 347-349.
    • (1996) Nature , vol.383 , pp. 347-349
    • Sheikh, S.P.1    Zvyaga, T.A.2    Lichtarge, O.3    Sakmar, T.P.4    Bourne, H.R.5
  • 31
    • 0023215761 scopus 로고
    • Assignment of fingerprint vibrations in the resonance Raman spectra of rhodopsin, isorhodopsin and bathorhodopsin: Implications for chromophore structure and environment
    • Palings, I., J. A. Pardoen, E. van den Berg, C. Winkel, J. Lugtenburg and R. A. Mathies (1987) Assignment of fingerprint vibrations in the resonance Raman spectra of rhodopsin, isorhodopsin and bathorhodopsin: implications for chromophore structure and environment. Biochemistry 26, 2544-2556.
    • (1987) Biochemistry , vol.26 , pp. 2544-2556
    • Palings, I.1    Pardoen, J.A.2    Van Den Berg, E.3    Winkel, C.4    Lugtenburg, J.5    Mathies, R.A.6
  • 32
    • 85005746610 scopus 로고
    • Application of FTIR spectroscopy to the investigation of dark structures and photoreactions of visual pigments
    • Siebert, F. (1995) Application of FTIR spectroscopy to the investigation of dark structures and photoreactions of visual pigments. Isr. J. Chem. 35, 309-323.
    • (1995) Isr. J. Chem. , vol.35 , pp. 309-323
    • Siebert, F.1
  • 33
    • 0028916739 scopus 로고
    • NMR constraints on the location of the retinal chromophore in rhodopsin and bathorhodopsin
    • Han, M. and S. O. Smith (1995) NMR constraints on the location of the retinal chromophore in rhodopsin and bathorhodopsin. Biochemistry 34, 1425-1432.
    • (1995) Biochemistry , vol.34 , pp. 1425-1432
    • Han, M.1    Smith, S.O.2
  • 34
  • 35
    • 0039114075 scopus 로고    scopus 로고
    • Time resolved spectroscopy of the early photolysis intermediates of rhodopsin Schiff base counterion mutants
    • Jäger, S., J. W. Lewis, T. A. Zvyaga, I. Szundi, T. P. Sakmar and D. S. Kliger (1997) Time resolved spectroscopy of the early photolysis intermediates of rhodopsin Schiff base counterion mutants. Biochemistry 36, 1999-2009.
    • (1997) Biochemistry , vol.36 , pp. 1999-2009
    • Jäger, S.1    Lewis, J.W.2    Zvyaga, T.A.3    Szundi, I.4    Sakmar, T.P.5    Kliger, D.S.6
  • 36
    • 0025044850 scopus 로고
    • The influence of the 13-methyl group of the retinal on the photoreaction of rhodopsin revealed by FTIR difference spectroscopy
    • Ganter, U. M., W. Gärtner and F. Siebert (1990) The influence of the 13-methyl group of the retinal on the photoreaction of rhodopsin revealed by FTIR difference spectroscopy. Eur. Biophvs. J. 18, 295-299.
    • (1990) Eur. Biophvs. J. , vol.18 , pp. 295-299
    • Ganter, U.M.1    Gärtner, W.2    Siebert, F.3
  • 37
    • 0001461410 scopus 로고
    • FTIR evidence for an altered chromophore-protein interaction in the artificial visual pigment cis-5,6-dihydro-isorhodopsin and its photoproducts BSI, lumirhodopsin and metarhodopsin I
    • Ganter, U. M., T. Kashima, M. Sheves and F. Siebert (1990) FTIR evidence for an altered chromophore-protein interaction in the artificial visual pigment cis-5,6-dihydro-isorhodopsin and its photoproducts BSI, lumirhodopsin and metarhodopsin I. J. Am. Chem. Soc. 113, 4087-4092.
    • (1990) J. Am. Chem. Soc. , vol.113 , pp. 4087-4092
    • Ganter, U.M.1    Kashima, T.2    Sheves, M.3    Siebert, F.4


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