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Volumn 81, Issue 6, 2005, Pages 1356-1360

Partial dehydration of the retinal binding pocket and proof for photochemical deprotonation of the retinal Schiff base in bicelle bacteriorhodopsin crystals

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIORHODOPSIN; PROTON; RETINAL; SCHIFF BASE;

EID: 29844433028     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1562/2005-03-09-RA-458     Document Type: Article
Times cited : (2)

References (36)
  • 1
    • 0017062945 scopus 로고
    • On the primary quantum yields in the bacteriorhodopsin photocycle
    • Goldschmidt, C. R., M. Ottolenghi and R. Korenstein (1976) On the primary quantum yields in the bacteriorhodopsin photocycle. Biophys. J. 16, 839-843.
    • (1976) Biophys. J. , vol.16 , pp. 839-843
    • Goldschmidt, C.R.1    Ottolenghi, M.2    Korenstein, R.3
  • 3
    • 0015886107 scopus 로고
    • Reversible photolysis of the purple complex in the purple membrane of Halobacterium halobium
    • Oesterhelt, D. and B. Hess (1973) Reversible photolysis of the purple complex in the purple membrane of Halobacterium halobium. Eur. J. Biochem. 37, 316-326.
    • (1973) Eur. J. Biochem. , vol.37 , pp. 316-326
    • Oesterhelt, D.1    Hess, B.2
  • 4
    • 0016324977 scopus 로고
    • Light energy conversion in Halobacterium halobium
    • Stoeckenius, W. and R. H. Lozier (1974) Light energy conversion in Halobacterium halobium. J. Supramol. Struct. 2, 769-774.
    • (1974) J. Supramol. Struct. , vol.2 , pp. 769-774
    • Stoeckenius, W.1    Lozier, R.H.2
  • 5
    • 0016723355 scopus 로고
    • Bacteriorhodopsin, a light-driven proton pump in Halobacterium halobium
    • Lozier, R. H., R. A. Bogomolni and W. Stoeckenius (1975) Bacteriorhodopsin, a light-driven proton pump in Halobacterium halobium. Biophys. J. 15, 955-962.
    • (1975) Biophys. J. , vol.15 , pp. 955-962
    • Lozier, R.H.1    Bogomolni, R.A.2    Stoeckenius, W.3
  • 6
    • 0016565838 scopus 로고
    • Isomeric configuration of the bacteriorhodopsin chromophore
    • Jan, L. Y. (1975) Isomeric configuration of the bacteriorhodopsin chromophore. Vision Res. 15, 1081-1086.
    • (1975) Vision Res. , vol.15 , pp. 1081-1086
    • Jan, L.Y.1
  • 7
    • 0017420381 scopus 로고
    • The purple membrane from Halobacterium halobium
    • Henderson, R. (1977) The purple membrane from Halobacterium halobium. Annu. Rev. Biophys. Bioeng. 6, 87-109.
    • (1977) Annu. Rev. Biophys. Bioeng. , vol.6 , pp. 87-109
    • Henderson, R.1
  • 9
    • 0017195595 scopus 로고
    • Light-induced changes of the pH gradient and the membrane potential in H. halobium
    • Michel, H. and D. Oesterhelt (1976) Light-induced changes of the pH gradient and the membrane potential in H. halobium. FEBS Lett. 65, 175-178.
    • (1976) FEBS Lett. , vol.65 , pp. 175-178
    • Michel, H.1    Oesterhelt, D.2
  • 10
    • 0017172823 scopus 로고
    • An estimation of the light-induced electrochemical potential difference of protons across the membrane of Halobacterium halobium
    • Bakker, E. P., H. Rottenberg and S. R. Caplan (1976) An estimation of the light-induced electrochemical potential difference of protons across the membrane of Halobacterium halobium. Biochim. Biophys. Acta 440, 557-572.
    • (1976) Biochim. Biophys. Acta , vol.440 , pp. 557-572
    • Bakker, E.P.1    Rottenberg, H.2    Caplan, S.R.3
  • 13
    • 0020008581 scopus 로고
    • Resonance Raman spectra of bacteriorhodopsin's primary photoproduct: Evidence for a distorted 13-cis retinal chromophore
    • Braiman, M. and R. Mathies (1982) Resonance Raman spectra of bacteriorhodopsin's primary photoproduct: evidence for a distorted 13-cis retinal chromophore. Proc. Natl. Acad. Sci. USA 79, 403-407.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 403-407
    • Braiman, M.1    Mathies, R.2
  • 14
    • 0024279842 scopus 로고
    • Direct observation of the femtosecond excited-state cis-trans isomerization in bacteriorhodopsin
    • Mathies, R. A., C. H. Brito Cruz, W. T. Pollard and C. V. Shank (1988) Direct observation of the femtosecond excited-state cis-trans isomerization in bacteriorhodopsin. Science 240, 777-779.
    • (1988) Science , vol.240 , pp. 777-779
    • Mathies, R.A.1    Brito Cruz, C.H.2    Pollard, W.T.3    Shank, C.V.4
  • 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., C. H. Cruz, C. V. Shank and R. A. Mathies (1989) 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, 199-208.
    • (1989) J. Chem. Phys. , vol.90 , pp. 199-208
    • Pollard, W.T.1    Cruz, C.H.2    Shank, C.V.3    Mathies, R.A.4
  • 16
    • 0025299602 scopus 로고
    • The role of back-reactions and proton uptake during the N-O transition in bacteriorhodopsin's photocycle: A kinetic resonance Raman study
    • Ames, J. B. and R. A. Mathies (1990) The role of back-reactions and proton uptake during the N-O transition in bacteriorhodopsin's photocycle: a kinetic resonance Raman study. Biochemistry 29, 7181-7190.
    • (1990) Biochemistry , vol.29 , pp. 7181-7190
    • Ames, J.B.1    Mathies, R.A.2
  • 17
    • 0023676060 scopus 로고
    • Vibrational spectroscopy of bacteriorhodopsin mutants. I. Tyrosine-185 protonates and deprotonates during the photocycle
    • Braiman, M. S., T. Mogi, L. J. Stern, N. R. Hackett, B. H. Chao, H. G. Khorana and K. J. Rothschild (1988) Vibrational spectroscopy of bacteriorhodopsin mutants. I. Tyrosine-185 protonates and deprotonates during the photocycle. Proteins 3, 219-229.
    • (1988) Proteins , vol.3 , pp. 219-229
    • Braiman, M.S.1    Mogi, T.2    Stern, L.J.3    Hackett, N.R.4    Chao, B.H.5    Khorana, H.G.6    Rothschild, K.J.7
  • 18
    • 0024707259 scopus 로고
    • Role of aspartate-96 in proton translocation by bacteriorhodopsin
    • Gerwert, K., B. Hess, J. Soppa and D. Oesterhelt (1989) Role of aspartate-96 in proton translocation by bacteriorhodopsin. Proc. Natl. Acad. Sci. USA 86, 4943-4947.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 4943-4947
    • Gerwert, K.1    Hess, B.2    Soppa, J.3    Oesterhelt, D.4
  • 19
    • 0025820289 scopus 로고
    • Thermodynamics and energy coupling in the bacteriorhodopsin photocycle
    • Varo, G. and J. K. Lanyi (1991) Thermodynamics and energy coupling in the bacteriorhodopsin photocycle. Biochemistry 30, 5016-5022.
    • (1991) Biochemistry , vol.30 , pp. 5016-5022
    • Varo, G.1    Lanyi, J.K.2
  • 20
    • 0036301007 scopus 로고    scopus 로고
    • Bicelle crystallization: A new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure
    • Bowie, J. and S. Farham (2002) Bicelle crystallization: a new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure. J. Mol. Biol. 316, 1-6.
    • (2002) J. Mol. Biol. , vol.316 , pp. 1-6
    • Bowie, J.1    Farham, S.2
  • 21
    • 0029992660 scopus 로고    scopus 로고
    • Lipidic cubic phases: A novel concept for the crystallization of membrane proteins
    • Landau, E. M. and J. P. Rosenbusch (1996) Lipidic cubic phases: a novel concept for the crystallization of membrane proteins. Proc. Natl. Acad. Sci. USA 93, 14532-14535.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14532-14535
    • Landau, E.M.1    Rosenbusch, J.P.2
  • 22
    • 23244434448 scopus 로고    scopus 로고
    • The protonation-deprotonation kinetics of the protonated Schiff base in bicelle bacteriorhodopsin crystals
    • Sanii, L. S., A. W. Schill, C. E. Moran and M. A. El-Sayed (2005) The protonation-deprotonation kinetics of the protonated Schiff base in bicelle bacteriorhodopsin crystals. Biophys. J. 89, 444-451.
    • (2005) Biophys. J. , vol.89 , pp. 444-451
    • Sanii, L.S.1    Schill, A.W.2    Moran, C.E.3    El-Sayed, M.A.4
  • 23
    • 29844456852 scopus 로고
    • Time-resolved resonance Raman studies of the photochemical cycle of bacteriorhodopsin
    • Edited by G. H. Atkinson, Academic Press, New York, Proceedings of the International Conference on Time-Resolved Vibrational Spectroscopy, 1982
    • Alshuth, T., I. Grieger, and M. Stockburger and Max-Planck-Institute of Biophysical Chemistry, Federal Republic of Germany (1982) Time-resolved resonance Raman studies of the photochemical cycle of bacteriorhodopsin. In Time-Resolved Vibrational Spectroscopy (Edited by G. H. Atkinson), pp. 231-237. Academic Press, New York, Proceedings of the International Conference on Time-Resolved Vibrational Spectroscopy, 1982.
    • (1982) Time-Resolved Vibrational Spectroscopy , pp. 231-237
    • Alshuth, T.1    Grieger, I.2    Stockburger, M.3
  • 24
  • 27
    • 0017774407 scopus 로고
    • Resonance Raman studies of the conformation of retinal in rhodopsin and isorhodopsin
    • Mathies, R., T. B. Freedman and L. Stryer (1977) Resonance Raman studies of the conformation of retinal in rhodopsin and isorhodopsin. J. Mol. Biol. 109, 367-372.
    • (1977) J. Mol. Biol. , vol.109 , pp. 367-372
    • Mathies, R.1    Freedman, T.B.2    Stryer, L.3
  • 28
    • 0016289846 scopus 로고
    • Resonance Raman spectroscopy of rhodopsin in retinal disk membranes
    • Oseroff, A. R. and R. H. Callender (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    Callender, R.H.2
  • 29
    • 0000217440 scopus 로고
    • Role of water in bacteriorhodopsin's chromophore: Resonance Raman study
    • Hildebrandt, P. and M. Stockburger (1984) Role of water in bacteriorhodopsin's chromophore: resonance Raman study. Biochemistry 23, 5539-5548.
    • (1984) Biochemistry , vol.23 , pp. 5539-5548
    • Hildebrandt, P.1    Stockburger, M.2
  • 30
    • 0018805372 scopus 로고
    • Photochemical cycle of bacteriorhodopsin studied by resonance Raman spectroscopy
    • Stockburger, M., W. Klusmann, H. Gattermann, G. Massig and R. Peters (1979) Photochemical cycle of bacteriorhodopsin studied by resonance Raman spectroscopy. Biochemistry 18, 4886-4900.
    • (1979) Biochemistry , vol.18 , pp. 4886-4900
    • Stockburger, M.1    Klusmann, W.2    Gattermann, H.3    Massig, G.4    Peters, R.5
  • 31
    • 0019123462 scopus 로고
    • Resonance Raman evidence for an all-trans to 13-cis isomerization in the proton-pumping cycle of bacteriorhodopsin
    • Braiman, M. and R. Mathies (1980) Resonance Raman evidence for an all-trans to 13-cis isomerization in the proton-pumping cycle of bacteriorhodopsin. Biochemistry 19, 5421-5428.
    • (1980) Biochemistry , vol.19 , pp. 5421-5428
    • Braiman, M.1    Mathies, R.2
  • 32
    • 0018175997 scopus 로고
    • Resonance Raman spectroscopy of squid and bovine visual pigments: The primary photochemistry in visual transduction
    • Henderson, R., M. Sulkes, A. Lewis and M. A. Marcus (1978) Resonance Raman spectroscopy of squid and bovine visual pigments: the primary photochemistry in visual transduction. Biochemistry 17, 4712-4722.
    • (1978) Biochemistry , vol.17 , pp. 4712-4722
    • Henderson, R.1    Sulkes, M.2    Lewis, A.3    Marcus, M.A.4
  • 34
    • 84989665835 scopus 로고
    • Time-resolved resonance Raman spectra of the photocycle intermediates of acid and deionized bacteriorhodopsin
    • Chronister, E. L. and M. A. El-Sayed (1987) Time-resolved resonance Raman spectra of the photocycle intermediates of acid and deionized bacteriorhodopsin. Photochem. Photobiol. 45, 507-513.
    • (1987) Photochem. Photobiol. , vol.45 , pp. 507-513
    • Chronister, E.L.1    El-Sayed, M.A.2
  • 36
    • 0025493084 scopus 로고
    • Ultraviolet resonance Raman spectroscopy of bacteriorhodopsin
    • Netto, M. M., S. P. A. Fodor and R. A. Mathies (1990) Ultraviolet resonance Raman spectroscopy of bacteriorhodopsin. Photochem. Photobiol. 52, 605-607.
    • (1990) Photochem. Photobiol. , vol.52 , pp. 605-607
    • Netto, M.M.1    Fodor, S.P.A.2    Mathies, R.A.3


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