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Volumn 75, Issue 4, 1998, Pages 1689-1699

Three electronic state model of the primary phototransformation of bacteriorhodopsin

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIORHODOPSIN;

EID: 0031660699     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)77611-8     Document Type: Article
Times cited : (61)

References (67)
  • 1
    • 0346400157 scopus 로고    scopus 로고
    • Nonadiabatic molecular dynamics: Validation of the multiple spawning method for a multi-dimensional problem
    • in press
    • Ben-Nun, M., and T. Martinez. 1998. Nonadiabatic molecular dynamics: validation of the multiple spawning method for a multi-dimensional problem. J. Chem. Phys. (in press).
    • (1998) J. Chem. Phys.
    • Ben-Nun, M.1    Martinez, T.2
  • 3
    • 0000321633 scopus 로고
    • Quantum simulation of reaction dynamics by density matrix evolution
    • Berendsen, H., and J. Mavri. 1993. Quantum simulation of reaction dynamics by density matrix evolution. J. Phys. Chem. 97:13464-13468.
    • (1993) J. Phys. Chem. , vol.97 , pp. 13464-13468
    • Berendsen, H.1    Mavri, J.2
  • 4
    • 36549094506 scopus 로고
    • Two photon spectroscopy of light adapted bacteriorhodopsin
    • Birge, R. R., and C. F. Zhang. 1990. Two photon spectroscopy of light adapted bacteriorhodopsin. J. Chem. Phys. 92:7178-7195.
    • (1990) J. Chem. Phys. , vol.92 , pp. 7178-7195
    • Birge, R.R.1    Zhang, C.F.2
  • 5
    • 0001755637 scopus 로고
    • Critically heterosymmetric biradicaloid geometries of the protonated schiff bases
    • Bonacic-Koutecky, V., K. Schoffel, and J. Michl. 1987. Critically heterosymmetric biradicaloid geometries of the protonated schiff bases. Theor. Chim. Acta. 72:459-474.
    • (1987) Theor. Chim. Acta. , vol.72 , pp. 459-474
    • Bonacic-Koutecky, V.1    Schoffel, K.2    Michl, J.3
  • 6
    • 0000563788 scopus 로고    scopus 로고
    • Quantum-classical molecular dynamics as an approximation of full quantum dynamics
    • Bornemann, F. A., P. Nettesheim, and C. Schütte. 1996. Quantum-classical molecular dynamics as an approximation of full quantum dynamics. J. Chem. Phys. 105:1074-1083.
    • (1996) J. Chem. Phys. , vol.105 , pp. 1074-1083
    • Bornemann, F.A.1    Nettesheim, P.2    Schütte, C.3
  • 7
    • 0024289369 scopus 로고
    • Vibrational spectroscopy of bacteriorhodopsin mutants: Light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212
    • Braiman, M. S., T. Mogi, T. Marti, L. J. Stern. H. G. Khorana, and K. J. Rothschild. 1988. Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212. Biochemistry. 27:8516-8520.
    • (1988) Biochemistry , vol.27 , pp. 8516-8520
    • Braiman, M.S.1    Mogi, T.2    Marti, T.3    Stern, L.J.4    Khorana, H.G.5    Rothschild, K.J.6
  • 10
  • 11
    • 0001649161 scopus 로고
    • Excited-state reaction dynamics of bacteriorhodopsin studied by femtosecond spectroscopy
    • Dobler, J., W. Zinth, W. Kaiser, and D. Oesterhelt. 1988. Excited-state reaction dynamics of bacteriorhodopsin studied by femtosecond spectroscopy. Chem. Phys. Lett. 144:215-220.
    • (1988) Chem. Phys. Lett. , vol.144 , pp. 215-220
    • Dobler, J.1    Zinth, W.2    Kaiser, W.3    Oesterhelt, D.4
  • 12
    • 0027752269 scopus 로고
    • Femtosecond time-resolved fluorescence spectroscopy of bacteriorhodopsin: Direct observation of excited state dynamics in the primary step of the proton pump cycle
    • Du, M., and G. Fleming. 1993. Femtosecond time-resolved fluorescence spectroscopy of bacteriorhodopsin: direct observation of excited state dynamics in the primary step of the proton pump cycle. Biol. Cybern. 48:101-111.
    • (1993) Biol. Cybern. , vol.48 , pp. 101-111
    • Du, M.1    Fleming, G.2
  • 13
    • 0000945541 scopus 로고
    • Ab initio study on the excitation energies of the protonated schiff base of 11-cis-retinal
    • Du, P., and R. Davidson. 1990. Ab initio study on the excitation energies of the protonated schiff base of 11-cis-retinal. J. Phys. Chem. 94: 7013-1020.
    • (1990) J. Phys. Chem. , vol.94 , pp. 7013-11020
    • Du, P.1    Davidson, R.2
  • 14
    • 0002979180 scopus 로고
    • Light energy transduction in bacteriorhodopsin
    • M. Jacobson, editor. CRC Press, Boca Raton, FL
    • Ebrey, T. 1993. Light energy transduction in bacteriorhodopsin. In Thermodynamics of Membranes, Receptors and Channels. M. Jacobson, editor. CRC Press, Boca Raton, FL. 353-387.
    • (1993) Thermodynamics of Membranes, Receptors and Channels , pp. 353-387
    • Ebrey, T.1
  • 15
    • 0032549731 scopus 로고    scopus 로고
    • Chemical dynamics in proteins: The photoisomerization of retinal in bacteriorhodopsin
    • Gai, F., K. C. Hasson, J. C. McDonald, and P. A. Anfinrud. 1998. Chemical dynamics in proteins: the photoisomerization of retinal in bacteriorhodopsin. Science. 279:1886-1891.
    • (1998) Science. , vol.279 , pp. 1886-1891
    • Gai, F.1    Hasson, K.C.2    McDonald, J.C.3    Anfinrud, P.A.4
  • 16
    • 0025034111 scopus 로고
    • Quantum efficiency of the photochemical cycle of bacteriorhodopsin
    • Govindjee, R., S. P. Balashov, and T. G. Ebrey. 1990. Quantum efficiency of the photochemical cycle of bacteriorhodopsin. Biophys. J. 58: 597-608.
    • (1990) Biophys. J. , vol.58 , pp. 597-608
    • Govindjee, R.1    Balashov, S.P.2    Ebrey, T.G.3
  • 17
    • 0029903197 scopus 로고    scopus 로고
    • Electron-crystallographic refinement of the structure of bacteriorhopsin
    • Grigorieff, N., T. Ceska, K. Downing, J. Baldwin, and R. Henderson. 1996. Electron-crystallographic refinement of the structure of bacteriorhopsin. J. Mol. Biol. 259:393-421.
    • (1996) J. Mol. Biol. , vol.259 , pp. 393-421
    • Grigorieff, N.1    Ceska, T.2    Downing, K.3    Baldwin, J.4    Henderson, R.5
  • 18
    • 0030299802 scopus 로고    scopus 로고
    • The photoisomerization of retinal in bacteriorhodopsin: A new model
    • Hasson, K., F. Gai, and P. Anfinrud. 1996. The photoisomerization of retinal in bacteriorhodopsin: a new model. Proc. Natl. Acad. Sci. USA. 93:15124-15129.
    • (1996) Proc. Natl. Acad. Sci. USA. , vol.93 , pp. 15124-15129
    • Hasson, K.1    Gai, F.2    Anfinrud, P.3
  • 19
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson, R., J. M. Baldwin, T. A. Ceska, F. Zemlin, E. Beckmann, and K. H. Downing. 1990. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 213: 899-929.
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 20
    • 0002192623 scopus 로고
    • Linear polyene electronic structure and potential surfaces
    • E. C. Lim, editor. Academic Press, New York
    • Hudson, B. S., B. E. Kohler, and K. Schulten. 1982. Linear polyene electronic structure and potential surfaces. In Excited States, Vol. 6. E. C. Lim, editor. Academic Press, New York. 1-95.
    • (1982) Excited States , vol.6 , pp. 1-95
    • Hudson, B.S.1    Kohler, B.E.2    Schulten, K.3
  • 21
    • 0031041820 scopus 로고    scopus 로고
    • Photoproducts of bacteriorhodopsin mutants: A molecular dynamics study
    • Humphrey, W., E. Bamberg, and K. Schulten. 1997. Photoproducts of bacteriorhodopsin mutants: a molecular dynamics study. Biophys. J. 72:1347-1356.
    • (1997) Biophys. J. , vol.72 , pp. 1347-1356
    • Humphrey, W.1    Bamberg, E.2    Schulten, K.3
  • 23
    • 0028258544 scopus 로고
    • Molecular dynamics study of bacteriorhodopsin and artificial pigments
    • Humphrey, W., I. Logunov, K. Schulten, and M. Sheves. 1994. Molecular dynamics study of bacteriorhodopsin and artificial pigments. Biochemistry. 33:3668-3678.
    • (1994) Biochemistry , vol.33 , pp. 3668-3678
    • Humphrey, W.1    Logunov, I.2    Schulten, K.3    Sheves, M.4
  • 24
    • 0001513332 scopus 로고
    • Molecular dynamics study of the early intermediates in the bacteriorhodopsin photocycle
    • Humphrey, W., D. Xu, M. Sheves, and K. Schulten. 1995. Molecular dynamics study of the early intermediates in the bacteriorhodopsin photocycle. J. Phys. Chem. 99:14549-14560.
    • (1995) J. Phys. Chem. , vol.99 , pp. 14549-14560
    • Humphrey, W.1    Xu, D.2    Sheves, M.3    Schulten, K.4
  • 25
    • 0000034171 scopus 로고
    • Phase coherence and nonadiabatic transition at a level crossing in a periodically driven two-level system
    • Kayanuma, Y. 1993. Phase coherence and nonadiabatic transition at a level crossing in a periodically driven two-level system. Phys. Rev. B. 47: 9940-9943.
    • (1993) Phys. Rev. B. , vol.47 , pp. 9940-9943
    • Kayanuma, Y.1
  • 27
    • 5944242677 scopus 로고
    • An efficient second-order MC SCF method for long configuration expansions
    • Knowles, P. J., and H.-J. Werner. 1985. An efficient second-order MC SCF method for long configuration expansions. Chem. Phys. Lett. 115: 259-267.
    • (1985) Chem. Phys. Lett. , vol.115 , pp. 259-267
    • Knowles, P.J.1    Werner, H.-J.2
  • 29
    • 0031282975 scopus 로고    scopus 로고
    • Mechanism of ion transport across membranes: Bacteriorhodopsin as a prototype for proton pumps
    • Lanyi, J. 1997. Mechanism of ion transport across membranes: bacteriorhodopsin as a prototype for proton pumps. J. Biol. Chem. 272: 31290-31212.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31290-131212
    • Lanyi, J.1
  • 30
    • 0030010933 scopus 로고    scopus 로고
    • Replacement effects of neutral amino acid residues of different molecular volumes in the retinal binding cavity of bacteriorhodopsin on the dynamics of its primary process
    • Logunov, S., M. El-Sayed, and J. Lanyi. 1996a. Replacement effects of neutral amino acid residues of different molecular volumes in the retinal binding cavity of bacteriorhodopsin on the dynamics of its primary process. Biophys. J. 70:2875-2881.
    • (1996) Biophys. J. , vol.70 , pp. 2875-2881
    • Logunov, S.1    El-Sayed, M.2    Lanyi, J.3
  • 31
    • 33751130970 scopus 로고    scopus 로고
    • Photoisomerization quantum yield and apparent energy content of the K intermediate in the photocycles of bacteriorhodopsin, its mutants D85N, R82Q, and D212N, and deionized blue bacteriorhodopsin
    • Logunov, S., M. El-Sayed, and L. Song. 1996b. Photoisomerization quantum yield and apparent energy content of the K intermediate in the photocycles of bacteriorhodopsin, its mutants D85N, R82Q, and D212N, and deionized blue bacteriorhodopsin. J. Phys. Chem. 100:2391-2398.
    • (1996) J. Phys. Chem. , vol.100 , pp. 2391-2398
    • Logunov, S.1    El-Sayed, M.2    Song, L.3
  • 32
    • 84961983828 scopus 로고    scopus 로고
    • Quantum chemistry - Molecular dynamics study of the dark adaptation process in bacteriorhodopsin
    • Logunov, I., and K. Schulten. 1996. Quantum chemistry - molecular dynamics study of the dark adaptation process in bacteriorhodopsin. J. Am. Chem. Soc. 118:9727-9735.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 9727-9735
    • Logunov, I.1    Schulten, K.2
  • 33
    • 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
  • 34
    • 0031553028 scopus 로고    scopus 로고
    • Molecular collision dynamics on several electronic states
    • Martinez, T., M. Ben-Nun, and R. Levine. 1997. Molecular collision dynamics on several electronic states. J. Phys. Chem. A. 101: 6389-6402.
    • (1997) J. Phys. Chem. A. , vol.101 , pp. 6389-6402
    • Martinez, T.1    Ben-Nun, M.2    Levine, R.3
  • 35
    • 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
  • 36
    • 33751385143 scopus 로고
    • Influence of solvent on intramolecular proton transfer in hydrogen malonate -molecular dynamics simulation study of tunneling by density matrix evolution and nonequilibrium solvation
    • Mavri, J., H. J. C. Berendsen, and W. F. V. Gunsteren. 1993. Influence of solvent on intramolecular proton transfer in hydrogen malonate -molecular dynamics simulation study of tunneling by density matrix evolution and nonequilibrium solvation. J. Phys. Chem. 97: 13469-13476.
    • (1993) J. Phys. Chem. , vol.97 , pp. 13469-13476
    • Mavri, J.1    Berendsen, H.J.C.2    Gunsteren, W.F.V.3
  • 38
    • 0024024413 scopus 로고
    • Aspartic acid substitutions affect proton translocation by bacteriorhodopsin
    • Mogi, T., L. Stern, T. Marti, B. Chao, and H. Khorana. 1988. Aspartic acid substitutions affect proton translocation by bacteriorhodopsin. Proc. Natl. Acad. Sci. USA. 85:4148-4152.
    • (1988) Proc. Natl. Acad. Sci. USA. , vol.85 , pp. 4148-4152
    • Mogi, T.1    Stern, L.2    Marti, T.3    Chao, B.4    Khorana, H.5
  • 41
    • 0026623260 scopus 로고
    • A unifying concept for ion translocation in retinal proteins
    • Oesterhelt, D., I. Tittor, and E. Bamberg. 1992. A unifying concept for ion translocation in retinal proteins. J. Bioenerg. Biomembr. 24:181-191.
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 181-191
    • Oesterhelt, D.1    Tittor, I.2    Bamberg, E.3
  • 42
    • 0001319898 scopus 로고
    • Excited-state cis-trans isomerization of cis-hexatriene. A CAS-SCF computational study
    • Olivucci, M., F. Bernardi, P. Celani, I. Ragazos, and M. A. Robb. 1994. Excited-state cis-trans isomerization of cis-hexatriene. A CAS-SCF computational study. J. Am. Chem. Soc. 116:1077-1085.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 1077-1085
    • Olivucci, M.1    Bernardi, F.2    Celani, P.3    Ragazos, I.4    Robb, M.A.5
  • 43
    • 4444254527 scopus 로고
    • A conical intersection mechanism for the photochemistry of butadiene: A MC-SCF study
    • Ollivuci, M., I. Ragazos, F. Bernardi, and M. Robb. 1993. A conical intersection mechanism for the photochemistry of butadiene: a MC-SCF study. J. Am. Chem. Soc. 115:3710-3721.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 3710-3721
    • Ollivuci, M.1    Ragazos, I.2    Bernardi, F.3    Robb, M.4
  • 44
    • 0025016817 scopus 로고
    • Substitution of amino acids Asp-85, Asp-212, and Arg-82 in bacteriorhodopsin affects the proton release phase of the pump and the pK of the Schiff base
    • Otto, H., T. Marti, M. Holz, T. Mogi, L. J. Stern, F. Engel, H. G. Khorana, and M. P. Heyn. 1990. Substitution of amino acids Asp-85, Asp-212, and Arg-82 in bacteriorhodopsin affects the proton release phase of the pump and the pK of the Schiff base. Proc. Natl. Acad. Sci. USA. 87:1018-1022.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1018-1022
    • Otto, H.1    Marti, T.2    Holz, M.3    Mogi, T.4    Stern, L.J.5    Engel, F.6    Khorana, H.G.7    Heyn, M.P.8
  • 45
    • 0030864048 scopus 로고    scopus 로고
    • X-ray structure of bacteriorhodopsin at 2.5 Ångstroms from microcrystals grown in lipidic cubic phases
    • Pebay-Peyroula, E., G. Rummel, J. P. Rosenbusch, and E. M. Landau. 1997. X-ray structure of bacteriorhodopsin at 2.5 Ångstroms from microcrystals grown in lipidic cubic phases. Science. 227:1676-1691.
    • (1997) Science , vol.227 , pp. 1676-1691
    • Pebay-Peyroula, E.1    Rummel, G.2    Rosenbusch, J.P.3    Landau, E.M.4
  • 46
    • 0002650691 scopus 로고
    • Photochemical quantum yield of bacteriorhodopsin from resonance Raman scattering as a probe for photolysis
    • Schneider, G., R. Diller, and M. Stockburger. 1989. Photochemical quantum yield of bacteriorhodopsin from resonance Raman scattering as a probe for photolysis. Chem. Phys. 131:17-29.
    • (1989) Chem. Phys. , vol.131 , pp. 17-29
    • Schneider, G.1    Diller, R.2    Stockburger, M.3
  • 47
    • 0001595417 scopus 로고
    • The spectra of carbonium ions, cyanine dyes, and protonated Schiff base polyenes
    • Schulten, K., U. Dinur, and B. Honig. 1980. The spectra of carbonium ions, cyanine dyes, and protonated Schiff base polyenes. J. Chem. Phys. 73:3927-3935.
    • (1980) J. Chem. Phys. , vol.73 , pp. 3927-3935
    • Schulten, K.1    Dinur, U.2    Honig, B.3
  • 48
    • 85005653287 scopus 로고
    • Molecular dynamics studies of bacteriorhodopsin's photocycles
    • Schulten, K., W. Humphrey, I. Logunov, M. Sheves, and D. Xu. 1995. Molecular dynamics studies of bacteriorhodopsin's photocycles. Isr. J. Chem. 35:447-464.
    • (1995) Isr. J. Chem. , vol.35 , pp. 447-464
    • Schulten, K.1    Humphrey, W.2    Logunov, I.3    Sheves, M.4    Xu, D.5
  • 49
    • 3042528708 scopus 로고
    • On the origin of a low-lying forbidden transition in polyenes and related molecules
    • Schulten, K., and M. Karplus. 1972. On the origin of a low-lying forbidden transition in polyenes and related molecules. Chem. Phys. Lett. 14: 305-309.
    • (1972) Chem. Phys. Lett. , vol.14 , pp. 305-309
    • Schulten, K.1    Karplus, M.2
  • 50
    • 0030126484 scopus 로고    scopus 로고
    • Quantum decoherence and the isotope effect in condensed phase nonadiabatic molecular dynamics simulations
    • Schwartz, B., E. Bittner, O. Prezhdo, and P. Rossky. 1996. Quantum decoherence and the isotope effect in condensed phase nonadiabatic molecular dynamics simulations. J. Chem. Phys. 104:5492-5955.
    • (1996) J. Chem. Phys. , vol.104 , pp. 5492-5955
    • Schwartz, B.1    Bittner, E.2    Prezhdo, O.3    Rossky, P.4
  • 51
    • 0000897059 scopus 로고
    • Theoretical study of the electronic spectrum of all-trans-1,3.5,7-octatetraene
    • Serrano-Andreas, L., R. Lindh, B. Roos, and M. Merchan. 1993a. Theoretical study of the electronic spectrum of all-trans-1,3.5,7-octatetraene. J. Phys. Chem. 97:9360-9368.
    • (1993) J. Phys. Chem. , vol.97 , pp. 9360-9368
    • Serrano-Andreas, L.1    Lindh, R.2    Roos, B.3    Merchan, M.4
  • 52
    • 0004705927 scopus 로고
    • Towards an accurate molecular orbital theory for excited states: Ethene, butadiene, and hexatriene
    • Serrano-Andreas, L., M. Merchan, I. Nebot-Gil, and B. Roos. 1993b. Towards an accurate molecular orbital theory for excited states: ethene, butadiene, and hexatriene. J. Chem. Phys. 98:3151-3162.
    • (1993) J. Chem. Phys. , vol.98 , pp. 3151-3162
    • Serrano-Andreas, L.1    Merchan, M.2    Nebot-Gil, I.3    Roos, B.4
  • 53
    • 0027303125 scopus 로고
    • Protein catalysis of the retinal subpicosecond photo-isomerization in the primary process of bacteriorhodopsin photosynthesis
    • Song, L., M. A. El-Sayed, and J. K. Lanyi. 1993. Protein catalysis of the retinal subpicosecond photo-isomerization in the primary process of bacteriorhodopsin photosynthesis. Science. 261:891-894.
    • (1993) Science , vol.261 , pp. 891-894
    • Song, L.1    El-Sayed, M.A.2    Lanyi, J.K.3
  • 54
    • 84989742241 scopus 로고
    • Isomer composition and spectra of the dark and light adapted forms of artificial bacteriorhodopsins
    • Steinberg, G., N. Friedman, M. Sheves, and M. Ottolenghi. 1991. Isomer composition and spectra of the dark and light adapted forms of artificial bacteriorhodopsins. Photochem. Photobiol. 54:969-676.
    • (1991) Photochem. Photobiol. , vol.54 , pp. 969-1676
    • Steinberg, G.1    Friedman, N.2    Sheves, M.3    Ottolenghi, M.4
  • 55
    • 84984201096 scopus 로고
    • The active site of bacteriorhodopsin. Two-photon spectroscopic evidence for a positively charged chromophore binding site mediated by calcium
    • Stuart, J. A., B. W. Vought, C. F. Zhang, and R. R. Birge. 1995. The active site of bacteriorhodopsin. Two-photon spectroscopic evidence for a positively charged chromophore binding site mediated by calcium. Biospectroscopy. 1:9-28.
    • (1995) Biospectroscopy , vol.1 , pp. 9-28
    • Stuart, J.A.1    Vought, B.W.2    Zhang, C.F.3    Birge, R.R.4
  • 56
    • 0025157075 scopus 로고
    • Protonation state of Asp (Glu)-85 regulates the purple-to-blue transition in bacteriorhodopsin mutants Arg-82 → Ala and Asp-85 → Glu: The blue form is inactive in proton translocation
    • Subramaniam, S., T. Marti, and H. G. Khorana. 1990. Protonation state of Asp (Glu)-85 regulates the purple-to-blue transition in bacteriorhodopsin mutants Arg-82 → Ala and Asp-85 → Glu: the blue form is inactive in proton translocation. Proc. Natl. Acad. Sci. USA. 87:1013-1017.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1013-1017
    • Subramaniam, S.1    Marti, T.2    Khorana, H.G.3
  • 57
  • 58
    • 0006589319 scopus 로고
    • The low-lying electronic excitations in long polyenes: A PPP-MRD-CI study
    • Tavan, P., and K. Schulten. 1986. The low-lying electronic excitations in long polyenes: a PPP-MRD-CI study. J. Chem. Phys. 85:6602-6609.
    • (1986) J. Chem. Phys. , vol.85 , pp. 6602-6609
    • Tavan, P.1    Schulten, K.2
  • 59
    • 13044304431 scopus 로고
    • Molecular dynamics with electronic transitions
    • Tully, J. C. 1990. Molecular dynamics with electronic transitions. J. Chem. Phys. 93:1061-1071.
    • (1990) J. Chem. Phys. , vol.93 , pp. 1061-1071
    • Tully, J.C.1
  • 61
    • 0001604008 scopus 로고
    • The dynamics of the primary event in rhodopsins revisited
    • Warshel, A., Z.T. Chu, and J.-K. Hwang. 1991. The dynamics of the primary event in rhodopsins revisited. Chem. Phys. 158:303-314.
    • (1991) Chem. Phys. , vol.158 , pp. 303-314
    • Warshel, A.1    Chu, Z.T.2    Hwang, J.-K.3
  • 62
    • 85050310023 scopus 로고
    • Matrix-formulated direct multiconfiguration self-consistent field and multiconfiguration reference configuration-interaction methods
    • Werner, H.-J. 1987. Matrix-formulated direct multiconfiguration self-consistent field and multiconfiguration reference configuration-interaction methods. Adv. Chem. Phys. 69:1-62.
    • (1987) Adv. Chem. Phys. , vol.69 , pp. 1-62
    • Werner, H.-J.1
  • 63
    • 0037780883 scopus 로고
    • A second order multiconfiguration SCF procedure with optimum convergence
    • Werner, H.-J., and P. J. Knowles. 1985. A second order multiconfiguration SCF procedure with optimum convergence. J. Chem. Phys. 82: 5053-5063.
    • (1985) J. Chem. Phys. , vol.82 , pp. 5053-5063
    • Werner, H.-J.1    Knowles, P.J.2
  • 64
    • 0030058834 scopus 로고    scopus 로고
    • Molecular dynamics study of early picosecond events in the bacteriorhodopsin photocycle: Dielectric response, vibrational cooling and the J, K intermediates
    • Xu, D., C. Martin, and K. Schulten. 1996. Molecular dynamics study of early picosecond events in the bacteriorhodopsin photocycle: dielectric response, vibrational cooling and the J, K intermediates. Biophys. J. 70:453-460.
    • (1996) Biophys. J. , vol.70 , pp. 453-460
    • Xu, D.1    Martin, C.2    Schulten, K.3
  • 65
    • 0028845662 scopus 로고
    • Molecular dynamics study of the M412 intermediate of bacteriorhodopsin
    • Xu, D., M. Sheves, and K. Schulten. 1995. Molecular dynamics study of the M412 intermediate of bacteriorhodopsin. Biophys. J. 69:2745-2760.
    • (1995) Biophys. J. , vol.69 , pp. 2745-2760
    • Xu, D.1    Sheves, M.2    Schulten, K.3
  • 66
    • 0001332554 scopus 로고
    • Non-adiabatic crossing of energy levels
    • Zener, C. 1932. Non-adiabatic crossing of energy levels. Proc. Natl. Acad. Sci. USA. A137:696-702.
    • (1932) Proc. Natl. Acad. Sci. USA , vol.A137 , pp. 696-702
    • Zener, C.1
  • 67
    • 0027476774 scopus 로고
    • Molecular dynamics study of the proton pump cycle of bacteriorhodopsin
    • Zhou, F., A. Windemuth, and K. Schulten. 1993. Molecular dynamics study of the proton pump cycle of bacteriorhodopsin. Biochemistry. 32:2291-2306.
    • (1993) Biochemistry , vol.32 , pp. 2291-2306
    • Zhou, F.1    Windemuth, A.2    Schulten, K.3


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