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Volumn 43, Issue 31, 2004, Pages 10255-10264

Photoreactions of Metarhodopsin III

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ENERGY; CHROMOPHORES; FOURIER TRANSFORM INFRARED SPECTROSCOPY; ISOMERIZATION; PHOTOCHEMICAL REACTIONS;

EID: 3543078041     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049182q     Document Type: Article
Times cited : (12)

References (36)
  • 1
    • 0034784920 scopus 로고    scopus 로고
    • Rhodopsin: Structural basis of molecular physiology
    • Menon, S. T., Han, M., and Sakmar, T. P. (2001) Rhodopsin: structural basis of molecular physiology, Physiol. Rev. 81, 1659-1688.
    • (2001) Physiol. Rev. , vol.81 , pp. 1659-1688
    • Menon, S.T.1    Han, M.2    Sakmar, T.P.3
  • 2
    • 0032412196 scopus 로고    scopus 로고
    • Visual pigment: G-protein-coupled receptor for light signals
    • Shichida, Y., and Imai, H. (1998) Visual pigment: G-protein-coupled receptor for light signals, Cell. Mol. Life Sci. 54, 1299-1315.
    • (1998) Cell. Mol. Life Sci. , vol.54 , pp. 1299-1315
    • Shichida, Y.1    Imai, H.2
  • 3
    • 0022869897 scopus 로고
    • Photoproducts of rhodopsin in the disc membrane
    • Hofmann, K. P. (1986) Photoproducts of rhodopsin in the disc membrane, Photobiochem. Photobiophys. 13, 309-327.
    • (1986) Photobiochem. Photobiophys. , vol.13 , pp. 309-327
    • Hofmann, K.P.1
  • 5
    • 0042473251 scopus 로고    scopus 로고
    • Deactivation of rhodopsin in the transition from the signaling state Meta II to Meta III involves a thermal isomerization of the retinal chromophore C=N double bond
    • Vogel, R., Siebert, F., Mathias, G., Tavan, P., Fan, G. B., and Sheves, M. (2003) Deactivation of rhodopsin in the transition from the signaling state Meta II to Meta III involves a thermal isomerization of the retinal chromophore C=N double bond, Biochemistry 42, 9863-9874.
    • (2003) Biochemistry , vol.42 , pp. 9863-9874
    • Vogel, R.1    Siebert, F.2    Mathias, G.3    Tavan, P.4    Fan, G.B.5    Sheves, M.6
  • 6
    • 3242687856 scopus 로고    scopus 로고
    • Formation of Meta III during the decay of activated rhodopsin proceeds via Meta I and not via Meta II
    • in press
    • Vogel, R., Siebert, F., Zhang, X. Y., Fan, G. B., and Sheves, M. (2004) Formation of Meta III during the decay of activated rhodopsin proceeds via Meta I and not via Meta II, Biochemistry, in press.
    • (2004) Biochemistry
    • Vogel, R.1    Siebert, F.2    Zhang, X.Y.3    Fan, G.B.4    Sheves, M.5
  • 8
    • 0038729667 scopus 로고    scopus 로고
    • Signaling states of rhodopsin. Formation of the storage form, metarhodopsin III, from active metarhodopsin II
    • Heck, M., Schädel, S. A., Maretzki, D., Bartl, F. J., Ritter, E., Palczewski, K., and Hofmann, K. P. (2003) Signaling states of rhodopsin. Formation of the storage form, metarhodopsin III, from active metarhodopsin II, J. Biol. Chem. 278, 3162-3169.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3162-3169
    • Heck, M.1    Schädel, S.A.2    Maretzki, D.3    Bartl, F.J.4    Ritter, E.5    Palczewski, K.6    Hofmann, K.P.7
  • 9
    • 0031017636 scopus 로고    scopus 로고
    • Metarhodopsin III formation and decay kinetics: Comparison of bovine and human rhodopsin
    • Lewis, J. W., van Kuijk, F. J., Carruthers, J. A., and Kliger, D. S. (1997) Metarhodopsin III formation and decay kinetics: comparison of bovine and human rhodopsin, Vision Res. 37, 1-8.
    • (1997) Vision Res. , vol.37 , pp. 1-8
    • Lewis, J.W.1    Van Kuijk, F.J.2    Carruthers, J.A.3    Kliger, D.S.4
  • 10
    • 0018320164 scopus 로고
    • The orientation of the chromophore of vertebrate rhodopsin in the "Meta" intermediate states and the reversibility of the Meta II-Meta III transition
    • Chabre, M., and Breton, J. (1979) The orientation of the chromophore of vertebrate rhodopsin in the "Meta" intermediate states and the reversibility of the Meta II-Meta III transition, Vision Res. 19, 1005-1018.
    • (1979) Vision Res. , vol.19 , pp. 1005-1018
    • Chabre, M.1    Breton, J.2
  • 11
    • 0025823575 scopus 로고
    • Functional equivalence of metarhodopsin II and the Gt-activating form of photolyzed bovine rhodopsin
    • Kibelbek, J., Mitchell, D. C., Beach, J. M., and Litman, B. J. (1991) Functional equivalence of metarhodopsin II and the Gt-activating form of photolyzed bovine rhodopsin, Biochemistry 30, 6761-6768.
    • (1991) Biochemistry , vol.30 , pp. 6761-6768
    • Kibelbek, J.1    Mitchell, D.C.2    Beach, J.M.3    Litman, B.J.4
  • 12
    • 0035839574 scopus 로고    scopus 로고
    • Signaling states of rhodopsin: Absorption of light in active Metarhodopsin II generates an all-trans-retinal bound inactive state
    • Bartl, F. J., Ritter, E., and Hofmann, K. P. (2001) Signaling states of rhodopsin: absorption of light in active Metarhodopsin II generates an all-trans-retinal bound inactive state, J. Biol. Chem. 276, 30161-30166.
    • (2001) J. Biol. Chem. , vol.276 , pp. 30161-30166
    • Bartl, F.J.1    Ritter, E.2    Hofmann, K.P.3
  • 13
    • 0017182530 scopus 로고
    • Photoregeneration of rhodopsin and isorhodopsin from metarhodopsin III in the frog retina
    • Reuter, T. (1976) Photoregeneration of rhodopsin and isorhodopsin from metarhodopsin III in the frog retina, Vision Res. 16, 909-917.
    • (1976) Vision Res. , vol.16 , pp. 909-917
    • Reuter, T.1
  • 14
    • 0014007859 scopus 로고
    • Protein configuration changes in the photolysis of rhodopsin. II. The sequence of intermediates in thermal decay of cattle metarhodopsin in vitro
    • Ostroy, S. E., Erhardt, F., and Abrahamson, E. W. (1966) Protein configuration changes in the photolysis of rhodopsin. II. The sequence of intermediates in thermal decay of cattle metarhodopsin in vitro, Biochim. Biophys. Acta 112, 265-277.
    • (1966) Biochim. Biophys. Acta , vol.112 , pp. 265-277
    • Ostroy, S.E.1    Erhardt, F.2    Abrahamson, E.W.3
  • 15
    • 0037729260 scopus 로고    scopus 로고
    • New insights from FTIR spectroscopy into molecular properties and activation mechanisms of the visual pigment rhodopsin
    • Vogel, R., and Siebert, F. (2003) New insights from FTIR spectroscopy into molecular properties and activation mechanisms of the visual pigment rhodopsin, Biospectroscopy 72, 133-148.
    • (2003) Biospectroscopy , vol.72 , pp. 133-148
    • Vogel, R.1    Siebert, F.2
  • 16
    • 0020020855 scopus 로고
    • Preparation of retinal rod outer segments
    • Papermaster, D. S. (1982) Preparation of retinal rod outer segments, Methods Enzymol. 81, 48-52.
    • (1982) Methods Enzymol. , vol.81 , pp. 48-52
    • Papermaster, D.S.1
  • 17
    • 0035914463 scopus 로고    scopus 로고
    • Conformations of the active and inactive states of opsin
    • Vogel, R., and Siebert, F. (2001) Conformations of the active and inactive states of opsin, J. Biol. Chem. 276, 38487-38493.
    • (2001) J. Biol. Chem. , vol.276 , pp. 38487-38493
    • Vogel, R.1    Siebert, F.2
  • 18
    • 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
  • 19
    • 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., Pardoen, J. A., van den Berg, E. M., Winkel, C., Lugtenburg, J., and Mathies, R. A. (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.M.3    Winkel, C.4    Lugtenburg, J.5    Mathies, R.A.6
  • 20
    • 0020603954 scopus 로고
    • Fourier transform infrared spectroscopy applied to rhodopsin. The problem of the protonation state of the retinylidene Schiff base re-investigated
    • Siebert, F., Mäntele, W., and Gerwert, K. (1983) Fourier transform infrared spectroscopy applied to rhodopsin. The problem of the protonation state of the retinylidene Schiff base re-investigated, Eur. J. Biochem. 136, 119-127.
    • (1983) Eur. J. Biochem. , vol.136 , pp. 119-127
    • Siebert, F.1    Mäntele, W.2    Gerwert, K.3
  • 21
    • 0001649232 scopus 로고    scopus 로고
    • a control of the retinal Schiff base: A density functional study
    • a control of the retinal Schiff base: A density functional study, J. Phys. Chem. B 103, 4518-4527.
    • (1999) J. Phys. Chem. B , vol.103 , pp. 4518-4527
    • Tajkhorshid, E.1    Paizs, B.2    Suhai, S.3
  • 22
    • 0021744582 scopus 로고
    • Factors affecting the rate of thermal isomerization of 13-cis-bacteriorhodopsin to all-trans
    • Sheves, M., and Baasov, T. (1984) Factors affecting the rate of thermal isomerization of 13-cis-bacteriorhodopsin to all-trans, J. Am. Chem. Soc. 106, 6840-6841.
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 6840-6841
    • Sheves, M.1    Baasov, T.2
  • 24
    • 0024293241 scopus 로고
    • Rhodopsin-lumirhodopsin phototransition of bovine rhodopsin investigated by Fourier transform infrared difference spectroscopy
    • Ganter, U. M., Gärtner, W., and Siebert, F. (1988) Rhodopsin-lumirhodopsin phototransition of bovine rhodopsin investigated by Fourier transform infrared difference spectroscopy, Biochemistry 27, 7480-7488.
    • (1988) Biochemistry , vol.27 , pp. 7480-7488
    • Ganter, U.M.1    Gärtner, W.2    Siebert, F.3
  • 25
    • 0021758996 scopus 로고
    • Temperature and pH dependence of the Metarhodopsin I - Metarhodopsin II kinetics and equilibria in bovine rod disk membrane suspensions
    • Parkes, J. H., and Liebman, P. A. (1984) Temperature and pH dependence of the Metarhodopsin I - Metarhodopsin II kinetics and equilibria in bovine rod disk membrane suspensions, Biochemistry 23, 5054-5061.
    • (1984) Biochemistry , vol.23 , pp. 5054-5061
    • Parkes, J.H.1    Liebman, P.A.2
  • 26
    • 0038116670 scopus 로고    scopus 로고
    • Structural changes in lumirhodopsin and metarhodopsin I studied by their photoreactions at 77 K
    • Furutani, Y., Kandori, H., and Shichida, Y. (2003) Structural changes in lumirhodopsin and metarhodopsin I studied by their photoreactions at 77 K, Biochemistry 42, 8494-8500.
    • (2003) Biochemistry , vol.42 , pp. 8494-8500
    • Furutani, Y.1    Kandori, H.2    Shichida, Y.3
  • 27
    • 3543121594 scopus 로고    scopus 로고
    • Isomerization around a C=N double bond and a C=C double bond with a nitrogen atom attached: Thermal and photochemical routes
    • Zilberg, S., and Haas, Y. (2003) Isomerization around a C=N double bond and a C=C double bond with a nitrogen atom attached: thermal and photochemical routes, Photochem. Photobiol. Sci. 2, 1256-1263.
    • (2003) Photochem. Photobiol. Sci. , vol.2 , pp. 1256-1263
    • Zilberg, S.1    Haas, Y.2
  • 28
    • 0014397673 scopus 로고
    • Photolysis of metarhodopsin II. Rates of production of P470 and rhodopsin
    • Williams, T. P. (1968) Photolysis of metarhodopsin II. Rates of production of P470 and rhodopsin, Vision Res. 8, 1457-1466.
    • (1968) Vision Res. , vol.8 , pp. 1457-1466
    • Williams, T.P.1
  • 29
    • 0017770143 scopus 로고
    • Temperature and wavelength effects on the photochemistry of rhodopsin, isorhodopsin, bacteriorhodopsin and their photoproducts
    • Hurley, J. B., Ebrey, T. G., Honig, B., and Ottolenghi, M. (1977) Temperature and wavelength effects on the photochemistry of rhodopsin, isorhodopsin, bacteriorhodopsin and their photoproducts, Nature 270, 540-542.
    • (1977) Nature , vol.270 , pp. 540-542
    • Hurley, J.B.1    Ebrey, T.G.2    Honig, B.3    Ottolenghi, M.4
  • 30
    • 33751384971 scopus 로고
    • Femtosecond dynamics of cis-trans isomerizatino in a visual pigment analogue - Isorhodopsin
    • Schoenlein, R. W., Peteanu, L. A., Wang, Q., Mathies, R. A., and Shank, C. V. (1993) Femtosecond dynamics of cis-trans isomerizatino in a visual pigment analogue - isorhodopsin, J. Phys. Chem. 97, 12087-12092.
    • (1993) J. Phys. Chem. , vol.97 , pp. 12087-12092
    • Schoenlein, R.W.1    Peteanu, L.A.2    Wang, Q.3    Mathies, R.A.4    Shank, C.V.5
  • 31
    • 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
  • 32
    • 85005688720 scopus 로고
    • The photocycles of bacteriorhodopsin
    • Lanyi, J. K., and Váró, G. (1995) The photocycles of bacteriorhodopsin, Isr. J. Chem. 35, 365-385.
    • (1995) Isr. J. Chem. , vol.35 , pp. 365-385
    • Lanyi, J.K.1    Váró, G.2
  • 33
    • 0026577708 scopus 로고
    • Temperature and pH sensitivity of the O-640 intermediate of the bacteriorhodopsin photocycle
    • Chizhov, I., Engelhard, M., Chernavskii, D. S., Zubov, B., and Hess, B. (1992) Temperature and pH sensitivity of the O-640 intermediate of the bacteriorhodopsin photocycle, Biophys. J. 61, 1001-1006.
    • (1992) Biophys. J. , vol.61 , pp. 1001-1006
    • Chizhov, I.1    Engelhard, M.2    Chernavskii, D.S.3    Zubov, B.4    Hess, B.5
  • 34
    • 0028793135 scopus 로고
    • Molecular mechanism of protein-retinal coupling in bacteriorhodopsin
    • Delaney, J. K., Schweiger, U., and Subramaniam, S. (1995) Molecular mechanism of protein-retinal coupling in bacteriorhodopsin, Proc. Natl. Acad. Sci. U.S.A. 92, 11120-11124.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 11120-11124
    • Delaney, J.K.1    Schweiger, U.2    Subramaniam, S.3
  • 35
    • 17444451108 scopus 로고    scopus 로고
    • Photoexcitation of the O-intermediate in bacteriorhodopsin mutant L93A
    • Tóth-Boconádi, R., Keszthelyi, L., and Stoeckenius, W. (2003) Photoexcitation of the O-intermediate in bacteriorhodopsin mutant L93A, Biophys. J. 84, 3857-3863.
    • (2003) Biophys. J. , vol.84 , pp. 3857-3863
    • Tóth-Boconádi, R.1    Keszthelyi, L.2    Stoeckenius, W.3
  • 36
    • 0035818444 scopus 로고    scopus 로고
    • Anions stabilize a Metarhodopsin II-like photoproduct with a protonated Schiff base
    • Vogel, R., Fan, G. B., Siebert, F., and Sheves, M. (2001) Anions stabilize a Metarhodopsin II-like photoproduct with a protonated Schiff base, Biochemistry 40, 13342-13352.
    • (2001) Biochemistry , vol.40 , pp. 13342-13352
    • Vogel, R.1    Fan, G.B.2    Siebert, F.3    Sheves, M.4


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