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Volumn 8, Issue 2, 2003, Pages 285-296

Visual and archaeal rhodopsins: Similarities, differences and controversy

Author keywords

Bacteriorhodopsin; Primary Processes; Rhodopsin

Indexed keywords

BACTERIORHODOPSIN; CHLORIDE ION; HALORHODOPSIN; PROTON PUMP; RHODOPSIN; SENSORY RHODOPSIN;

EID: 0037929682     PISSN: 14258153     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (6)

References (41)
  • 2
    • 0032437382 scopus 로고    scopus 로고
    • Bacteriorhodopsin
    • Lanyi, J.K. Bacteriorhodopsin. Int. Rev. Cytology 187 (1999) 161-202.
    • (1999) Int. Rev. Cytology , vol.187 , pp. 161-202
    • Lanyi, J.K.1
  • 3
    • 0032510480 scopus 로고    scopus 로고
    • A cold break for photoreceptors
    • Essen, L.-O. and Oesterhelt, D. A cold break for photoreceptors. Nature 392 (1998) 131-133.
    • (1998) Nature , vol.392 , pp. 131-133
    • Essen, L.-O.1    Oesterhelt, D.2
  • 4
    • 0025829307 scopus 로고
    • From femtoseconds to biology: Mechanism of bacteriorhodopsin's light-driven proton pump
    • Mathies, R.A., Lin, S.W., Ames, J.B. and Pollard, W.T. From femtoseconds to biology: Mechanism of bacteriorhodopsin's light-driven proton pump. Annu. Rev. Biophys. Biophys. Chem. 20 (1991) 491-518.
    • (1991) Annu. Rev. Biophys. Biophys. Chem. , vol.20 , pp. 491-518
    • Mathies, R.A.1    Lin, S.W.2    Ames, J.B.3    Pollard, W.T.4
  • 5
    • 0036708439 scopus 로고    scopus 로고
    • Structural changes during the formation of early intermediates in the bacteriorhodopsin photocycle
    • Hayashi, S., Tajkhorshid, E. and Schulten, K. Structural changes during the formation of early intermediates in the bacteriorhodopsin photocycle. Biophys. J. 83 (2002) 1281-1297.
    • (2002) Biophys. J. , vol.83 , pp. 1281-1297
    • Hayashi, S.1    Tajkhorshid, E.2    Schulten, K.3
  • 6
    • 0001604008 scopus 로고
    • The dynamics of the primary event in rhodopsins revisited
    • Warshel, A., Chu, Z.T. and Hwang, J.-K. The dynamics of the primary event in rhodopsins revisited. Chem. Phys. 158 (1991) 303-314.
    • (1991) Chem. Phys. , vol.158 , pp. 303-314
    • Warshel, A.1    Chu, Z.T.2    Hwang, J.-K.3
  • 7
    • 0029086923 scopus 로고
    • Bacteriorhodopsin a paradigm for proton pumps?
    • Lanyi, J.K. Bacteriorhodopsin: a paradigm for proton pumps? Biophys. Chem. 56 (1995) 143-151.
    • (1995) Biophys. Chem. , vol.56 , pp. 143-151
    • Lanyi, J.K.1
  • 8
    • 0024279842 scopus 로고
    • Direct observation of the femtosecond excited-state cis-trans isomerization in bacteriorhodopsin
    • Mathies, R.A., Cruz, C.H.B., Pollard, W.T. and Shank, Ch.V. Direct observation of the femtosecond excited-state cis-trans isomerization in bacteriorhodopsin. Science 24 (1988) 777-779.
    • (1988) Science , vol.24 , pp. 777-779
    • Mathies, R.A.1    Cruz, C.H.B.2    Pollard, W.T.3    Shank, Ch.V.4
  • 9
    • 0001051029 scopus 로고    scopus 로고
    • Vibrational spectrum of the J-625 intermediate in the room temperature bacteriorhodopsin photocycle
    • Atkinson, G.H., Ujj, L. and Zhou, Y. Vibrational spectrum of the J-625 intermediate in the room temperature bacteriorhodopsin photocycle. J. Phys. Chem. A 104 (2000) 4130-4139.
    • (2000) J. Phys. Chem. A , vol.104 , pp. 4130-4139
    • Atkinson, G.H.1    Ujj, L.2    Zhou, Y.3
  • 10
    • 0037008526 scopus 로고    scopus 로고
    • Femtosecond infrared spectroscopy of bacteriorhodopsin chromophore isomerization
    • Herbst, J., Heyne, K. and Diller, R. Femtosecond infrared spectroscopy of bacteriorhodopsin chromophore isomerization. Science 297 (2002) 822-825.
    • (2002) Science , vol.297 , pp. 822-825
    • Herbst, J.1    Heyne, K.2    Diller, R.3
  • 11
    • 0001604008 scopus 로고
    • The dynamics of the primary event in rhodopsins revisited
    • Warshel, A., Chu, Z.T. and Hwang, J.-K. The dynamics of the primary event in rhodopsins revisited. Chem. Phys. 158 (1991) 303-314.
    • (1991) Chem. Phys. , vol.158 , pp. 303-314
    • Warshel, A.1    Chu, Z.T.2    Hwang, J.-K.3
  • 12
    • 0020741491 scopus 로고
    • Energy storage in the primary step of the photocycle of bacteriorhodopsin
    • Birge, R.R. and Cooper, T.M. Energy storage in the primary step of the photocycle of bacteriorhodopsin. Biophys. J. 42 (1983) 61-69.
    • (1983) Biophys. J. , vol.42 , pp. 61-69
    • Birge, R.R.1    Cooper, T.M.2
  • 13
    • 33845554105 scopus 로고
    • Energy storage and reaction pathways in the first step of the vision process
    • Warshel, A. and Barboy, N. Energy storage and reaction pathways in the first step of the vision process. J. Am. Chem. Soc. 104 (1982) 1469-1476.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 1469-1476
    • Warshel, A.1    Barboy, N.2
  • 14
    • 0009643868 scopus 로고
    • Photoisomerization energy storage, and charge separation: A model for light energy transduction in visual pigments and bacteriorhodopsin
    • Honig, B., Ebrey, T., Callender, R.H., Dinur, U. and Ottolenghi, M. Photoisomerization, energy storage, and charge separation: a model for light energy transduction in visual pigments and bacteriorhodopsin. Proc. Natl. Acad. Sci. USA 76 (1979) 2503-2507.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 2503-2507
    • Honig, B.1    Ebrey, T.2    Callender, R.H.3    Dinur, U.4    Ottolenghi, M.5
  • 15
    • 36549097689 scopus 로고
    • Direct observation of the excited-state cis-trans photoisomerization of bacteriorhodopsin: Multilevel line shape theory for femtosecond dynamic hole burning and its application
    • Pollard, W.T., Cruz, C.H.B., Shank, Ch. and Mathies, R.A. Direct observation of the excited-state cis-trans photoisomerization of bacteriorhodopsin: Multilevel line shape theory for femtosecond dynamic hole burning and its application. J. Chem. Phys. 90 (1989) 199-208.
    • (1989) J. Chem. Phys. , vol.90 , pp. 199-208
    • Pollard, W.T.1    Cruz, C.H.B.2    Shank, Ch.3    Mathies, R.A.4
  • 16
    • 0025741997 scopus 로고
    • Femtosecond spectroscopy of acidified and neutral bacteriorhodopsin
    • Kobayashi, T., Terauchi, M., Kouyama, T., Yoshizawa, M. and Taiji, M. Femtosecond spectroscopy of acidified and neutral bacteriorhodopsin. SPIE 1403 (1991) 407-416.
    • (1991) SPIE , vol.1403 , pp. 407-416
    • Kobayashi, T.1    Terauchi, M.2    Kouyama, T.3    Yoshizawa, M.4    Taiji, M.5
  • 17
    • 0035969547 scopus 로고    scopus 로고
    • Real-time spectroscopy of transition states in bacteriorhodopsin during retinal isomerization
    • Kobayashi, T., Saito, T. and Ohtani, H. Real-time spectroscopy of transition states in bacteriorhodopsin during retinal isomerization. Nature 414 (2001) 531-534.
    • (2001) Nature , vol.414 , pp. 531-534
    • Kobayashi, T.1    Saito, T.2    Ohtani, H.3
  • 18
    • 0032475417 scopus 로고    scopus 로고
    • Primary step in bacteriorhodopsin photosynthesis: Bond stretch rather than angle twist of its retinal excited-state structure
    • Song, L. and El-Sayed, M.A. Primary step in bacteriorhodopsin photosynthesis: Bond stretch rather than angle twist of its retinal excited-state structure. J. Am. Chem. Soc. 120 (1998) 8889-8890.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 8889-8890
    • Song, L.1    El-Sayed, M.A.2
  • 20
    • 0038249440 scopus 로고
    • Femtosecond absorption studies of 14-fluorobacteriorhodopsin
    • (Laubereau, A. and Seilmeier, A., Eds), IOP Publishing Ltd, Bristol, England
    • Taiji, M., Bryl, K., Sekiya, N., Yoshihara, K., Kobayashi, T. Femtosecond absorption studies of 14-fluorobacteriorhodopsin. In: Ultrafast processes in spectroscopy (Laubereau, A. and Seilmeier, A., Eds), IOP Publishing Ltd, Bristol, England, 1992, 595-598.
    • (1992) Ultrafast Processes in Spectroscopy , pp. 595-598
    • Taiji, M.1    Bryl, K.2    Sekiya, N.3    Yoshihara, K.4    Kobayashi, T.5
  • 21
    • 0001435437 scopus 로고
    • Charge stabilization mechanism in the visual and purple membrane pigments
    • Warshel, A. Charge stabilization mechanism in the visual and purple membrane pigments. Proc. Natl. Acad. Sci. USA 75 (1978) 2558-2562.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 2558-2562
    • Warshel, A.1
  • 22
    • 0018504783 scopus 로고
    • Conversion of light energy to electrostatic energy in the proton pump of Halobacterium halobium
    • Warshel, A. Conversion of light energy to electrostatic energy in the proton pump of Halobacterium halobium. Photochem. Photobiol. 30 (1979) 285-290.
    • (1979) Photochem. Photobiol. , vol.30 , pp. 285-290
    • Warshel, A.1
  • 23
    • 0008035769 scopus 로고
    • The molecular mechanism of excitation in visual transduction and bacteriorhodopsin
    • Lewis, A. The molecular mechanism of excitation in visual transduction and bacteriorhodopsin. Proc. Natl. Acad. Sci. USA 75 (1978) 549-553.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 549-553
    • Lewis, A.1
  • 25
    • 0034818544 scopus 로고    scopus 로고
    • Study of the opsin shift of bacteriorhodopsin: Insight from QM/MM calculations with electronic polarization effect of the protein environment
    • Houjou, H., Inoue, Y. and Sakurai, M. Houjou, H., Inoue, Y. and Sakurai, M. Study of the opsin shift of bacteriorhodopsin: insight from QM/MM calculations with electronic polarization effect of the protein environment. J. Phys. Chem. B, 105 (2001) 867-879.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 867-879
    • Houjou, H.1    Inoue, Y.2    Sakurai, M.3    Houjou, H.4    Inoue, Y.5    Sakurai, M.6
  • 26
    • 0030299802 scopus 로고    scopus 로고
    • The photoisomerization of retinal in bacteriorhodopsin: Experimental evidence for a three-state model
    • Hasson, K.C., Gai, F. and Anfinrud, P.A. The photoisomerization of retinal in bacteriorhodopsin: experimental evidence for a three-state model. Proc. Natl. Acad. Sci. USA 93 (1996) 15124-15129.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 15124-15129
    • Hasson, K.C.1    Gai, F.2    Anfinrud, P.A.3
  • 27
    • 0027394224 scopus 로고
    • Two light-transducing membrane proteins: Mammalian rhodopsin and bacteriorhodopsin
    • Khorana, H.G. Two light-transducing membrane proteins: mammalian rhodopsin and bacteriorhodopsin. Proc. Natl. Acad. Sci. USA 90 (1993) 1166-1171.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1166-1171
    • Khorana, H.G.1
  • 28
    • 0001628475 scopus 로고
    • A new view of the dynamics of singlet cistrans photoisomerization
    • Weiss, R.M. and Warshel, A. A new view of the dynamics of singlet cistrans photoisomerization. J. Am. Chem. Soc. 101 (1979) 6131-6133.
    • (1979) J. Am. Chem. Soc. , vol.101 , pp. 6131-6133
    • Weiss, R.M.1    Warshel, A.2
  • 29
    • 0027190359 scopus 로고
    • Projection structure of rhodopsin
    • Schertler, G.F.X., Villa, C. and Henderson, R. Projection structure of rhodopsin. Nature 362 (1993) 770-772.
    • (1993) Nature , vol.362 , pp. 770-772
    • Schertler, G.F.X.1    Villa, C.2    Henderson, R.3
  • 31
    • 0030864048 scopus 로고    scopus 로고
    • X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phase
    • Pebay-Peyroula, E., Rummel, G., Rosenbusch, J.P. and Landau, E.M. X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phase. Science 277 (1997) 1676-1681.
    • (1997) Science , vol.277 , pp. 1676-1681
    • Pebay-Peyroula, E.1    Rummel, G.2    Rosenbusch, J.P.3    Landau, E.M.4
  • 32
    • 0033028464 scopus 로고    scopus 로고
    • How vertebrate and invertebrate visual pigments differ in their mechanism of photoactivation
    • Nakagawa, M., Iwasa, T., Kikkawa, S., Tsuda, M. and Ebrey, T.G. How vertebrate and invertebrate visual pigments differ in their mechanism of photoactivation. Proc. Natl. Acad. Sci. USA 96 (1999) 6189-6192.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6189-6192
    • Nakagawa, M.1    Iwasa, T.2    Kikkawa, S.3    Tsuda, M.4    Ebrey, T.G.5
  • 36
    • 0006003823 scopus 로고    scopus 로고
    • Implications of proton retarded transfer from purple membrane into the aqueous bulk phase for energy-coupling theories
    • Bryl, K. and Yoshihara, K. Implications of proton retarded transfer from purple membrane into the aqueous bulk phase for energy-coupling theories. Eur. Biophys. J. 26 (1997) 100.
    • (1997) Eur. Biophys. J. , vol.26 , pp. 100
    • Bryl, K.1    Yoshihara, K.2
  • 39
    • 0035854788 scopus 로고    scopus 로고
    • Mechanism of rhodopsin activation as examines with ring-constrained retinal analogues and the crystal structure of the ground state protein
    • Jang, G-F., Kuksa, V., Filipek, S., Bartl, F., Ritter, E., Gelb, M.H., Hofmann, K.P. and Palczewski, K. Mechanism of rhodopsin activation as examines with ring-constrained retinal analogues and the crystal structure of the ground state protein. J. Biol. Chem. 276 (2001) 26148-26153.
    • (2001) J. Biol. Chem. , vol.276 , pp. 26148-26153
    • Jang, G.-F.1    Kuksa, V.2    Filipek, S.3    Bartl, F.4    Ritter, E.5    Gelb, M.H.6    Hofmann, K.P.7    Palczewski, K.8
  • 41
    • 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. Signaling states of rhodopsin. Absorption of light in active metarhodopsin II generates an all-trans-retinal bound inactive state. J. Biol. Chem. 276 (2001) 30161-30166.
    • (2001) J. Biol. Chem. , vol.276 , pp. 30161-30166
    • Bartl, F.J.1    Ritter, E.2    Hofmann, K.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.