메뉴 건너뛰기




Volumn 43, Issue 11, 2004, Pages 3195-3203

Proton Release and Uptake of pharaonis Phoborhodopsin (Sensory Rhodopsin II) Reconstituted into Phospholipids

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; ELECTRODES; GROUND STATE; PH; PHOSPHOLIPIDS; PROTEINS; PROTONS;

EID: 1542743836     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi035960n     Document Type: Article
Times cited : (26)

References (50)
  • 1
    • 0026723610 scopus 로고
    • Photocycle of phoborhodopsin from haloalkaliphilic bacterium (Natronobacterium pharaonis) studied by low-temperature spectrophotometry
    • Hirayama, J., Imamoto, Y., Shichida, Y., Kamo, N., Tomioka, H., and Yoshizawa, T. (1992) Photocycle of phoborhodopsin from haloalkaliphilic bacterium (Natronobacterium pharaonis) studied by low-temperature spectrophotometry, Biochemistry 31, 2093-2098.
    • (1992) Biochemistry , vol.31 , pp. 2093-2098
    • Hirayama, J.1    Imamoto, Y.2    Shichida, Y.3    Kamo, N.4    Tomioka, H.5    Yoshizawa, T.6
  • 2
    • 0026583426 scopus 로고
    • Biochemical and photochemical properties of the photophobic receptors from Halobacterium halobium and Natronobacterium pharaonis
    • Scharf, B., Pevec, B., Hess, B., and Engelhard, M. (1992) Biochemical and photochemical properties of the photophobic receptors from Halobacterium halobium and Natronobacterium pharaonis, Eur. J. Biochem. 206, 359-366.
    • (1992) Eur. J. Biochem. , vol.206 , pp. 359-366
    • Scharf, B.1    Pevec, B.2    Hess, B.3    Engelhard, M.4
  • 3
    • 0031820941 scopus 로고    scopus 로고
    • The photophobic receptor from natronobacterium pharaonis: Temperature and pH dependencies of the photocycle of sensory rhodopsin II
    • Chizhov, I., Schmies, G., Seidel, R., Sydor, J. R., Lüttenberg, B., and Engelhard, M. (1998) The photophobic receptor from natronobacterium pharaonis: temperature and pH dependencies of the photocycle of sensory rhodopsin II, Biophys. J. 75, 999-1009.
    • (1998) Biophys. J. , vol.75 , pp. 999-1009
    • Chizhov, I.1    Schmies, G.2    Seidel, R.3    Sydor, J.R.4    Lüttenberg, B.5    Engelhard, M.6
  • 4
    • 0036667744 scopus 로고    scopus 로고
    • Sensory rhodopsin II: Functional insights from structure
    • Spudich, J. L., and Luecke, H. (2002) Sensory rhodopsin II: functional insights from structure, Curr. Opin. Struct. Biol. 12, 540-546.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 540-546
    • Spudich, J.L.1    Luecke, H.2
  • 6
    • 1542645230 scopus 로고    scopus 로고
    • Photochemical properties of pharaonis phoborhodopsin (sensory rhodopsin II)
    • Iwamoto, M., Kandori, H., and Kamo, N. (2003) Photochemical properties of pharaonis phoborhodopsin (sensory rhodopsin II), Recent Res. Dev. Chem. 1, 15-30.
    • (2003) Recent Res. Dev. Chem. , vol.1 , pp. 15-30
    • Iwamoto, M.1    Kandori, H.2    Kamo, N.3
  • 7
    • 0015244581 scopus 로고
    • Rhodopsin-like protein from the purple membrane of Halobacterium halobium
    • Oesterhelt, D., and Stoeckenius, W. (1971) Rhodopsin-like protein from the purple membrane of Halobacterium halobium, Nat. New Biol. 233, 149-152.
    • (1971) Nat. New Biol. , vol.233 , pp. 149-152
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 8
    • 0032987196 scopus 로고    scopus 로고
    • Closing in on bacteriorhodopsin: Progress in understanding the molecule
    • Haupts, U., Tittor, J., and Oesterhelt, D. (1999) Closing in on bacteriorhodopsin: progress in understanding the molecule, Annu. Rev. Biophys. Biomol. Struct. 28, 367-399.
    • (1999) Annu. Rev. Biophys. Biomol. Struct. , vol.28 , pp. 367-399
    • Haupts, U.1    Tittor, J.2    Oesterhelt, D.3
  • 9
    • 0037285261 scopus 로고    scopus 로고
    • Structural clues to the mechanism of ion pumping in bacteriorhodopsin
    • Luecke, H., and Lanyi, J. K. (2003) Structural clues to the mechanism of ion pumping in bacteriorhodopsin, Adv. Protein Chem. 63, 111-130.
    • (2003) Adv. Protein Chem. , vol.63 , pp. 111-130
    • Luecke, H.1    Lanyi, J.K.2
  • 10
    • 0017694434 scopus 로고
    • Two possible roles of bacteriorhodopsin; a comparative study of strains of Halobacterium halobium differing in pigmentation
    • Matsuno-Yagi, A., and Mukohata, Y. (1977) Two possible roles of bacteriorhodopsin; a comparative study of strains of Halobacterium halobium differing in pigmentation, Biochem. Biophys. Res. Commun. 78, 237-243.
    • (1977) Biochem. Biophys. Res. Commun. , vol.78 , pp. 237-243
    • Matsuno-Yagi, A.1    Mukohata, Y.2
  • 11
    • 0342484454 scopus 로고    scopus 로고
    • Analogies between halorhodopsin and bacteriorhodopsin
    • Varo, G. (2000) Analogies between halorhodopsin and bacteriorhodopsin, Biochim. Biophys. Acta 1460, 220-229.
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 220-229
    • Varo, G.1
  • 12
    • 0036667739 scopus 로고    scopus 로고
    • Halorhodopsin: Light-driven ion pumping made simple?
    • Essen, L. O. (2002) Halorhodopsin: light-driven ion pumping made simple?, Curr. Opin. Struct. Biol. 12, 516-522.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 516-522
    • Essen, L.O.1
  • 13
    • 0000373165 scopus 로고
    • Identification of a third rhodopsin-like pigment in phototactic Halobacterium halobium
    • Bogomolni, R. A., and Spudich, J. L. (1982) Identification of a third rhodopsin-like pigment in phototactic Halobacterium halobium, Proc. Natl. Acad. Sci. U.S.A. 79, 6250-6254.
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 6250-6254
    • Bogomolni, R.A.1    Spudich, J.L.2
  • 14
    • 0030906654 scopus 로고    scopus 로고
    • Molecular mechanism of photosignaling by archaeal sensory rhodopsins
    • Hoff, W. D., Jung, K. H., and Spudich, J. L. (1997) Molecular mechanism of photosignaling by archaeal sensory rhodopsins, Annu. Rev. Biophys. Biomol. Struct. 26, 223-258.
    • (1997) Annu. Rev. Biophys. Biomol. Struct. , vol.26 , pp. 223-258
    • Hoff, W.D.1    Jung, K.H.2    Spudich, J.L.3
  • 15
    • 0031583910 scopus 로고    scopus 로고
    • Functional expression of pharaonis phoborhodopsin in Escherichia coli
    • Shimono, K., Iwamoto, M., Sumi, M., and Kamo, N. (1997) Functional expression of pharaonis phoborhodopsin in Escherichia coli, FEBS Lett. 420, 54-56.
    • (1997) FEBS Lett. , vol.420 , pp. 54-56
    • Shimono, K.1    Iwamoto, M.2    Sumi, M.3    Kamo, N.4
  • 16
    • 0035943457 scopus 로고    scopus 로고
    • Crystal structure of sensory rhodopsin II at 2.4 angstroms: Insights into color tuning and transducer interaction
    • Luecke, H., Schobert, B., Lanyi, J. K., Spudich, E. N., and Spudich, J. L. (2001) Crystal structure of sensory rhodopsin II at 2.4 angstroms: insights into color tuning and transducer interaction, Science 293, 1499-1503.
    • (2001) Science , vol.293 , pp. 1499-1503
    • Luecke, H.1    Schobert, B.2    Lanyi, J.K.3    Spudich, E.N.4    Spudich, J.L.5
  • 19
    • 0036927590 scopus 로고    scopus 로고
    • FTIR spectroscopy of the M photointermediate in pharaonis phoborhodopsin
    • Furutani, Y., Iwamoto, M., Shimono, K., Kamo, N., and Kandori, H. (2002) FTIR spectroscopy of the M photointermediate in pharaonis phoborhodopsin, Biophys. J. 83, 3482-3489.
    • (2002) Biophys. J. , vol.83 , pp. 3482-3489
    • Furutani, Y.1    Iwamoto, M.2    Shimono, K.3    Kamo, N.4    Kandori, H.5
  • 20
    • 0346034956 scopus 로고    scopus 로고
    • Proton-transfer reactions in the F86D and F86E mutants of pharaonis phoborhodopsin (sensory rhodopsin II)
    • Iwamoto, M., Furutani, Y., Kamo, N., and Kandori, H. (2003) Proton-transfer reactions in the F86D and F86E mutants of pharaonis phoborhodopsin (sensory rhodopsin II), Biochemistry 42, 2790-2796.
    • (2003) Biochemistry , vol.42 , pp. 2790-2796
    • Iwamoto, M.1    Furutani, Y.2    Kamo, N.3    Kandori, H.4
  • 21
    • 0030597107 scopus 로고    scopus 로고
    • Protonation changes during the photocycle of sensory rhodopsin II from Natronobacterium pharaonis
    • Engelhard, M., Scharf, B., and Siebert, F. (1996) Protonation changes during the photocycle of sensory rhodopsin II from Natronobacterium pharaonis, FEBS Lett. 395, 195-198.
    • (1996) FEBS Lett. , vol.395 , pp. 195-198
    • Engelhard, M.1    Scharf, B.2    Siebert, F.3
  • 22
    • 0342979867 scopus 로고    scopus 로고
    • Sensory rhodopsin II from the haloalkaliphilic Natronobacterium pharaonis: Light-activated proton-transfer reaction
    • Schmies, G., Lüttenberg, B., Chizhov, I., Engelhard, M., Becker, A., and Bamberg, E. (2000) Sensory rhodopsin II from the haloalkaliphilic Natronobacterium pharaonis: light-activated proton-transfer reaction, Biophys. J. 78, 967-976.
    • (2000) Biophys. J. , vol.78 , pp. 967-976
    • Schmies, G.1    Lüttenberg, B.2    Chizhov, I.3    Engelhard, M.4    Becker, A.5    Bamberg, E.6
  • 23
    • 0035142193 scopus 로고    scopus 로고
    • Photo-induced proton transport of pharaonis phoborhodopsin (sensory rhodopsin II) is ceased by association with the transducer
    • Sudo, Y., Iwamoto, M., Shimono, K., Sumi, M., and Kamo, N. (2001) Photo-induced proton transport of pharaonis phoborhodopsin (sensory rhodopsin II) is ceased by association with the transducer, Biophys. J. 80, 916-922.
    • (2001) Biophys. J. , vol.80 , pp. 916-922
    • Sudo, Y.1    Iwamoto, M.2    Shimono, K.3    Sumi, M.4    Kamo, N.5
  • 24
    • 0035852672 scopus 로고    scopus 로고
    • Electrophysiological characterization of specific interactions between bacterial sensory rhodopsins and their transducers
    • Schmies, G., Engelhard, M., Wood, P. G., Nagel, G., and Bamberg, E. (2001) Electrophysiological characterization of specific interactions between bacterial sensory rhodopsins and their transducers, Proc. Natl. Acad. Sci. U.S.A. 98, 1555-1559.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 1555-1559
    • Schmies, G.1    Engelhard, M.2    Wood, P.G.3    Nagel, G.4    Bamberg, E.5
  • 25
    • 0000079289 scopus 로고    scopus 로고
    • Light-induced proton uptake and release of pharaonis phoborhodopsin detected by a photoelectrochemical cell
    • Iwamoto, M., Shimono, K., Sumi, M., Koyama, K., and Kamo, N. (1999) Light-induced proton uptake and release of pharaonis phoborhodopsin detected by a photoelectrochemical cell, J. Phys. Chem. B 103, 10311-10315.
    • (1999) J. Phys. Chem. B , vol.103 , pp. 10311-10315
    • Iwamoto, M.1    Shimono, K.2    Sumi, M.3    Koyama, K.4    Kamo, N.5
  • 26
    • 0028965178 scopus 로고
    • The primary structure of sensory rhodopsin II: A member of an additional retinal protein subgroup is coexpressed with its transducer, the halobacterial transducer of rhodopsin II
    • Seidel, R., Scharf, B., Gautel, M., Kleine, K., Oesterhelt, D., and Engelhard, M. (1995) The primary structure of sensory rhodopsin II: a member of an additional retinal protein subgroup is coexpressed with its transducer, the halobacterial transducer of rhodopsin II, Proc. Natl. Acad. Sci. U.S.A. 92, 3036-3040.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 3036-3040
    • Seidel, R.1    Scharf, B.2    Gautel, M.3    Kleine, K.4    Oesterhelt, D.5    Engelhard, M.6
  • 27
    • 0035470682 scopus 로고    scopus 로고
    • pharaonis phoborhodopsin binds to its cognate truncated transducer even in the presence of a detergent with a 1:1 stoichiometry
    • Sudo, Y., Iwamoto, M., Shimono, K., and Kamo, N. (2001) pharaonis phoborhodopsin binds to its cognate truncated transducer even in the presence of a detergent with a 1:1 stoichiometry, Photochem. Photobiol. 74, 489-494.
    • (2001) Photochem. Photobiol. , vol.74 , pp. 489-494
    • Sudo, Y.1    Iwamoto, M.2    Shimono, K.3    Kamo, N.4
  • 28
    • 0035822679 scopus 로고    scopus 로고
    • Structural changes of pharaonis phoborhodopsin upon photoisomerization of the retinal chromophore: Infrared spectral comparison with bacteriorhodopsin
    • Kandori, H., Shimono, K., Sudo, Y., Iwamoto, M., Shichida, Y., and Kamo, N. (2001) Structural changes of pharaonis phoborhodopsin upon photoisomerization of the retinal chromophore: infrared spectral comparison with bacteriorhodopsin, Biochemistry 40, 9238-9246.
    • (2001) Biochemistry , vol.40 , pp. 9238-9246
    • Kandori, H.1    Shimono, K.2    Sudo, Y.3    Iwamoto, M.4    Shichida, Y.5    Kamo, N.6
  • 29
    • 0026482090 scopus 로고
    • Flash photolysis study on pharaonis phoborhodopsin from a haloalkaliphilic bacterium (Natronobacterium pharaonis)
    • Miyazaki, M., Hirayama, J., Hayakawa, M., and Kamo, N. (1992) Flash photolysis study on pharaonis phoborhodopsin from a haloalkaliphilic bacterium (Natronobacterium pharaonis), Biochim. Biophys. Acta 1140, 22-29.
    • (1992) Biochim. Biophys. Acta , vol.1140 , pp. 22-29
    • Miyazaki, M.1    Hirayama, J.2    Hayakawa, M.3    Kamo, N.4
  • 30
    • 0030808219 scopus 로고    scopus 로고
    • Glutamate-194 to cysteine mutation inhibits fast light-induced proton release in bacteriorhodopsin
    • Balashov, S. P., Imasheva, E. S., Ebrey, T. G., Chen, N., Menick, D. R., and Crouch, R. K. (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
  • 31
    • 0032562215 scopus 로고    scopus 로고
    • Existence of a proton-transfer chain in bacteriorhodopsin: Participation of Glu-194 in the release of protons to the extracellular surface
    • Dioumaev, A. K., Richter, H. T., Brown, L. S., Tanio, M., Tuzi, S., Saito, H., Kimura, Y., Needleman, R., and Lanyi, J. K. (1998) Existence of a proton-transfer chain in bacteriorhodopsin: participation of Glu-194 in the release of protons to the extracellular 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
  • 32
    • 0032578378 scopus 로고    scopus 로고
    • Lipid patches in membrane protein oligomers: Crystal structure of the bacteriorhodopsin-lipid complex
    • Essen, L. O., Siegert, R., Lehmann, W. D., and Oesterhelt, D. (1998) Lipid patches in membrane protein oligomers: crystal structure of the bacteriorhodopsin-lipid complex, Proc. Natl. Acad. Sci. U.S.A. 95, 11673-11678.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 11673-11678
    • Essen, L.O.1    Siegert, R.2    Lehmann, W.D.3    Oesterhelt, D.4
  • 33
    • 0034714097 scopus 로고    scopus 로고
    • Time-resolved detection of transient movement of helix F in spin-labeled pharaonis sensory rhodopsin II
    • Wegener, A. A., Chizhov, I., Engelhard, M., and Steinhoff, H. J. (2000) Time-resolved detection of transient movement of helix F in spin-labeled pharaonis sensory rhodopsin II, J. Mol. Biol. 301, 881-891.
    • (2000) J. Mol. Biol. , vol.301 , pp. 881-891
    • Wegener, A.A.1    Chizhov, I.2    Engelhard, M.3    Steinhoff, H.J.4
  • 34
    • 0036651031 scopus 로고    scopus 로고
    • Association between a photointermediate of a M-lacking mutant D75N of pharaonis phoborhodopsin and its cognate transducer
    • Sudo, Y., Iwamoto, M., Shimono, K., and Kamo, N. (2002) Association between a photointermediate of a M-lacking mutant D75N of pharaonis phoborhodopsin and its cognate transducer, J. Photochem. Photobiol. B 67, 171-176.
    • (2002) J. Photochem. Photobiol. B , vol.67 , pp. 171-176
    • Sudo, Y.1    Iwamoto, M.2    Shimono, K.3    Kamo, N.4
  • 35
    • 0036283968 scopus 로고    scopus 로고
    • Tyr-199 and charged residues of pharaonis phoborhodopsin are important for the interaction with its transducer
    • Sudo, Y., Iwamoto, M., Shimono, K., and Kamo, N. (2002) Tyr-199 and charged residues of pharaonis phoborhodopsin are important for the interaction with its transducer, Biophys. J. 83, 427-432.
    • (2002) Biophys. J. , vol.83 , pp. 427-432
    • Sudo, Y.1    Iwamoto, M.2    Shimono, K.3    Kamo, N.4
  • 37
    • 0035477798 scopus 로고    scopus 로고
    • Structural insights into the early steps of receptor-transducer signal transfer in archaeal phototaxis
    • Wegener, A. A., Klare, J. P., Engelhard, M., and Steinhoff, H. J. (2001) Structural insights into the early steps of receptor-transducer signal transfer in archaeal phototaxis, EMBO J. 20, 5312-5319.
    • (2001) EMBO J. , vol.20 , pp. 5312-5319
    • Wegener, A.A.1    Klare, J.P.2    Engelhard, M.3    Steinhoff, H.J.4
  • 39
    • 0001652299 scopus 로고
    • Time-course and stoichiometry of light-induced proton release and uptake during the photocycle of bacteriorhodopsin
    • Grzesiek, S., and Dencher, N. A. (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
  • 40
    • 0028864699 scopus 로고
    • Glutamic acid 204 is the terminal proton release group at the extracellular surface of bacteriorhodopsin
    • Brown, L. S., Sasaki, J., Kandori, H., Maeda, A., Needleman, R., and Lanyi, J. K. (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
  • 41
    • 0032492706 scopus 로고    scopus 로고
    • Bacteriorhodopsin's intramolecular proton-release pathway consists of a hydrogen-bonded network
    • Rammelsberg, R., Huhn, G., Lubben, M., and Gerwert, K. (1998) Bacteriorhodopsin's intramolecular proton-release pathway consists of a hydrogen-bonded network, Biochemistry 37, 5001-5009.
    • (1998) Biochemistry , vol.37 , pp. 5001-5009
    • Rammelsberg, R.1    Huhn, G.2    Lubben, M.3    Gerwert, K.4
  • 42
    • 0141592427 scopus 로고    scopus 로고
    • Conformational changes detected in a sensory rhodopsin II-transducer complex
    • Bergo, V., Spudich, E. N., Spudich, J. L., and Rothschild, K. J. (2003) Conformational changes detected in a sensory rhodopsin II-transducer complex, J. Biol. Chem. 278, 36556-36562.
    • (2003) J. Biol. Chem. , vol.278 , pp. 36556-36562
    • Bergo, V.1    Spudich, E.N.2    Spudich, J.L.3    Rothschild, K.J.4
  • 43
    • 0035997072 scopus 로고    scopus 로고
    • Role of Asp193 in chromophore-protein interaction of pharaonis phoborhodopsin (sensory rhodopsin II)
    • Iwamoto, M., Furutani, Y., Sudo, Y., Shimono, K., Kandori, H., and Kamo, N. (2002) Role of Asp193 in chromophore-protein interaction of pharaonis phoborhodopsin (sensory rhodopsin II), Biophys. J. 83, 1130-1135.
    • (2002) Biophys. J. , vol.83 , pp. 1130-1135
    • Iwamoto, M.1    Furutani, Y.2    Sudo, Y.3    Shimono, K.4    Kandori, H.5    Kamo, N.6
  • 44
    • 0242365582 scopus 로고    scopus 로고
    • Arg-72 of pharaonis phoborhodopsin (sensory rhodopsin II) is important for the maintenance of the protein structure in the solubilized states
    • Ikeura, Y., Shimono, K., Iwamoto, M., Sudo, Y., and Kamo, N. (2003) Arg-72 of pharaonis phoborhodopsin (sensory rhodopsin II) is important for the maintenance of the protein structure in the solubilized states, Photochem. Photobiol. 77, 96-100.
    • (2003) Photochem. Photobiol. , vol.77 , pp. 96-100
    • Ikeura, Y.1    Shimono, K.2    Iwamoto, M.3    Sudo, Y.4    Kamo, N.5
  • 45
    • 0027362929 scopus 로고
    • pH dependence of light-induced proton release by bacteriorhodopsin
    • Kono, M., Misra, S., and Ebrey, T. G. (1993) pH dependence of light-induced proton release by bacteriorhodopsin, FEBS Lett. 331, 31-34.
    • (1993) FEBS Lett. , vol.331 , pp. 31-34
    • Kono, M.1    Misra, S.2    Ebrey, T.G.3
  • 46
    • 0026737320 scopus 로고
    • Pathways of proton release in the bacteriorhodopsin photocycle
    • Zimanyi, L., Varo, G., Chang, M., Ni, B., Needleman, R., and Lanyi, J. K. (1992) Pathways of proton release in the bacteriorhodopsin photocycle, Biochemistry 31, 8535-8543.
    • (1992) Biochemistry , vol.31 , pp. 8535-8543
    • Zimanyi, L.1    Varo, G.2    Chang, M.3    Ni, B.4    Needleman, R.5    Lanyi, J.K.6
  • 47
    • 0032770157 scopus 로고    scopus 로고
    • Opening the Schiff base moiety of bacteriorhodopsin by mutation of the four extracellular Glu side chains
    • Sanz, C., Lazarova, T., Sepulcre, F., Gonzalez-Moreno, R., Bourdelande, J. L., Querol, E., and Padros, E. (1999) Opening the Schiff base moiety of bacteriorhodopsin by mutation of the four extracellular Glu side chains, FEBS Lett. 456, 191-195.
    • (1999) FEBS Lett. , vol.456 , pp. 191-195
    • Sanz, C.1    Lazarova, T.2    Sepulcre, F.3    Gonzalez-Moreno, R.4    Bourdelande, J.L.5    Querol, E.6    Padros, E.7
  • 48
    • 0037172777 scopus 로고    scopus 로고
    • Specific effects of chloride on the photocycle of E194Q and E204Q mutants of bacteriorhodopsin as measured by FTIR spectroscopy
    • Lazarova, T., Sanz, C., Sepulcre, F., Querol, E., and Padros, E. (2002) Specific effects of chloride on the photocycle of E194Q and E204Q mutants of bacteriorhodopsin as measured by FTIR spectroscopy, Biochemistry 41, 8176-8183.
    • (2002) Biochemistry , vol.41 , pp. 8176-8183
    • Lazarova, T.1    Sanz, C.2    Sepulcre, F.3    Querol, E.4    Padros, E.5
  • 49
    • 0037432194 scopus 로고    scopus 로고
    • Dynamic structure of pharaonis phoborhodopsin (sensory rhodopsin II) and complex with a cognate truncated transducer as revealed by site-directed 13C solid-state NMR
    • Arakawa, T., Shimono, K., Yamaguchi, S., Tuzi, S., Sudo, Y., Kamo, N., and Saito, H. (2003) Dynamic structure of pharaonis phoborhodopsin (sensory rhodopsin II) and complex with a cognate truncated transducer as revealed by site-directed 13C solid-state NMR, FEBS Lett. 536, 237-240.
    • (2003) FEBS Lett. , vol.536 , pp. 237-240
    • Arakawa, T.1    Shimono, K.2    Yamaguchi, S.3    Tuzi, S.4    Sudo, Y.5    Kamo, N.6    Saito, H.7
  • 50
    • 0026331216 scopus 로고
    • Identification of signaling states of a sensory receptor by modulation of lifetimes of stimulus-induced conformations: The case of sensory rhodopsin II
    • Yan, B., Takahashi, T., Johnson, R., and Spudich, J. L. (1991) Identification of signaling states of a sensory receptor by modulation of lifetimes of stimulus-induced conformations: the case of sensory rhodopsin II, Biochemistry 30, 10686-10692.
    • (1991) Biochemistry , vol.30 , pp. 10686-10692
    • Yan, B.1    Takahashi, T.2    Johnson, R.3    Spudich, J.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.