메뉴 건너뛰기




Volumn 273, Issue 5, 1997, Pages 951-957

Transient channel-opening in bacteriorhodopsin: An EPR study

Author keywords

Bacteriorhodopsin; Electron paramagnetic resonance; Photocycle; Retinal proteins; Spin labels

Indexed keywords

BACTERIORHODOPSIN; SCHIFF BASE;

EID: 0031567784     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1362     Document Type: Editorial
Times cited : (107)

References (30)
  • 1
    • 0028787636 scopus 로고
    • Functional significance of a protein conformation change at the cytoplasmic end of helix F during the bacteriorhodopsin photocycle
    • Brown, L. S., Váró, G., Needleman, R. & Lanyi, J. K. (1995). Functional significance of a protein conformation change at the cytoplasmic end of helix F during the bacteriorhodopsin photocycle. Biophys. J. 69, 2103-2111.
    • (1995) Biophys. J. , vol.69 , pp. 2103-2111
    • Brown, L.S.1    Váró, G.2    Needleman, R.3    Lanyi, J.K.4
  • 2
    • 0026332339 scopus 로고
    • Water is required for proton transfer from aspartate-96 to the bacteriorhodopsin Schiff base
    • Cao, Y., Váró, G., Chang, M., Ni, B., Needleman, R. & Lanyi, J. K. (1991). Water is required for proton transfer from aspartate-96 to the bacteriorhodopsin Schiff base. Biochemistry, 30, 10972-10979.
    • (1991) Biochemistry , vol.30 , pp. 10972-10979
    • Cao, Y.1    Váró, G.2    Chang, M.3    Ni, B.4    Needleman, R.5    Lanyi, J.K.6
  • 3
    • 0024744871 scopus 로고
    • Structural changes in bacteriorhodopsin during proton translocation revealed by neutron diffraction
    • Dencher, N. A., Dresselhaus, D., Zaccai, G. & Büldt, G. (1989). Structural changes in bacteriorhodopsin during proton translocation revealed by neutron diffraction. Proc. Natl Acad. Sci. USA, 86, 7876-7879.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 7876-7879
    • Dencher, N.A.1    Dresselhaus, D.2    Zaccai, G.3    Büldt, G.4
  • 4
    • 0029907599 scopus 로고    scopus 로고
    • Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin
    • Farrens, D. L., Altenbach, C., Yang, K., Hubbell, W. L. & Khorana, H. G. (1996). Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin. Science, 274, 768-770.
    • (1996) Science , vol.274 , pp. 768-770
    • Farrens, D.L.1    Altenbach, C.2    Yang, K.3    Hubbell, W.L.4    Khorana, H.G.5
  • 6
    • 0028335096 scopus 로고
    • Structural mechanisms for domain movements in proteins
    • Gerstein, M., Lesk, A. M. & Chothia, C. (1994). Structural mechanisms for domain movements in proteins. Biochemistry, 33, 6739-6749.
    • (1994) Biochemistry , vol.33 , pp. 6739-6749
    • Gerstein, M.1    Lesk, A.M.2    Chothia, C.3
  • 7
    • 0029903197 scopus 로고    scopus 로고
    • Electron crystallographic refinement of the structure of bacteriorhodopsin
    • Grigorieff, N., Ceska, T. A., Downing, K. H., Baldwin, J. M. & Henderson, R. (1996). Electron crystallographic refinement of the structure of bacteriorhodopsin. J. Mol. Biol. 259, 393-421.
    • (1996) J. Mol. Biol. , vol.259 , pp. 393-421
    • Grigorieff, N.1    Ceska, T.A.2    Downing, K.H.3    Baldwin, J.M.4    Henderson, R.5
  • 8
    • 0030757501 scopus 로고    scopus 로고
    • Two modes of ligand binding in maltose-binding protein of Escherichia coli
    • Hall, J. A., Thorgeirsson, T. E., Liu, J., Shin, Y.-K. & Nikaido, H. (1997). Two modes of ligand binding in maltose-binding protein of Escherichia coli. J. Biol. Chem. 272, 17610-17614.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17610-17614
    • Hall, J.A.1    Thorgeirsson, T.E.2    Liu, J.3    Shin, Y.-K.4    Nikaido, H.5
  • 9
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryomicroscopy
    • Henderson, R., Baldwin, J. M., Ceska, T. A., Zemlin, R., Beckmann, E. & Downing, K. H. (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, R.4    Beckmann, E.5    Downing, K.H.6
  • 10
    • 0014029736 scopus 로고
    • Simple allosteric model for membrane pumps
    • Jardetzky, O. (1966). Simple allosteric model for membrane pumps. Nature, 211, 969-970.
    • (1966) Nature , vol.211 , pp. 969-970
    • Jardetzky, O.1
  • 11
    • 0031043155 scopus 로고    scopus 로고
    • Rapid loop dynamics of Yersinia protein phosphatases
    • Juszcak, L. J., Zhang, Z.-Y., Gottfried, D. S. & Eads, D. D. (1997). Rapid loop dynamics of Yersinia protein phosphatases. Biochemistry, 36, 2227-2236.
    • (1997) Biochemistry , vol.36 , pp. 2227-2236
    • Juszcak, L.J.1    Zhang, Z.-Y.2    Gottfried, D.S.3    Eads, D.D.4
  • 14
    • 0025976082 scopus 로고
    • Time-resolved X-ray diffraction study of structural changes associated with the photocycle of bacteriorhodopsin
    • Koch, M. H. J., Dencher, N. A., Oesterhelt, D., Plöhn, H.-J., Rapp, G. & Büldt, G. (1991). Time-resolved X-ray diffraction study of structural changes associated with the photocycle of bacteriorhodopsin. EMBO J. 10, 521-526.
    • (1991) EMBO J. , vol.10 , pp. 521-526
    • Koch, M.H.J.1    Dencher, N.A.2    Oesterhelt, D.3    Plöhn, H.-J.4    Rapp, G.5    Büldt, G.6
  • 15
    • 0027769837 scopus 로고
    • Proton translocation mechanism and energetics in the light-driven pump bacteriorhodopsin
    • Lanyi, J. K. (1993). Proton translocation mechanism and energetics in the light-driven pump bacteriorhodopsin. Biochim. Biophys. Acta, 241-261.
    • (1993) Biochim. Biophys. Acta , pp. 241-261
    • Lanyi, J.K.1
  • 16
    • 0029057198 scopus 로고
    • Bacteriorhodopsin as a model for proton pumps
    • Lanyi, J. K. (1995). Bacteriorhodopsin as a model for proton pumps. Nature, 375, 461-463.
    • (1995) Nature , vol.375 , pp. 461-463
    • Lanyi, J.K.1
  • 17
    • 85005688720 scopus 로고
    • The photocycles of bacteriorhodopsin
    • Lanyi, J. K. & Váró, G. (1995). The photocycles of bacteriorhodopsin. Israel J. Chem. 35, 365-385.
    • (1995) Israel J. Chem. , vol.35 , pp. 365-385
    • Lanyi, J.K.1    Váró, G.2
  • 18
    • 0016723355 scopus 로고
    • Bacteriorhodopsin: A light-driven proton pump in Halobacterium halobium
    • Lozier, R. H., Bogomolni, R. A. & Stoeckenius, W. (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
  • 19
    • 0026342828 scopus 로고
    • Intrasubunit signal transduction by the aspartate chemoreceptor
    • Milligan, D. L. & Koshland, D. E. (1991). Intrasubunit signal transduction by the aspartate chemoreceptor. Science, 254, 1651-1654.
    • (1991) Science , vol.254 , pp. 1651-1654
    • Milligan, D.L.1    Koshland, D.E.2
  • 20
    • 0026094796 scopus 로고
    • Crystallographic characterization by X-ray diffraction of the M-intermediate from the photocycle of bacteriorhodopsin at room temperature
    • Nakasako, M., Kataoka, M., Amemiya, Y. & Tokunaga, F. (1991). Crystallographic characterization by X-ray diffraction of the M-intermediate from the photocycle of bacteriorhodopsin at room temperature. FEBS Letters, 292, 73-75.
    • (1991) FEBS Letters , vol.292 , pp. 73-75
    • Nakasako, M.1    Kataoka, M.2    Amemiya, Y.3    Tokunaga, F.4
  • 21
    • 0029115328 scopus 로고
    • Determination of the distance between two spin labels attached to a macromolecule
    • Rabenstein, M. D. & Shin, Y. K. (1995). Determination of the distance between two spin labels attached to a macromolecule. Proc. Natl Acad. Sci. USA, 92, 8239-8243.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 8239-8243
    • Rabenstein, M.D.1    Shin, Y.K.2
  • 22
    • 0029904711 scopus 로고    scopus 로고
    • HIV-1 gp41 tertiary structure studied by EPR spectroscopy
    • Rabenstein, M. D. & Shin, Y. K. (1996). HIV-1 gp41 tertiary structure studied by EPR spectroscopy. Biochemistry, 35, 13922-13928.
    • (1996) Biochemistry , vol.35 , pp. 13922-13928
    • Rabenstein, M.D.1    Shin, Y.K.2
  • 23
    • 0029665673 scopus 로고    scopus 로고
    • A linkage of the pKas of Asp-85 and Glu-204 forms part of the reprotonation switch of bacteriorhodopsin
    • Richter, H. T., Brown, L. S., Needleman, R. & Lanyi, J. K. (1996). A linkage of the pKas 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
  • 24
    • 0027447891 scopus 로고
    • Colicin-E1 binding to membranes: Time-resolved studies of spin-labeled mutants
    • Shin, Y.-K., Levinthal, C., Levinthal, F. & Hubbell, W. L. (1993). Colicin-E1 binding to membranes: time-resolved studies of spin-labeled mutants. Science, 259, 960-963.
    • (1993) Science , vol.259 , pp. 960-963
    • Shin, Y.-K.1    Levinthal, C.2    Levinthal, F.3    Hubbell, W.L.4
  • 25
    • 0030222328 scopus 로고    scopus 로고
    • Shuttling between two protein conformations: The common mechanism for sensory transduction and ion transport
    • Spudich, J. L. & Lanyi, J. K. (1996). Shuttling between two protein conformations: the common mechanism for sensory transduction and ion transport. Curr. Opinion Cell. Biol. 8, 452-457.
    • (1996) Curr. Opinion Cell. Biol. , vol.8 , pp. 452-457
    • Spudich, J.L.1    Lanyi, J.K.2
  • 26
    • 0027972897 scopus 로고
    • Time-resolved detection of structural changes during the photocycle of spin-labeled bacteriorhodopsin
    • Steinhoff, H. J., Mollaaghababa, R., Altenbach, C., Hideg, K., Krebs, M., Khorana, H. G. & Hubbell, W. L. (1994). Time-resolved detection of structural changes during the photocycle of spin-labeled bacteriorhodopsin. Science, 266, 105-107.
    • (1994) Science , vol.266 , pp. 105-107
    • Steinhoff, H.J.1    Mollaaghababa, R.2    Altenbach, C.3    Hideg, K.4    Krebs, M.5    Khorana, H.G.6    Hubbell, W.L.7
  • 27
    • 0020669965 scopus 로고
    • Mechanism of free energy coupling in active transport
    • Tanford, C. (1983). Mechanism of free energy coupling in active transport. Annu Rev. Biochem. 52, 379-409.
    • (1983) Annu Rev. Biochem. , vol.52 , pp. 379-409
    • Tanford, C.1
  • 28
    • 0028921479 scopus 로고
    • Acetylcholine receptor channel imaged in the open state
    • Unwin, N. (1995). Acetylcholine receptor channel imaged in the open state. Nature, 373, 37-43.
    • (1995) Nature , vol.373 , pp. 37-43
    • Unwin, N.1
  • 29
    • 0030065552 scopus 로고    scopus 로고
    • Protein structural change at the cytoplasmic surface as the cause of cooperativity in the bacteriorhodopsin photocycle
    • Váró, G., Needleman, R. & Lanyi, J. K. (1996). Protein structural change at the cytoplasmic surface as the cause of cooperativity in the bacteriorhodopsin photocycle. Biophys. J. 70, 461-467.
    • (1996) Biophys. J. , vol.70 , pp. 461-467
    • Váró, G.1    Needleman, R.2    Lanyi, J.K.3
  • 30
    • 0029886089 scopus 로고    scopus 로고
    • A three-dimensional difference map of the N intermediate in hte bacteriorhodopsin photocycle: Part of the F helix tilts in the M to N transition
    • Vonck, J. (1996). A three-dimensional difference map of the N intermediate in hte bacteriorhodopsin photocycle: part of the F helix tilts in the M to N transition. Biochemistry, 35, 5870-5878.
    • (1996) Biochemistry , vol.35 , pp. 5870-5878
    • Vonck, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.