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Volumn 78, Issue 6, 2000, Pages 3170-3177

Buffer effects on electric signals of light-excited bacteriorhodopsin

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIORHODOPSIN; BUFFER; DEUTERIUM OXIDE; GLYCYLGLYCINE; PROPANE; PROTON PUMP; SODIUM CHLORIDE;

EID: 0342657187     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76853-6     Document Type: Article
Times cited : (12)

References (31)
  • 1
    • 0028887546 scopus 로고
    • Rapid long-range proton diffusion along the surface of the purple membrane and delayed proton transfer into the bulk
    • Alexiev, U., R. Mollaghababa, P. Scherrer, H. G. Khorana, and M. Heyn. 1995. Rapid long-range proton diffusion along the surface of the purple membrane and delayed proton transfer into the bulk. Proc. Natl. Acad. Sci. USA. 92:372-376.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 372-376
    • Alexiev, U.1    Mollaghababa, R.2    Scherrer, P.3    Khorana, H.G.4    Heyn, M.5
  • 2
    • 0030808219 scopus 로고    scopus 로고
    • Glutamate-194 to cysteine mutation inhibits fast light-induced proton release in bacteriorhodopsin
    • Balashov, S. P., E. S. Imasheva, T. G. Ebrey, N. Chen, D. R. Menick, and R. K. Crouch. 1997. Glutamate-194 to cysteine mutation inhibits fast light-induced proton release in bacteriorhodopsin. Biochemistry. 36: 8671-8676.
    • (1997) Biochemistry , vol.36 , pp. 8671-8676
    • Balashov, S.P.1    Imasheva, E.S.2    Ebrey, T.G.3    Chen, N.4    Menick, D.R.5    Crouch, R.K.6
  • 3
    • 0028239690 scopus 로고
    • The proton transfers in the cytoplasmic domain of bacteriorhodopsin are facilitated by a cluster of interacting residues
    • Brown, L. S., Y. Yamazaki, A. Maeda, L. Sun, R. Needleman, and J. K. Lanyi. 1994. The proton transfers in the cytoplasmic domain of bacteriorhodopsin are facilitated by a cluster of interacting residues. J. Mol. Biol. 239:401-414.
    • (1994) J. Mol. Biol. , vol.239 , pp. 401-414
    • Brown, L.S.1    Yamazaki, Y.2    Maeda, A.3    Sun, L.4    Needleman, R.5    Lanyi, J.K.6
  • 4
    • 0028864699 scopus 로고
    • Glutamic acid 204 is the terminal group at the extracellular surface of the bacteriorhodopsin
    • Brown, S. L., J. Sasaki, H. Kandori, A. Maeda, R. Needleman, and J. K. Lanyi. 1995. Glutamic acid 204 is the terminal group at the extracellular surface of the bacteriorhodopsin. J Biol. Chem. 27:27122-27126.
    • (1995) J Biol. Chem. , vol.27 , pp. 27122-27126
    • Brown, S.L.1    Sasaki, J.2    Kandori, H.3    Maeda, A.4    Needleman, R.5    Lanyi, J.K.6
  • 5
    • 0028949144 scopus 로고
    • Relationship of proton release at the extracellular surface to deprotonation of the Schiff- base in the bacteriorhodopsin photocycle
    • Cao, Y., L. S. Brown, J. Sasaki, A. Maeda, R. Needleman, and J. K. Lanyi. 1995. Relationship of proton release at the extracellular surface to deprotonation of the Schiff- base in the bacteriorhodopsin photocycle. Biophys. J. 68:1518-1530.
    • (1995) Biophys. J. , vol.68 , pp. 1518-1530
    • Cao, Y.1    Brown, L.S.2    Sasaki, J.3    Maeda, A.4    Needleman, R.5    Lanyi, J.K.6
  • 6
    • 0030665489 scopus 로고    scopus 로고
    • Mechanism of proton entry into the cytoplasmic section of the proton-conducting channel of bacteriorhodopsin
    • Checover, S., E. Nachliel, N. A. Dencher, and M. Gutman. 1997. Mechanism of proton entry into the cytoplasmic section of the proton-conducting channel of bacteriorhodopsin. Biochemistry. 36: 13919-13928.
    • (1997) Biochemistry , vol.36 , pp. 13919-13928
    • Checover, S.1    Nachliel, E.2    Dencher, N.A.3    Gutman, M.4
  • 7
    • 0021983430 scopus 로고
    • Time resolved photoelectric and absorption signals from oriented purple membranes immobilised in gels
    • Dér, A., P. Hargittai, and J. Simon. 1985. Time resolved photoelectric and absorption signals from oriented purple membranes immobilised in gels. J. Biochem. Biophys. Methods. 10:295-300.
    • (1985) J. Biochem. Biophys. Methods. , vol.10 , pp. 295-300
    • Dér, A.1    Hargittai, P.2    Simon, J.3
  • 8
    • 0342999421 scopus 로고
    • Counterions and the bacteriorhodopsin proton pump
    • Dér, A., R. Tóth-Boconádi, and L. Keszthelyi. 1988. Counterions and the bacteriorhodopsin proton pump. FEBS Lett. 229:313-316.
    • (1988) FEBS Lett. , vol.229 , pp. 313-316
    • Dér, A.1    Tóth-Boconádi, R.2    Keszthelyi, L.3
  • 9
    • 0032562215 scopus 로고    scopus 로고
    • Existence of a proton transfer chain in bacteriorhodopsin: Participation of Glu-194 in the release of protons to the external surface
    • Dioumaev, A. K., H. T. Richter, L. S. Brown, M. Tanio, S. Tuzi, H. Saito, Y. Kimura, R. Needleman, and J. K. Lanyi. 1998. Existence of a proton transfer chain in bacteriorhodopsin: participation of Glu-194 in the release of protons to the external surface. Biochemistry. 37:2496-2506.
    • (1998) Biochemistry , vol.37 , pp. 2496-2506
    • Dioumaev, A.K.1    Richter, H.T.2    Brown, L.S.3    Tanio, M.4    Tuzi, S.5    Saito, H.6    Kimura, Y.7    Needleman, R.8    Lanyi, J.K.9
  • 11
    • 0016193990 scopus 로고
    • Buffer facilitated proton transport, pH profile of hound enzymes
    • Engasser, J. M., and Cs. Horvath. 1973. Buffer facilitated proton transport, pH profile of hound enzymes. Biochim. Biophys. Acta. 338:178-192.
    • (1973) Biochim. Biophys. Acta. , vol.338 , pp. 178-192
    • Engasser, J.M.1    Horvath, Cs.2
  • 12
    • 0025629995 scopus 로고
    • Simultaneous monitoring of light-induced changes in protein side-group protonation, chromophore isomerization, and backbone motion of bacteriorhodopsin by time-resolved Fourier-transform infrared spectroscopy
    • Gerwert, K., G. Souvignier, and B. Hess. 1990. Simultaneous monitoring of light-induced changes in protein side-group protonation, chromophore isomerization, and backbone motion of bacteriorhodopsin by time-resolved Fourier-transform infrared spectroscopy. Proc. Natl. Acad. Sci. USA. 87:9774-9778.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 9774-9778
    • Gerwert, K.1    Souvignier, G.2    Hess, B.3
  • 13
    • 0001652299 scopus 로고
    • Time-course and stoichiometry of light-induced proton release and uptake during the photocycle of bacteriorhodopsin
    • Grzesiek, S., and N. A. Dencher. 1986. Time-course and stoichiometry of light-induced proton release and uptake during the photocycle of bacteriorhodopsin. FEBS Lett. 208:337-342.
    • (1986) FEBS Lett. , vol.208 , pp. 337-342
    • Grzesiek, S.1    Dencher, N.A.2
  • 14
    • 0025181491 scopus 로고
    • The dynamic aspects of proton transfer processes
    • Gutman, M., and E. Nachliel, E. 1990. The dynamic aspects of proton transfer processes. Biochim. Biophys. Acta. 1015:391-414.
    • (1990) Biochim. Biophys. Acta. , vol.1015 , pp. 391-414
    • Gutman, M.1    E Nachliel, E.2
  • 15
    • 0343870692 scopus 로고    scopus 로고
    • Proton transfer reactions across bacteriorhodopsin and along the membrane
    • in press
    • Heberle, J. 1999. Proton transfer reactions across bacteriorhodopsin and along the membrane. Biochim. Biophys. Acta. (in press).
    • (1999) Biochim. Biophys. Acta.
    • Heberle, J.1
  • 16
    • 0025608977 scopus 로고
    • Bacteriorhodopsin in ice: Accelerated proton transfer from the purple membrane surface
    • Heberle, J., and N. A. Dencher. 1990. Bacteriorhodopsin in ice: accelerated proton transfer from the purple membrane surface. FEBS Lett. 277: 277-280.
    • (1990) FEBS Lett. , vol.277 , pp. 277-280
    • Heberle, J.1    Dencher, N.A.2
  • 17
    • 0026725522 scopus 로고
    • Surface bound optical probes monitor proton translocation and surface potential changes during the bacteriorhodopsin photocycle
    • Heberle, J., and N. A. Dencher. 1992. Surface bound optical probes monitor proton translocation and surface potential changes during the bacteriorhodopsin photocycle. Proc. Natl. Acad. Sci. USA. 89: 5996-6000.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5996-6000
    • Heberle, J.1    Dencher, N.A.2
  • 18
    • 0028102402 scopus 로고
    • Proton migration along the membrane surface and retarded surface to bulk transfer
    • Heberle, J., J. Riesle, G. Thiedemann, D. Oesterhelt, and N. A. Dencher. 1994. Proton migration along the membrane surface and retarded surface to bulk transfer. Nature. 379:379-382.
    • (1994) Nature , vol.379 , pp. 379-382
    • Heberle, J.1    Riesle, J.2    Thiedemann, G.3    Oesterhelt, D.4    Dencher, N.A.5
  • 19
    • 0000910683 scopus 로고
    • Primary charge motion and light-energy transduction in bacteriorhodopsin
    • Keszthelyi, L. 1988. Primary charge motion and light-energy transduction in bacteriorhodopsin. Biophys. Chem. 29:127-136.
    • (1988) Biophys. Chem. , vol.29 , pp. 127-136
    • Keszthelyi, L.1
  • 20
    • 0024335154 scopus 로고
    • Protein electric response signals from dielectrically polarized systems
    • Keszthelyi, L., and P. Ormos. 1989. Protein electric response signals from dielectrically polarized systems. J. Membr. Biol. 109:193-200.
    • (1989) J. Membr. Biol. , vol.109 , pp. 193-200
    • Keszthelyi, L.1    Ormos, P.2
  • 21
    • 0021396558 scopus 로고
    • Anisotropic electric properties of purple membrane and their change during the photoreaction cycle
    • Kimura, Y., M. Fujiwara, and A. Ikegami. 1984. Anisotropic electric properties of purple membrane and their change during the photoreaction cycle. Biophys. J. 45:615-625.
    • (1984) Biophys. J. , vol.45 , pp. 615-625
    • Kimura, Y.1    Fujiwara, M.2    Ikegami, A.3
  • 22
    • 0025880477 scopus 로고
    • Effect of pH buffer molecules on the light-induced currents from oriented purple membrane
    • Liu, S. Y., M. Kono, and T. G. Ebrey. 1991. Effect of pH buffer molecules on the light-induced currents from oriented purple membrane. Biophys. J. 60:204-216.
    • (1991) Biophys. J. , vol.60 , pp. 204-216
    • Liu, S.Y.1    Kono, M.2    Ebrey, T.G.3
  • 23
    • 0023664492 scopus 로고
    • Counterion collapse and the effect of diamines on bacteriorhodopsin
    • Marinetti, T. 1987. Counterion collapse and the effect of diamines on bacteriorhodopsin. FEBS Lett. 216:155-158.
    • (1987) FEBS Lett. , vol.216 , pp. 155-158
    • Marinetti, T.1
  • 24
    • 0029744105 scopus 로고    scopus 로고
    • Protonation dynamics of the extracellular and cytoplasmic surface of bacteriorhodopsin in the purple membrane
    • Nachliel, E., M. Gutman, S. Kiryati, and N. A. Dencher. 1996. Protonation dynamics of the extracellular and cytoplasmic surface of bacteriorhodopsin in the purple membrane. Proc. Natl. Acad. Sci. USA. 93: 10747-10752.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10747-10752
    • Nachliel, E.1    Gutman, M.2    Kiryati, S.3    Dencher, N.A.4
  • 25
    • 0016376428 scopus 로고
    • Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane
    • Oesterhelt, D., and W. Stoeckenius. 1974. Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane. Methods. Enzymol. 31:667-678.
    • (1974) Methods. Enzymol. , vol.31 , pp. 667-678
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 26
    • 0032492706 scopus 로고    scopus 로고
    • The role of Glu204 in the proton release pathway
    • Rammelsberg, R., G. Huhn, R. Lübben, and K. Gerwert. 1998. The role of Glu204 in the proton release pathway. Biochemistry. 37:5001-5009.
    • (1998) Biochemistry , vol.37 , pp. 5001-5009
    • Rammelsberg, R.1    Huhn, G.2    Lübben, R.3    Gerwert, K.4
  • 27
    • 0030010796 scopus 로고    scopus 로고
    • D38 is an essential part of the proton translocation pathway in bacteriorhodopsin
    • Riesle, J., D. Oesterhelt, N. A. Dencher, and J. Heberle. 1996. D38 is an essential part of the proton translocation pathway in bacteriorhodopsin. Biochemistry. 35:6635-6643.
    • (1996) Biochemistry , vol.35 , pp. 6635-6643
    • Riesle, J.1    Oesterhelt, D.2    Dencher, N.A.3    Heberle, J.4
  • 28
    • 0033401014 scopus 로고    scopus 로고
    • Buffer effect on the photoelectrochemical response of bacteriorhodopsin
    • Saga, Y., T. Watanabe, K. Koyama, and T. Mayasaka. 1999. Buffer effect on the photoelectrochemical response of bacteriorhodopsin. Anal. Sci. 15:365-369.
    • (1999) Anal. Sci. , vol.15 , pp. 365-369
    • Saga, Y.1    Watanabe, T.2    Koyama, K.3    Mayasaka, T.4
  • 29
    • 0022489333 scopus 로고
    • Diamines reverse the direction of the bacteriorhodopsin proton pump
    • Tóth-Boconádi, R., S. G. Hristova, and L. Keszthelyi. 1986. Diamines reverse the direction of the bacteriorhodopsin proton pump. FEBS Lett. 195:164-168.
    • (1986) FEBS Lett. , vol.195 , pp. 164-168
    • Tóth-Boconádi, R.1    Hristova, S.G.2    Keszthelyi, L.3
  • 30
    • 0025820289 scopus 로고
    • Thermodynamics and energy coupling in the bacteriorhodopsin photocycle
    • Váró, 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
    • Váró, G.1    Lanyi, J.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.