메뉴 건너뛰기




Volumn 72, Issue 3, 1997, Pages 1347-1356

Photoproducts of bacteriorhodopsin mutants: A molecular dynamics study

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; BACTERIORHODOPSIN; MUTANT PROTEIN; PROTON PUMP; RETINAL;

EID: 0031041820     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(97)78781-2     Document Type: Article
Times cited : (27)

References (33)
  • 2
    • 0027531526 scopus 로고
    • Light-driven proton or chloride pumping by halorhodopsin
    • Bamberg, E., J. Tittor, and D. Oesterhelt. 1992. Light-driven proton or chloride pumping by halorhodopsin. Proc. Natl. Acad. Sci. USA. 90: 473-486.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 473-486
    • Bamberg, E.1    Tittor, J.2    Oesterhelt, D.3
  • 4
    • 0028864699 scopus 로고
    • Glutamic acid 204 is the terminal proton release group at the extracellular surface of bacteriorhodopsin
    • Brown, L. S., J. Sasaki, H. Kandori, A. Maeda, R. Needleman, and J. K. Lanyi. 1995. Glutamic acid 204 is the terminal proton release group at the extracellular surface of bacteriorhodopsin. J. Biol. Chem. 270: 27122-27126.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27122-27126
    • Brown, L.S.1    Sasaki, J.2    Kandori, H.3    Maeda, A.4    Needleman, R.5    Lanyi, J.K.6
  • 5
    • 0004283184 scopus 로고
    • The Howard Hughes Medical Institute and Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT
    • Brünger, A. T. 1988. X-PLOR. The Howard Hughes Medical Institute and Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT.
    • (1988) X-PLOR
    • Brünger, A.T.1
  • 6
    • 0002979180 scopus 로고
    • Light energy transduction in bacteriorhodopsin
    • M. Jacobson, editor. CRC Press, New York
    • Ebrey, T. 1993. Light energy transduction in bacteriorhodopsin. In Thermodynamics of Membranes, Receptors and Channels. M. Jacobson, editor. CRC Press, New York. 353-387.
    • (1993) Thermodynamics of Membranes, Receptors and Channels , pp. 353-387
    • Ebrey, T.1
  • 7
    • 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
  • 8
    • 0028946790 scopus 로고
    • Effects of substitution of tyrosine 57 with asparagine and phenylalanine on the properties of bacteriorhodopsin
    • Govindjee, R., M. Kono, S. P. Balashov, E. Imasheva, M. Sheves, and T. G. Ebrey. 1995. Effects of substitution of tyrosine 57 with asparagine and phenylalanine on the properties of bacteriorhodopsin. Biochemistry. 34:4828-4838.
    • (1995) Biochemistry , vol.34 , pp. 4828-4838
    • Govindjee, R.1    Kono, M.2    Balashov, S.P.3    Imasheva, E.4    Sheves, M.5    Ebrey, T.G.6
  • 9
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryomicroscopy
    • 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 cryomicroscopy. 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
  • 10
    • 0024651574 scopus 로고
    • Replacement of aspartic acid-96 by asparagine in bacteriorhodopsin slows both the decay of the M intermediate and the associated proton movement
    • Holz, M., L. A. Drachev, T. Mogi, H. Otto, A. D. Kaulen, M. P. Heyn, V. P. Skulachev, and H. G. Khorana. 1989. Replacement of aspartic acid-96 by asparagine in bacteriorhodopsin slows both the decay of the M intermediate and the associated proton movement. Proc. Natl. Acad. Sci. USA. 86:2167-2171.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 2167-2171
    • Holz, M.1    Drachev, L.A.2    Mogi, T.3    Otto, H.4    Kaulen, A.D.5    Heyn, M.P.6    Skulachev, V.P.7    Khorana, H.G.8
  • 11
    • 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
  • 12
    • 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
  • 13
    • 0017764227 scopus 로고
    • Hydration effects on cis-trans isomerization of bacteriorhodopsin
    • Korenstein, R., and B. Hess. 1977. Hydration effects on cis-trans isomerization of bacteriorhodopsin. FEBS Lett. 82:7-11.
    • (1977) FEBS Lett. , vol.82 , pp. 7-11
    • Korenstein, R.1    Hess, B.2
  • 14
    • 0026654787 scopus 로고
    • Proton-transfer and energy coupling in the bacteriorhodopsin photocycle
    • Lanyi, J. K. 1992. Proton-transfer and energy coupling in the bacteriorhodopsin photocycle. J. Bioenerg. Biomembr. 24:169-179.
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 169-179
    • Lanyi, J.K.1
  • 15
    • 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
  • 16
    • 0028279038 scopus 로고
    • Interaction of aspartate-85 with a water molecule and the protonated Schiff base in the L intermediate of bacteriorhodopsin - A Fourier-transform infrared spectroscopic study
    • Maeda, A., J. Sasaki, Y. Yamazaki, R. Needleman, and J. K. Lanyi. 1994. Interaction of aspartate-85 with a water molecule and the protonated Schiff base in the L intermediate of bacteriorhodopsin - a Fourier-transform infrared spectroscopic study. Biochemistry. 33:1713-1717.
    • (1994) Biochemistry , vol.33 , pp. 1713-1717
    • Maeda, A.1    Sasaki, J.2    Yamazaki, Y.3    Needleman, R.4    Lanyi, J.K.5
  • 17
    • 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
  • 21
    • 0026623260 scopus 로고
    • A unifying concept for ion translocation in retinal proteins
    • Oesterhelt, D., J. 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, J.2    Bamberg, E.3
  • 22
    • 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
  • 23
    • 0025298852 scopus 로고
    • Water molecules and exchangeable hydrogen ions at the active centre of bacteriorhodopsin localized by neutron diffraction
    • Papadopoulos, G., N. Dencher, G. Zaccai, and G. Büldt. 1990. Water molecules and exchangeable hydrogen ions at the active centre of bacteriorhodopsin localized by neutron diffraction. J. Mol. Biol. 214: 15-19.
    • (1990) J. Mol. Biol. , vol.214 , pp. 15-19
    • Papadopoulos, G.1    Dencher, N.2    Zaccai, G.3    Büldt, G.4
  • 24
    • 0029665673 scopus 로고    scopus 로고
    • A linkage of the pKa's of Asp-85 and Glu-204 forms part of the reprotonation switch of bacteriorhodopsin
    • Richter, H.-T, L. S. Brown, R. Needleman, and J. K. Lanyi. 1996. A linkage of the pKa's of Asp-85 and Glu-204 forms part of the reprotonation switch of bacteriorhodopsin. Biochemistry. 35:4054-4062.
    • (1996) Biochemistry , vol.35 , pp. 4054-4062
    • Richter, H.-T.1    Brown, L.S.2    Needleman, R.3    Lanyi, J.K.4
  • 25
    • 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
  • 26
    • 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
  • 27
    • 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
  • 28
    • 0025327261 scopus 로고
    • The quantum yield of bacteriorhodopsin
    • Tittor, J., and D. Oesterhelt. 1990. The quantum yield of bacteriorhodopsin. FEBS Lett. 263:269-273.
    • (1990) FEBS Lett. , vol.263 , pp. 269-273
    • Tittor, J.1    Oesterhelt, D.2
  • 29
    • 0029160250 scopus 로고
    • Bacteriorhodopsin mutants D85N, D85T, and D85,96N as proton pumps
    • Tittor, J., D. Oesterhelt, and E. Bamberg. 1995. Bacteriorhodopsin mutants D85N, D85T, and D85,96N as proton pumps. Biophys. Chem. 56: 153-157.
    • (1995) Biophys. Chem. , vol.56 , pp. 153-157
    • Tittor, J.1    Oesterhelt, D.2    Bamberg, E.3
  • 30
    • 0027999089 scopus 로고
    • Inversion of proton translocation in bacteriorhodopsin mutants D85N, D85T, and D85,96N
    • Tittor, J., U. Schweiger, D. Oesterhelt, and E. Bamberg. 1994. Inversion of proton translocation in bacteriorhodopsin mutants D85N, D85T, and D85,96N. Biophys. J. 67:1682-1690.
    • (1994) Biophys. J. , vol.67 , pp. 1682-1690
    • Tittor, J.1    Schweiger, U.2    Oesterhelt, D.3    Bamberg, E.4
  • 31
    • 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
  • 32
    • 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
  • 33
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.