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Volumn 86, Issue 2, 2010, Pages 316-323

Kinetics of the M-Intermediate in the photocycle of bacteriorhodopsin upon chemical modification with surfactants

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIORHODOPSIN; SCHIFF BASE; SURFACTANT;

EID: 77649258649     PISSN: 00318655     EISSN: 17511097     Source Type: Journal    
DOI: 10.1111/j.1751-1097.2009.00666.x     Document Type: Article
Times cited : (10)

References (52)
  • 1
    • 0030864048 scopus 로고    scopus 로고
    • X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases
    • Pebay-Peyroula, E., G. Rummel, J. P. Rosenbusch E. M. Landau (1997) X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases. Science 277, 1676 1681.
    • (1997) Science , vol.277 , pp. 1676-1681
    • Pebay-Peyroula, E.1    Rummel, G.2    Rosenbusch, J.P.3    Landau, E.M.4
  • 2
    • 0032578378 scopus 로고    scopus 로고
    • Lipid patches in membrane protein oligomers: Crystal structure of the bacteriorhodopsin-lipid complex
    • Essen, L.-O., R. Siegert, W. D. Lehmann D. Oesterhelt (1998) Lipid patches in membrane protein oligomers: Crystal structure of the bacteriorhodopsin-lipid complex. Proc. Natl. Acad. Sci. USA 95, 11673 11678.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11673-11678
    • Essen, L.-O.1    Siegert, R.2    Lehmann, W.D.3    Oesterhelt, D.4
  • 3
    • 0032546920 scopus 로고    scopus 로고
    • Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution
    • Luecke, H., H.-T. Richter J. K. Lanyi (1998) Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution. Science 280, 1934 1937.
    • (1998) Science , vol.280 , pp. 1934-1937
    • Luecke, H.1    Richter, H.-T.2    Lanyi, J.K.3
  • 6
    • 85005688720 scopus 로고
    • The photocycles of bacteriorhodopsin
    • Lanyi, J. K. G. Váró (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
  • 7
    • 0018805369 scopus 로고
    • Binding of all-trans-retinal to the purple membrane. Evidence for cooperativity and determination of the extinction coefficient
    • Rehorek, M. M. P. Heyn (1979) Binding of all-trans-retinal to the purple membrane. Evidence for cooperativity and determination of the extinction coefficient. Biochemistry 18, 4977 4983.
    • (1979) Biochemistry , vol.18 , pp. 4977-4983
    • Rehorek, M.1    Heyn, M.P.2
  • 9
    • 0025871066 scopus 로고
    • Kinetic and spectroscopic evidence for an irreversible step between deprotonation and reprotonation of the Schiff base in the bacteriorhodopsin photocycle
    • Váró, G. J. K. Lanyi (1991) Kinetic and spectroscopic evidence for an irreversible step between deprotonation and reprotonation of the Schiff base in the bacteriorhodopsin photocycle. Biochemistry 30, 5008 5015.
    • (1991) Biochemistry , vol.30 , pp. 5008-5015
    • Váró, G.1    Lanyi, J.K.2
  • 10
    • 0025820289 scopus 로고
    • Thermodynamics and energy coupling in the bacteriorhodopsin photocycle
    • Váró, G. J. K. Lanyi (1991) Thermodynamics and energy coupling in the bacteriorhodopsin photocycle. Biochemistry 30, 5016 5022.
    • (1991) Biochemistry , vol.30 , pp. 5016-5022
    • Váró, G.1    Lanyi, J.K.2
  • 11
    • 0025723894 scopus 로고
    • Effects of the crystalline structure of purple membrane on the kinetics and energetics of the bacteriorhodopsin photocycle
    • Váró, G. J. K. Lanyi (1991) Effects of the crystalline structure of purple membrane on the kinetics and energetics of the bacteriorhodopsin photocycle. Biochemistry 30, 7165 7171.
    • (1991) Biochemistry , vol.30 , pp. 7165-7171
    • Váró, G.1    Lanyi, J.K.2
  • 13
    • 0035823064 scopus 로고    scopus 로고
    • a calculations suggest storage of an excess proton in a hydrogen-bonded water network in bacteriorhodopsin
    • a calculations suggest storage of an excess proton in a hydrogen-bonded water network in bacteriorhodopsin. J. Mol. Biol. 312, 203 219.
    • (2001) J. Mol. Biol. , vol.312 , pp. 203-219
    • Spassov, V.Z.1    Luecke, H.2    Gerwert, K.3    Bashford, D.4
  • 15
    • 0031556661 scopus 로고    scopus 로고
    • Bacteriorhodopsin intermediate spectra determined over a wide pH range
    • Gergely, C., L. Zimányi G. Váró (1997) Bacteriorhodopsin intermediate spectra determined over a wide pH range. J. Phys. Chem. B 101, 9390 9395.
    • (1997) J. Phys. Chem. B , vol.101 , pp. 9390-9395
    • Gergely, C.1    Zimányi, L.2    Váró, G.3
  • 16
    • 0034734242 scopus 로고    scopus 로고
    • Chemical and physical evidence for multiple functional steps comprising the M state of the bacteriorhodopsin photocycle
    • and references therein
    • Betancourt, F. M. H. R. M. Glaeser (2000) Chemical and physical evidence for multiple functional steps comprising the M state of the bacteriorhodopsin photocycle. Biochim. Biophys. Acta 1460, 106 118, and references therein.
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 106-118
    • Betancourt, F.M.H.1    Glaeser, R.M.2
  • 17
    • 0034734253 scopus 로고    scopus 로고
    • Crystallographic analysis of protein conformational changes in the bacteriorhodopsin photocycle
    • Subramaniam, S. R. Henderson (2000) Crystallographic analysis of protein conformational changes in the bacteriorhodopsin photocycle. Biochim. Biophys. Acta 1460, 157 165.
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 157-165
    • Subramaniam, S.1    Henderson, R.2
  • 18
    • 0025968915 scopus 로고
    • Protein dynamics in the bacteriorhodopsin photocycle: Submillisecond Fourier transform infrared spectra of the L, M, and N photointermediates
    • Braiman, M. S., O. Bousché K. J. Rothschild (1991) Protein dynamics in the bacteriorhodopsin photocycle: Submillisecond Fourier transform infrared spectra of the L, M, and N photointermediates. Proc. Natl. Acad. Sci. USA 88, 2388 2392.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2388-2392
    • Braiman, M.S.1    Bousché, O.2    Rothschild, K.J.3
  • 20
    • 0037466289 scopus 로고    scopus 로고
    • 2′ intermediates of the photocycle
    • DOI 10.1016/S0022-2836(03)00263-8
    • 2′ intermediates of the photocycle. J. Mol. Biol. 328, 439 450, and references therein. (Pubitemid 36407586)
    • (2003) Journal of Molecular Biology , vol.328 , Issue.2 , pp. 439-450
    • Lanyi, J.K.1    Schobert, B.2
  • 21
    • 2942556920 scopus 로고    scopus 로고
    • X-ray diffraction of bacteriorhodopsin photocycle intermediates (Review)
    • Lanyi, J. K. (2004) X-ray diffraction of bacteriorhodopsin photocycle intermediates (Review). Mol. Membr. Biol. 21, 143 150.
    • (2004) Mol. Membr. Biol. , vol.21 , pp. 143-150
    • Lanyi, J.K.1
  • 23
    • 0034632821 scopus 로고    scopus 로고
    • Helix deformation is coupled to vectorial proton transport in the photocycle of bacteriorhodopsin
    • Royant, A., K. Edman, T. Ursby, E. Pebay-Peyroula, E. M. Landauk R. Neutze (2000) Helix deformation is coupled to vectorial proton transport in the photocycle of bacteriorhodopsin. Nature 406, 645 648.
    • (2000) Nature , vol.406 , pp. 645-648
    • Royant, A.1    Edman, K.2    Ursby, T.3    Pebay-Peyroula, E.4    Landauk, E.M.5    Neutze, R.6
  • 24
    • 0034632864 scopus 로고    scopus 로고
    • Molecular mechanism of vectorial proton translocation by bacteriorhodopsin
    • Subramaniam, S. R. Henderson (2000) Molecular mechanism of vectorial proton translocation by bacteriorhodopsin. Nature 406, 653 657.
    • (2000) Nature , vol.406 , pp. 653-657
    • Subramaniam, S.1    Henderson, R.2
  • 25
    • 1242274581 scopus 로고    scopus 로고
    • Dynamics of proton transfer in bacteriorhodopsin
    • Lee, Y.-S. M. Krauss (2004) Dynamics of proton transfer in bacteriorhodopsin. J. Am. Chem. Soc. 126, 2225 2230.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 2225-2230
    • Lee, Y.-S.1    Krauss, M.2
  • 26
    • 17344381776 scopus 로고    scopus 로고
    • Unidirectional proton transfer mechanism in the L → M → N sequence of bacteriorhodopsin
    • Murata, K., T. Hoshino, Y. Sato, M. Hata M. Tsuda (2003) Unidirectional proton transfer mechanism in the L → M → N sequence of bacteriorhodopsin. J. Mol. Struct. (Theochem) 664-665, 125 133.
    • (2003) J. Mol. Struct. (Theochem) , vol.664-665 , pp. 125-133
    • Murata, K.1    Hoshino, T.2    Sato, Y.3    Hata, M.4    Tsuda, M.5
  • 27
    • 0042386423 scopus 로고    scopus 로고
    • Proton affinity changes driving unidirectional proton transport in the bacteriorhodopsin photocycle
    • Onufriev, A., A. Smondyrev D. Bashford (2003) Proton affinity changes driving unidirectional proton transport in the bacteriorhodopsin photocycle. J. Mol. Biol. 332, 1183 1193.
    • (2003) J. Mol. Biol. , vol.332 , pp. 1183-1193
    • Onufriev, A.1    Smondyrev, A.2    Bashford, D.3
  • 29
    • 0025260818 scopus 로고
    • Effect of partial delipidation of purple membrane on the photodynamics of bacteriorhodopsin
    • Fukuda, K., A. Ikegami, A. Nasuda-Kouyama T. Kouyama (1990) Effect of partial delipidation of purple membrane on the photodynamics of bacteriorhodopsin. Biochemistry 29, 1997 2002.
    • (1990) Biochemistry , vol.29 , pp. 1997-2002
    • Fukuda, K.1    Ikegami, A.2    Nasuda-Kouyama, A.3    Kouyama, T.4
  • 30
    • 0017749540 scopus 로고
    • Hydration effects on the photocycle of bacteriorhodopsin in thin layers of purple membrane
    • Korenstein, R. B. Hess (1977) Hydration effects on the photocycle of bacteriorhodopsin in thin layers of purple membrane. Nature 270, 184 186.
    • (1977) Nature , vol.270 , pp. 184-186
    • Korenstein, R.1    Hess, B.2
  • 31
    • 0034734238 scopus 로고    scopus 로고
    • Water and bacteriorhodopsin: Structure, dynamics, and function
    • Dencher, N. A., H. J. Sass G. Büldt (2000) Water and bacteriorhodopsin: Structure, dynamics, and function. Biochim. Biophys. Acta 1460, 192 203.
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 192-203
    • Dencher, N.A.1    Sass, H.J.2    Büldt, G.3
  • 32
    • 0030813030 scopus 로고    scopus 로고
    • The last phase of the reprotonation switch in bacteriorhodopsin: The transition between the M-type and the N-type protein conformation depends on hydration
    • Kamikubo, H., T. Oka, Y. Imamoto, F. Tokunaga, J. K. Lanyi M. Kataoka (1997) The last phase of the reprotonation switch in bacteriorhodopsin: The transition between the M-type and the N-type protein conformation depends on hydration. Biochemistry 36, 12282 12287.
    • (1997) Biochemistry , vol.36 , pp. 12282-12287
    • Kamikubo, H.1    Oka, T.2    Imamoto, Y.3    Tokunaga, F.4    Lanyi, J.K.5    Kataoka, M.6
  • 33
    • 0027327364 scopus 로고
    • Photoreaction of the N intermediate of bacteriorhodopsin, and its relationship to the decay kinetics of the M intermediate
    • Brown, L. S., L. Zimányi, R. Needleman, M. Ottolenghi J. K. Lanyi (1993) Photoreaction of the N intermediate of bacteriorhodopsin, and its relationship to the decay kinetics of the M intermediate. Biochemistry 32, 7679 7685.
    • (1993) Biochemistry , vol.32 , pp. 7679-7685
    • Brown, L.S.1    Zimányi, L.2    Needleman, R.3    Ottolenghi, M.4    Lanyi, J.K.5
  • 34
    • 0020852470 scopus 로고
    • Effects of pressure and temperature on the M412 intermediate of the bacteriorhodopsin photocycle
    • Tsuda, M., R. Govindjee T. G. Ebrey (1983) Effects of pressure and temperature on the M412 intermediate of the bacteriorhodopsin photocycle. Biophys. J. 44, 249 254.
    • (1983) Biophys. J. , vol.44 , pp. 249-254
    • Tsuda, M.1    Govindjee, R.2    Ebrey, T.G.3
  • 35
    • 0038650626 scopus 로고    scopus 로고
    • Proton transfer reactions in native and deionized bacteriorhodopsin upon delipidation and monomerization
    • Heyes, C. D. M. A. El-Sayed (2003) Proton transfer reactions in native and deionized bacteriorhodopsin upon delipidation and monomerization. Biophys. J. 85, 426 434.
    • (2003) Biophys. J. , vol.85 , pp. 426-434
    • Heyes, C.D.1    El-Sayed, M.A.2
  • 36
    • 0024061598 scopus 로고
    • Deprotonation of lipid-depleted bacteriorhodopsin
    • Jang, D.-J. M. A. El-Sayed (1988) Deprotonation of lipid-depleted bacteriorhodopsin. Proc. Natl. Acad. Sci. USA 85, 5918 5922.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5918-5922
    • Jang, D.-J.1    El-Sayed, M.A.2
  • 37
    • 0025731582 scopus 로고
    • Effects of detergent environments on the photocycle of purified monomeric bacteriorhodopsin
    • Milder, S. J., T. E. Thorgeirsson, L. J. W. Miercke, R. M. Stroud D. S. Kliger (1991) Effects of detergent environments on the photocycle of purified monomeric bacteriorhodopsin. Biochemistry 30, 1751 1761.
    • (1991) Biochemistry , vol.30 , pp. 1751-1761
    • Milder, S.J.1    Thorgeirsson, T.E.2    Miercke, L.J.W.3    Stroud, R.M.4    Kliger, D.S.5
  • 38
    • 0011288153 scopus 로고
    • Formation and decay kinetics of bacteriorhodopsin's N intermediate: Softening the protein conformation with alcohols affects intra-protein proton transfer and retinal isomerization
    • Fukuda, K. T. Kouyama (1992) Formation and decay kinetics of bacteriorhodopsin's N intermediate: Softening the protein conformation with alcohols affects intra-protein proton transfer and retinal isomerization. Photochem. Photobiol. 56, 1057 1062.
    • (1992) Photochem. Photobiol. , vol.56 , pp. 1057-1062
    • Fukuda, K.1    Kouyama, T.2
  • 39
    • 67749119979 scopus 로고    scopus 로고
    • Gold nanoparticles surface plasmon field effects on the proton pump process of the bacteriorhodopsin photosynthesis
    • Biesso, A., W. Qian, X. Huang M. A. El-Sayed (2009) Gold nanoparticles surface plasmon field effects on the proton pump process of the bacteriorhodopsin photosynthesis. J. Am. Chem. Soc. 131, 2442 2443.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 2442-2443
    • Biesso, A.1    Qian, W.2    Huang, X.3    El-Sayed, M.A.4
  • 40
    • 0016376428 scopus 로고
    • Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane
    • Oesterhelt, D. W. Stoeckenius (1974) Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane. Methods Enzyml. 31, 667 678.
    • (1974) Methods Enzyml. , vol.31 , pp. 667-678
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 41
    • 0025096943 scopus 로고
    • Large scale preparation of homogeneous bacteriorhodopsin
    • Lorber, B. L. J. DeLucas (1990) Large scale preparation of homogeneous bacteriorhodopsin. FEBS Lett. 261, 14 18.
    • (1990) FEBS Lett. , vol.261 , pp. 14-18
    • Lorber, B.1    Delucas, L.J.2
  • 42
    • 0037899632 scopus 로고    scopus 로고
    • Small-angle neutron scattering studies of aqueous solutions of short-chain amphiphiles
    • D'Arrigo, G. R. Giordano J. Teixeira (2003) Small-angle neutron scattering studies of aqueous solutions of short-chain amphiphiles. Eur. Phys. J. E10, 135 142.
    • (2003) Eur. Phys. J. , vol.10 , pp. 135-142
    • D'Arrigo, G.1    Giordano, R.2    Teixeira, J.3
  • 44
    • 33751385602 scopus 로고
    • Effect of head-group size on micellization and phase behavior in quaternary ammonium surfactant systems
    • Buckingham, S. A., C. J. Garvey G. G. Warr (1993) Effect of head-group size on micellization and phase behavior in quaternary ammonium surfactant systems. J. Phys. Chem. 97, 10236 10244.
    • (1993) J. Phys. Chem. , vol.97 , pp. 10236-10244
    • Buckingham, S.A.1    Garvey, C.J.2    Warr, G.G.3
  • 45
    • 0021515705 scopus 로고
    • Exploratory study of the effect of polyelectrolyte-surfactant aggregates on photochemical behavior
    • Abuin, E. B. J. C. Scaiano (1984) Exploratory study of the effect of polyelectrolyte-surfactant aggregates on photochemical behavior. J. Am. Chem. Soc. 106, 6274 6283.
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 6274-6283
    • Abuin, E.B.1    Scaiano, J.C.2
  • 46
    • 0032396564 scopus 로고    scopus 로고
    • Determination of critical micelle concentration of anionic surfactants by capillary electrophoresis using 2-Naphthalenemethanol as a marker for micelle formation
    • Nakamura, H., A. Sano K. Matsuura (1998) Determination of critical micelle concentration of anionic surfactants by capillary electrophoresis using 2-Naphthalenemethanol as a marker for micelle formation. Anal. Sci. 14, 379 382.
    • (1998) Anal. Sci. , vol.14 , pp. 379-382
    • Nakamura, H.1    Sano, A.2    Matsuura, K.3
  • 47
    • 34047258702 scopus 로고    scopus 로고
    • The solubility of ethane in aqueous solutions of sodium 1-pentanesulfonate, sodium 1-hexanesulfonate, sodium 1-heptanesulfonate, and sodium 1-octanesulfonate at 25°C
    • Calhoun, A. R. A. D. King Jr. (2007) The solubility of ethane in aqueous solutions of sodium 1-pentanesulfonate, sodium 1-hexanesulfonate, sodium 1-heptanesulfonate, and sodium 1-octanesulfonate at 25°C. J. Coll. Interf. Sci. 309, 505 510.
    • (2007) J. Coll. Interf. Sci. , vol.309 , pp. 505-510
    • Calhoun, A.R.1    King, Jr.A.D.2
  • 48
    • 0019873844 scopus 로고
    • Photochemistry and fluorescence of bacteriorhodopsin excited in its 280-nm absorption band
    • Kalisky, O., J. Feitelson M. Ottolenghi (1981) Photochemistry and fluorescence of bacteriorhodopsin excited in its 280-nm absorption band. Biochemistry 20, 205 209.
    • (1981) Biochemistry , vol.20 , pp. 205-209
    • Kalisky, O.1    Feitelson, J.2    Ottolenghi, M.3
  • 50
    • 0030897749 scopus 로고    scopus 로고
    • Light-induced protein conformational changes in the photolysis of octopus rhodopsin
    • Nakagawa, M., S. Kikkawa, T. Iwasa M. Tsuda (1997) Light-induced protein conformational changes in the photolysis of octopus rhodopsin. Biophys. J. 72, 2320 2328.
    • (1997) Biophys. J. , vol.72 , pp. 2320-2328
    • Nakagawa, M.1    Kikkawa, S.2    Iwasa, T.3    Tsuda, M.4
  • 51
    • 0029880335 scopus 로고    scopus 로고
    • Correlation between surfactant\micelle structure and the stability of bacteriorhodopsin in solution
    • Tan, E. H. L. R. R. Birge (1996) Correlation between surfactant\micelle structure and the stability of bacteriorhodopsin in solution. Biophys. J. 70, 2385 2395.
    • (1996) Biophys. J. , vol.70 , pp. 2385-2395
    • Tan, E.H.L.1    Birge, R.R.2
  • 52
    • 0031738407 scopus 로고    scopus 로고
    • Kinetic and thermodynamic study of the bacteriorhodopsin photocycle over a wide pH range
    • Ludmann, K., C. Gergely G. Váró (1998) Kinetic and thermodynamic study of the bacteriorhodopsin photocycle over a wide pH range. Biophys. J. 75, 3110 3119. (Pubitemid 28548979)
    • (1998) Biophysical Journal , vol.75 , Issue.6 , pp. 3110-3119
    • Ludmann, K.1    Gergely, C.2    Varo, G.3


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