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Volumn 271, Issue 3, 1997, Pages 405-416

Chloride and proton transport in bacteriorhodopsin mutant D85T: Different modes of ion translocation in a retinal protein

Author keywords

Chloride pump; Proton pump; Vectorial transport

Indexed keywords

BACTERIORHODOPSIN; CHLORIDE; MUTANT PROTEIN; PROTON; PROTON PUMP;

EID: 0031583474     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1204     Document Type: Article
Times cited : (70)

References (54)
  • 2
    • 0000825539 scopus 로고
    • The chromoprotein of halorhodopsin is the light-driven chloride pump inHalobacterium halobium
    • Bamberg E., Hegemann P., Oesterhelt D. The chromoprotein of halorhodopsin is the light-driven chloride pump inHalobacterium halobium. Biochemistry. 23:1986;6216-6221.
    • (1986) Biochemistry , vol.23 , pp. 6216-6221
    • Bamberg, E.1    Hegemann, P.2    Oesterhelt, D.3
  • 6
    • 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., Mogi T., Marti T., Stern L., Khorana H. G., Rothschild K. Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96 and 212. Biochemistry. 27:1988;8516-8520.
    • (1988) Biochemistry , vol.27 , pp. 8516-8520
    • Braiman, M.1    Mogi, T.2    Marti, T.3    Stern, L.4    Khorana, H.G.5    Rothschild, K.6
  • 7
    • 0344335730 scopus 로고
    • Aspartic acid 96 and 85 play a central role in the function of bacteriorhodopsin as a proton pump
    • Butt H. J., Fendler K., Bamberg E., Tittor J., Oesterhelt D. Aspartic acid 96 and 85 play a central role in the function of bacteriorhodopsin as a proton pump. EMBO J. 8:1989;1675-1663.
    • (1989) EMBO J. , vol.8 , pp. 1675-1663
    • Butt, H.J.1    Fendler, K.2    Bamberg, E.3    Tittor, J.4    Oesterhelt, D.5
  • 8
    • 0029828763 scopus 로고    scopus 로고
    • Hydration of the counterion of the Schiff base in the chloride-transporting mutant of bacteriorhodopsin: FTIR and FT-Raman studies of the effects of anion binding when Asp85 is replaced with a neutral residue
    • Chon Y.-S., Sasaki J., Kandori H., Brown L., Lanyi J. K., Needleman R., Maeda A. Hydration of the counterion of the Schiff base in the chloride-transporting mutant of bacteriorhodopsin: FTIR and FT-Raman studies of the effects of anion binding when Asp85 is replaced with a neutral residue. Biochemistry. 35:1996;14244-14250.
    • (1996) Biochemistry , vol.35 , pp. 14244-14250
    • Chon, Y.-S.1    Sasaki, J.2    Kandori, H.3    Brown, L.4    Lanyi, J.K.5    Needleman, R.6    Maeda, A.7
  • 13
    • 0027536538 scopus 로고
    • Homologous bacterioopsin-encoding gene expression via site-specific vector integration
    • Ferrando E., Schweiger U., Oesterhelt D. Homologous bacterioopsin-encoding gene expression via site-specific vector integration. Gene. 125:1993;41-47.
    • (1993) Gene , vol.125 , pp. 41-47
    • Ferrando, E.1    Schweiger, U.2    Oesterhelt, D.3
  • 14
    • 0018635144 scopus 로고
    • Chromophore equilibra in bacteriorhodopsin
    • Fischer U., Oesterhelt D. Chromophore equilibra in bacteriorhodopsin. Biophys. J. 28:1979;211-230.
    • (1979) Biophys. J. , vol.28 , pp. 211-230
    • Fischer, U.1    Oesterhelt, D.2
  • 15
    • 0024707259 scopus 로고
    • The role of aspartate 96 in proton translocation by bacteriorhodopsin
    • Gerwert K., Hess B., Soppa J., Oesterhelt D. The role of aspartate 96 in proton translocation by bacteriorhodopsin. Proc. Natl Acad. Sci. USA. 86:1989;2167-2171.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 2167-2171
    • Gerwert, K.1    Hess, B.2    Soppa, J.3    Oesterhelt, D.4
  • 17
    • 0029069269 scopus 로고
    • The photoreceptor sensory rhodopsin I as a two-photon-driven pump
    • Haupts U., Haupts Ch., Oesterhelt D. the photoreceptor sensory rhodopsin I as a two-photon-driven pump. Proc. Natl Acad. Sci. USA. 92:1995;3834-3838.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 3834-3838
    • Haupts, U.1    Haupts, Ch.2    Oesterhelt, D.3
  • 18
    • 0029926580 scopus 로고    scopus 로고
    • Different modes of proton translocation by sensory rhodopsin I
    • Haupts U., Bamberg E., Oesterhelt D. Different modes of proton translocation by sensory rhodopsin I. EMBO J. 15:1996;1834-1841.
    • (1996) EMBO J. , vol.15 , pp. 1834-1841
    • Haupts, U.1    Bamberg, E.2    Oesterhelt, D.3
  • 19
    • 0031021374 scopus 로고    scopus 로고
    • General concept for ion translocation by halobacterial proteins: The IST-model
    • Haupts U., Tittor J., Bamberg E., Oesterhelt D. General concept for ion translocation by halobacterial proteins: The IST-model. Biochemistry. 36:1997;2-7.
    • (1997) Biochemistry , vol.36 , pp. 2-7
    • Haupts, U.1    Tittor, J.2    Bamberg, E.3    Oesterhelt, D.4
  • 20
    • 0028959025 scopus 로고
    • Three-dimensional structure of halorhodopsin at 7 Å resolution
    • Havelka W., Henderson R., Oesterhelt D. Three-dimensional structure of halorhodopsin at 7 Å resolution. J. Mol. Biol. 247:1995;726-738.
    • (1995) J. Mol. Biol. , vol.247 , pp. 726-738
    • Havelka, W.1    Henderson, R.2    Oesterhelt, D.3
  • 21
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson R., Baldwin J., Ceska T., Zemlin F., Beckmann F., Downing K. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 213:1990;899-929.
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.2    Ceska, T.3    Zemlin, F.4    Beckmann, F.5    Downing, K.6
  • 22
    • 0031041820 scopus 로고    scopus 로고
    • Photoproducts of bacteriorhodopsin mutants: A molecular dynamics study
    • Humphrey W., Bamberg E., Schulten K. Photoproducts of bacteriorhodopsin mutants: a molecular dynamics study. Biophys. J. 72:1997;1347-1356.
    • (1997) Biophys. J. , vol.72 , pp. 1347-1356
    • Humphrey, W.1    Bamberg, E.2    Schulten, K.3
  • 23
    • 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., Mogi T., Otto H., Kaulen A., Heyn M. P., Skulachev V. P., Khorana H. G. 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. 86:1989;2167-2171.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 2167-2171
    • Holz, M.1    Drachev, L.2    Mogi, T.3    Otto, H.4    Kaulen, A.5    Heyn, M.P.6    Skulachev, V.P.7    Khorana, H.G.8
  • 24
    • 0030561197 scopus 로고    scopus 로고
    • Electrospray ionization mass spectroscopy of genetically and chemically modified bacteriorhodopsins
    • Hufnagel P., Schweiger U., Eckerskorn C, Oesterhelt D. Electrospray ionization mass spectroscopy of genetically and chemically modified bacteriorhodopsins. Anal. Biochem. 243:1996;46-54.
    • (1996) Anal. Biochem. , vol.243 , pp. 46-54
    • Hufnagel, P.1    Schweiger, U.2    Eckerskorn, C.3    Oesterhelt, D.4
  • 27
    • 0025976082 scopus 로고
    • Time-resolved X-ray diffraction study of structural changes associated with the photocycle of bacteriorhodopsin
    • Koch M., Dencher N., Oesterhelt D., Plöhn H.-J., Büldt G. Time-resolved X-ray diffraction study of structural changes associated with the photocycle of bacteriorhodopsin. EMBO J. 10:1991;521-526.
    • (1991) EMBO J. , vol.10 , pp. 521-526
    • Koch, M.1    Dencher, N.2    Oesterhelt, D.3    Plöhn, H.-J.4    Büldt, G.5
  • 28
    • 0027769837 scopus 로고
    • Proton translocation mechanism and energetics in the light-driven pump bacteriorhodopsin
    • Lanyi J. K. Proton translocation mechanism and energetics in the light-driven pump bacteriorhodopsin. Biochim. Biophys. Acta. 1183:1993;241-246.
    • (1993) Biochim. Biophys. Acta , vol.1183 , pp. 241-246
    • Lanyi, J.K.1
  • 29
    • 0026557012 scopus 로고
    • Influence of the size and protonation state of acidic residue 85 on the absorption spectrum and photoreaction of the bacteriorhodopsin chromophore
    • Lanyi J. K., Tittor J., Varo G., Krippahl G., Oesterhelt D. Influence of the size and protonation state of acidic residue 85 on the absorption spectrum and photoreaction of the bacteriorhodopsin chromophore. Biochim. Biophys. Acta. 1099:1992;102-110.
    • (1992) Biochim. Biophys. Acta , vol.1099 , pp. 102-110
    • Lanyi, J.K.1    Tittor, J.2    Varo, G.3    Krippahl, G.4    Oesterhelt, D.5
  • 30
    • 0021886417 scopus 로고
    • Resonance Raman study on binding of chloride to the chromophore of halorhodopsin
    • Maeda A., Ogurusu T., Yoshizawa T., Kitagawa T. Resonance Raman study on binding of chloride to the chromophore of halorhodopsin. Biochemistry. 24:1985;2517-2521.
    • (1985) Biochemistry , vol.24 , pp. 2517-2521
    • Maeda, A.1    Ogurusu, T.2    Yoshizawa, T.3    Kitagawa, T.4
  • 31
    • 0026059269 scopus 로고
    • The retinylidene Schiff base counterion in bacteriorhodopsin
    • Marti T., Rösselet S., Otto H., Heyn M., Khorana G. The retinylidene Schiff base counterion in bacteriorhodopsin. J. Biol. Chem. 266:1991;18674-18683.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18674-18683
    • Marti, T.1    Rösselet, S.2    Otto, H.3    Heyn, M.4    Khorana, G.5
  • 32
    • 0026786078 scopus 로고
    • Anion binding to the Schiff base of the bacteriorhodopsin mutants asp85→asn/asp212→asn and arg82→gln/asp85→asn/asp212→asn
    • Marti T., Otto H., Rösselet S., Heyn M., Khorana G. Anion binding to the Schiff base of the bacteriorhodopsin mutants asp85→asn/asp212→asn and arg82→gln/asp85→asn/asp212→asn. J. Biol. Chem. 267:1992;16922-16927.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16922-16927
    • Marti, T.1    Otto, H.2    Rösselet, S.3    Heyn, M.4    Khorana, G.5
  • 33
  • 34
    • 0029620915 scopus 로고
    • Protein conformational changes during the bacteriorhodopsin photocycle
    • Nilsson A., Rath P., Oleijnik J., Coleman M., Rothschild K. Protein conformational changes during the bacteriorhodopsin photocycle. J. Biol. Chem. 270:1995;29746-29751.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29746-29751
    • Nilsson, A.1    Rath, P.2    Oleijnik, J.3    Coleman, M.4    Rothschild, K.5
  • 35
    • 85005560634 scopus 로고
    • Structure and function of halorhodopsin
    • Oesterhelt D. Structure and function of halorhodopsin. Isr. J. Chem. 35:1995;475-494.
    • (1995) Isr. J. Chem. , vol.35 , pp. 475-494
    • Oesterhelt, D.1
  • 36
    • 0016376428 scopus 로고
    • Isolation of the cell membrane ofHalobacterium halobium
    • Oesterhelt D., Stoeckenius W. Isolation of the cell membrane ofHalobacterium halobium. Methods Enzyme. 31:1974;667-678.
    • (1974) Methods Enzyme. , vol.31 , pp. 667-678
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 37
    • 0026623260 scopus 로고
    • A unifying concept for ion translocation by retinal proteins
    • Oesterhelt D., Tittor J., Bamberg E. A unifying concept for ion translocation by retinal proteins. J. Bioener. Biomemb. 24:1992;181-191.
    • (1992) J. Bioener. Biomemb. , vol.24 , pp. 181-191
    • Oesterhelt, D.1    Tittor, J.2    Bamberg, E.3
  • 38
    • 0029586467 scopus 로고
    • Over-expression of a new photo-active halorhodopsin in Halobacterium salinarum
    • Otomo J., Muramatsu T. Over-expression of a new photo-active halorhodopsin in Halobacterium salinarum. Biochim. Biophys. Acta. 1240:1995;248-256.
    • (1995) Biochim. Biophys. Acta , vol.1240 , pp. 248-256
    • Otomo, J.1    Muramatsu, T.2
  • 39
    • 0027171130 scopus 로고
    • Hydrogen bonding interactions with the Schiff base of bacteriorhodopsin
    • Rath P., Marti T., Sonar S., Khorana G, Rothschild K. Hydrogen bonding interactions with the Schiff base of bacteriorhodopsin. J. Biol. Chem. 268:1993;17742-17749.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17742-17749
    • Rath, P.1    Marti, T.2    Sonar, S.3    Khorana, G.4    Rothschild, K.5
  • 40
    • 0030010796 scopus 로고    scopus 로고
    • D38 is an essential part of the proton translocation pathway in bacteriorhodopsin
    • Riesle J., Oesterhelt D., Dencher N. A., Heberle J. D38 is an essential part of the proton translocation pathway in bacteriorhodopsin. Biochemistry. 35:1996;6635-6643.
    • (1996) Biochemistry , vol.35 , pp. 6635-6643
    • Riesle, J.1    Oesterhelt, D.2    Dencher, N.A.3    Heberle, J.4
  • 41
    • 0029040316 scopus 로고
    • Chemical reconstitution of a chloride pump inactivated by a single point mutation
    • Rüdiger M., Haupts U., Gerwert K., Oesterhelt D. Chemical reconstitution of a chloride pump inactivated by a single point mutation. EMBO J. 14:1995;1599-1606.
    • (1995) EMBO J. , vol.14 , pp. 1599-1606
    • Rüdiger, M.1    Haupts, U.2    Gerwert, K.3    Oesterhelt, D.4
  • 42
    • 0343853021 scopus 로고    scopus 로고
    • Reconstitution of bacteriorhodopsin from the apoprotein and retinal studied by Fourier-transform infrared spectoscopy
    • Rüdiger M., Tittor J., Gerwert K., Oesterhelt D. Reconstitution of bacteriorhodopsin from the apoprotein and retinal studied by Fourier-transform infrared spectoscopy. Biochemistry. 36:1997;4867-4874.
    • (1997) Biochemistry , vol.36 , pp. 4867-4874
    • Rüdiger, M.1    Tittor, J.2    Gerwert, K.3    Oesterhelt, D.4
  • 44
    • 0028286154 scopus 로고
    • Blue halorhodopsin fromNatronobacterium pharaonis
    • Scharf B., Engelhard M. Blue halorhodopsin fromNatronobacterium pharaonis. Biochemistry. 33:1994;6387-6393.
    • (1994) Biochemistry , vol.33 , pp. 6387-6393
    • Scharf, B.1    Engelhard, M.2
  • 45
    • 0023049947 scopus 로고
    • Electrostatic interaction between anions bound to site I and the retinal Schiff base of halorhodopsin
    • Schobert B., Lanyi J. K. Electrostatic interaction between anions bound to site I and the retinal Schiff base of halorhodopsin. Biochemistry. 25:1986;4163-4167.
    • (1986) Biochemistry , vol.25 , pp. 4163-4167
    • Schobert, B.1    Lanyi, J.K.2
  • 46
    • 85005653287 scopus 로고
    • Molecular dynamics studies of bacteriorhodopsin's photo cycles
    • Schulten K., Humphrey W., Logunov I., Sheves M., Xu D. Molecular dynamics studies of bacteriorhodopsin's photo cycles. Isr. J. Chem. 35:1995;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
  • 47
    • 0021341533 scopus 로고
    • Halide binding by the purified halorhodopsin chromophore
    • Steiner M., Oesterhelt D., Ariki M., Lanyi J. K. Halide binding by the purified halorhodopsin chromophore. J. Biol. Chem. 259:1984;2179-2184.
    • (1984) J. Biol. Chem. , vol.259 , pp. 2179-2184
    • Steiner, M.1    Oesterhelt, D.2    Ariki, M.3    Lanyi, J.K.4
  • 48
    • 0027439826 scopus 로고
    • Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin
    • Subramaniam S., Gerstein M., Oesterhelt D., Henderson R. Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin. EMBO J. 12:1993;1-8.
    • (1993) EMBO J. , vol.12 , pp. 1-8
    • Subramaniam, S.1    Gerstein, M.2    Oesterhelt, D.3    Henderson, R.4
  • 49
    • 0027999089 scopus 로고
    • Inversion of proton translocation in bacteriorhodopsin mutants D85N, D85T and D85,96N
    • Tittor J., Schweiger U., Oesterhelt D., Bamberg E. Inversion of proton translocation in bacteriorhodopsin mutants D85N, D85T and D85,96N. Biophys. J. 67:1994;1682-1690.
    • (1994) Biophys. J. , vol.67 , pp. 1682-1690
    • Tittor, J.1    Schweiger, U.2    Oesterhelt, D.3    Bamberg, E.4
  • 50
    • 0029160250 scopus 로고
    • Bacteriorhodopsin mutants D85N and D85,96N as proton pumps
    • Tittor J., Oesterhelt D., Bamberg E. Bacteriorhodopsin mutants D85N and D85,96N as proton pumps. Biophys. Chem. 56:1995;153-157.
    • (1995) Biophys. Chem. , vol.56 , pp. 153-157
    • Tittor, J.1    Oesterhelt, D.2    Bamberg, E.3
  • 53
    • 0024829218 scopus 로고
    • Photoreactions of bacteriorhodopsin at acid pH
    • Varo G., Lanyi J. Photoreactions of bacteriorhodopsin at acid pH. Biophys. J. 56:1989;1143-1151.
    • (1989) Biophys. J. , vol.56 , pp. 1143-1151
    • Varo, G.1    Lanyi, J.2


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