메뉴 건너뛰기




Volumn 125, Issue 2, 1999, Pages 270-276

Time-resolved measurements of photovoltage generation by bacteriorhodopsin and halorhodopsin adsorbed on a thin polymer film

Author keywords

Bacteriorhodopsin; Halobacteria; Halorhodopsin; Photocycle; Photovoltage

Indexed keywords

BACTERIORHODOPSIN; CHLORIDE; HALORHODOPSIN; POLYMER;

EID: 0032992449     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022283     Document Type: Article
Times cited : (15)

References (33)
  • 3
    • 0017839866 scopus 로고
    • Time resolution of the intermediate steps in the bacteriorhodopsin-linked electrogenesis
    • Drachev, L.A., Kaulen, A.D., Ostroumov, S.A., and Skulachev, V.P. (1978) Time resolution of the intermediate steps in the bacteriorhodopsin-linked electrogenesis. FEBS Lett. 87, 161-167
    • (1978) FEBS Lett. , vol.87 , pp. 161-167
    • Drachev, L.A.1    Kaulen, A.D.2    Ostroumov, S.A.3    Skulachev, V.P.4
  • 4
    • 0018392155 scopus 로고
    • Lipid-impregnated filters as a tool for studying the electric current-generating proteins
    • Drachev, L.A., Kaulen, A.D., Semenov, A. Yu., Severina, I.I., and Skulachev, V.P. (1979) Lipid-Impregnated filters as a tool for studying the electric current-generating proteins. Anal. Biochem. 96, 250-262
    • (1979) Anal. Biochem. , vol.96 , pp. 250-262
    • Drachev, L.A.1    Kaulen, A.D.2    Semenov, A.Yu.3    Severina, I.I.4    Skulachev, V.P.5
  • 5
    • 85025567406 scopus 로고
    • Distributed kinetics of the charge movements in bacteriorhodopsin: Evidence for conformational substates
    • Holz, M., Lindau, M., and Heyn, M.P. (1988) Distributed kinetics of the charge movements in bacteriorhodopsin: Evidence for conformational substates. Biophys. J. 88, 623-633
    • (1988) Biophys. J. , vol.88 , pp. 623-633
    • Holz, M.1    Lindau, M.2    Heyn, M.P.3
  • 6
    • 0019589865 scopus 로고
    • Fast stages of photoelectric processes in biological membranes. I. Bacteriorhodopsin
    • Drachev, L.A., Kaulen, A.D., Khitrina, L.V., and Skulachev, V.P. (1981) Fast stages of photoelectric processes in biological membranes. I. Bacteriorhodopsin. Eur. J. Biochem. 117, 461-470
    • (1981) Eur. J. Biochem. , vol.117 , pp. 461-470
    • Drachev, L.A.1    Kaulen, A.D.2    Khitrina, L.V.3    Skulachev, V.P.4
  • 7
    • 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., Drachev, L.A., Mogi, T., Otto, H., Kaulen, A.D., Heyn, M.P., Skulachev, V.P., and Khorana, H.G. (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
  • 8
    • 0024317089 scopus 로고
    • Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsin
    • Otto, H., Marti, T., Holz, M., Mogi, T., Lindau, M., Khorana, H.G., and Heyn, M.P. (1989) Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsin. Proc. Natl. Acad. Sci. USA 86, 9228-9232
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9228-9232
    • Otto, H.1    Marti, T.2    Holz, M.3    Mogi, T.4    Lindau, M.5    Khorana, H.G.6    Heyn, M.P.7
  • 9
    • 0024707259 scopus 로고
    • Role of aspartate-96 in proton translocation by bacteriorhodopsin
    • Gerwert, K., Hess, B., Soppa, J., and Oesterhelt, D. (1989) Role of aspartate-96 in proton translocation by bacteriorhodopsin. Proc. Natl. Acad. Sci. USA 86, 4943-4947
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 4943-4947
    • Gerwert, K.1    Hess, B.2    Soppa, J.3    Oesterhelt, D.4
  • 10
    • 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., Marti, T., Holz, M., Mogi, T., Stern, L.J., Engel, F., Khorana, H.G., and Heyn, M.P. (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
  • 11
    • 0029610070 scopus 로고
    • Proton transport by a bacteriorhodopsin mutant, aspartic acid-85→asparagine, initiated in the unprotonated Schiff base state
    • Dickopf, S., Alexiev, U., Krebs, M.P., Otto, H., Mollaaghhaababa, R., Khorana, H.G., and Heyn, M.P. (1995) Proton transport by a bacteriorhodopsin mutant, aspartic acid-85→asparagine, initiated in the unprotonated Schiff base state. Proc. Natl. Acad. Sci. USA 92, 11519-11523
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11519-11523
    • Dickopf, S.1    Alexiev, U.2    Krebs, M.P.3    Otto, H.4    Mollaaghhaababa, R.5    Khorana, H.G.6    Heyn, M.P.7
  • 13
    • 0032546920 scopus 로고    scopus 로고
    • Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution
    • Luecke, H., Richter, H.-T., and Lanyi, J.K. (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
  • 14
    • 0025304015 scopus 로고
    • Halorhodopsin, a light-driven electrogenic chloride-transport system
    • Lanyi, J.K. (1990) Halorhodopsin, a light-driven electrogenic chloride-transport system. Physiol. Rev. 70, 319-330
    • (1990) Physiol. Rev. , vol.70 , pp. 319-330
    • Lanyi, J.K.1
  • 15
    • 85005560634 scopus 로고
    • Structure and function of halorhodopsin
    • Oesterhelt, D. (1995) Structure and function of halorhodopsin. Isr. J. Chem. 35, 475-494
    • (1995) Isr. J. Chem. , vol.35 , pp. 475-494
    • Oesterhelt, D.1
  • 16
    • 0002282747 scopus 로고
    • Reconstitution of the light-driven electrogenic ion pump halorhodopsin in black lipid membranes
    • Bamberg, E., Hegemann, P., and Oesterhelt, D. (1984) Reconstitution of the light-driven electrogenic ion pump halorhodopsin in black lipid membranes. Biochim. Biophys. Acta 773, 53-60
    • (1984) Biochim. Biophys. Acta , vol.773 , pp. 53-60
    • Bamberg, E.1    Hegemann, P.2    Oesterhelt, D.3
  • 17
  • 18
    • 0027531526 scopus 로고
    • Light-driven proton or chloride pumping by halorhodopsin
    • Bamberg, E., Tittor, J., and Oesterhelt, D. (1993) Light-driven proton or chloride pumping by halorhodopsin. Proc. Natl. Acad. Sci. USA 90, 639-643
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 639-643
    • Bamberg, E.1    Tittor, J.2    Oesterhelt, D.3
  • 19
    • 0032079347 scopus 로고    scopus 로고
    • Flash-induced voltage changes in halorhodopsin from Natronobacterium pharaonis
    • Kalaidzidis, I.V., Kalaidzidis, Y.L., and Kaulen, A.D. (1998) Flash-induced voltage changes in halorhodopsin from Natronobacterium pharaonis. FEBS Lett. 427, 59-63
    • (1998) FEBS Lett. , vol.427 , pp. 59-63
    • Kalaidzidis, I.V.1    Kalaidzidis, Y.L.2    Kaulen, A.D.3
  • 21
    • 0028869129 scopus 로고
    • Light-driven chloride ion transport by halorhodopsin from Natronobacterium pharaonis. 1. The photochemical cycle
    • Váró, G., Brown, L.S., Sasaki, J., Kandori, H., Maeda, A., Needleman, R., and Lanyi, J.K. (1995) Light-driven chloride ion transport by halorhodopsin from Natronobacterium pharaonis. 1. The photochemical cycle. Biochemistry 34, 14490-14499
    • (1995) Biochemistry , vol.34 , pp. 14490-14499
    • Váró, G.1    Brown, L.S.2    Sasaki, J.3    Kandori, H.4    Maeda, A.5    Needleman, R.6    Lanyi, J.K.7
  • 22
    • 0028808334 scopus 로고
    • Light-driven chloride ion transport by halorhodopsin from Natronobacterium pharaonis. 2. Chloride release and uptake, protein conformation change, and thermodynamics
    • Váró, G., Needleman, R., and Lanyi, J.K. (1995) Light-driven chloride ion transport by halorhodopsin from Natronobacterium pharaonis. 2. Chloride release and uptake, protein conformation change, and thermodynamics. Biochemistry 34, 14500-14507
    • (1995) Biochemistry , vol.34 , pp. 14500-14507
    • Váró, G.1    Needleman, R.2    Lanyi, J.K.3
  • 23
    • 0032080017 scopus 로고    scopus 로고
    • A new system for the measurement of electrogenicity produced by ion pumps using a thin polymer film: Examination of wild type bR and the D96N mutant over a wide pH range
    • Muneyuki, E., Okuno, D., Yoshida, M., Ikai, A., and Arakawa, H. (1998) A new system for the measurement of electrogenicity produced by ion pumps using a thin polymer film: Examination of wild type bR and the D96N mutant over a wide pH range. FEBS Lett. 427, 109-114
    • (1998) FEBS Lett. , vol.427 , pp. 109-114
    • Muneyuki, E.1    Okuno, D.2    Yoshida, M.3    Ikai, A.4    Arakawa, H.5
  • 24
    • 0000790347 scopus 로고    scopus 로고
    • H+ dependency of proton translocation by bacteriorhodopsin and a stochastic energization-relaxation channel model
    • H+ dependency of proton translocation by bacteriorhodopsin and a stochastic energization-relaxation channel model. J. Phys. Chem. 100, 19687-19691
    • (1996) J. Phys. Chem. , vol.100 , pp. 19687-19691
    • Muneyuki, E.1    Ikematsu, M.2    Yoshida, M.3
  • 25
    • 0016376428 scopus 로고
    • Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane
    • Oesterhelt, D. and Stoeckenius, W. (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
    • 84989725879 scopus 로고
    • Laser photolysis of the purple membrane of Halobacterium halobium in the photostationary state: The photobranching process from O640 intermediate
    • Ohtani, H., Naramoto, S., and Yamamoto, N. (1994) Laser photolysis of the purple membrane of Halobacterium halobium in the photostationary state: the photobranching process from O640 intermediate. Photochem. Photobiol. 60, 394-398
    • (1994) Photochem. Photobiol. , vol.60 , pp. 394-398
    • Ohtani, H.1    Naramoto, S.2    Yamamoto, N.3
  • 27
    • 0039355490 scopus 로고    scopus 로고
    • Specific arginine and threonine residues control anion binding and transport in the light-driven chloride pump halorhodopsin
    • Rüdiger, M. and Oesterhelt, D. (1997) Specific arginine and threonine residues control anion binding and transport in the light-driven chloride pump halorhodopsin. EMBO J. 16, 3813-3821
    • (1997) EMBO J. , vol.16 , pp. 3813-3821
    • Rüdiger, M.1    Oesterhelt, D.2
  • 28
    • 0031982562 scopus 로고    scopus 로고
    • Voltage dependence of proton pumping by bacteriorhodopsin is regulated by the voltage-sensitive ratio of M1 to M2
    • Nagel, G., Kelety, B., Möckel, B., Büldt, G., and Bamberg, E. (1998) Voltage dependence of proton pumping by bacteriorhodopsin is regulated by the voltage-sensitive ratio of M1 to M2. Biophys. J. 74, 403-412
    • (1998) Biophys. J. , vol.74 , pp. 403-412
    • Nagel, G.1    Kelety, B.2    Möckel, B.3    Büldt, G.4    Bamberg, E.5
  • 29
    • 0027050450 scopus 로고
    • Resonance Raman study of halorhodopsin photocycle kinetics, chromophore structure, and chloride-pumping mechanism
    • Ames, J.B., Raap, J., Lugtenburg, J., and Mathies, R.A. (1992) Resonance Raman study of halorhodopsin photocycle kinetics, chromophore structure, and chloride-pumping mechanism. Biochemistry 31, 12546-12554
    • (1992) Biochemistry , vol.31 , pp. 12546-12554
    • Ames, J.B.1    Raap, J.2    Lugtenburg, J.3    Mathies, R.A.4
  • 30
    • 0028285064 scopus 로고
    • Anion-protein interactions during halorhodopsin pumping: Halide binding at the protonated Schiff base
    • Walter, T.J. and Braiman, M.S. (1994) Anion-protein interactions during halorhodopsin pumping: halide binding at the protonated Schiff base. Biochemistry 33, 1724-1733
    • (1994) Biochemistry , vol.33 , pp. 1724-1733
    • Walter, T.J.1    Braiman, M.S.2
  • 31
    • 0023049947 scopus 로고
    • Electrostatic interaction between anions bound to site I and the retinal Schiff base of halorhodopsin
    • Schobert, B. and Lanyi, J.K. (1986) Electrostatic interaction between anions bound to site I and the retinal Schiff base of halorhodopsin. Biochemistry 25, 4163-4167
    • (1986) Biochemistry , vol.25 , pp. 4163-4167
    • Schobert, B.1    Lanyi, J.K.2
  • 32
    • 0024515846 scopus 로고
    • Effects of various anions on the Raman spectrum of halorhodopsin
    • Pande, C., Lanyi, J.K., and Callender, R.H. (1989) Effects of various anions on the Raman spectrum of halorhodopsin. Biophys. J. 55, 425-431
    • (1989) Biophys. J. , vol.55 , pp. 425-431
    • Pande, C.1    Lanyi, J.K.2    Callender, R.H.3
  • 33
    • 0028223284 scopus 로고
    • Infrared spectroscopic detection of light-induced change in chloride arginine interaction in halorhodopsin
    • Braiman, M.S., Walter, T.J., and Briercheck, D.M. (1994) Infrared spectroscopic detection of light-induced change in chloride arginine interaction in halorhodopsin. Biochemistry 33, 1629-1635
    • (1994) Biochemistry , vol.33 , pp. 1629-1635
    • Braiman, M.S.1    Walter, T.J.2    Briercheck, D.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.