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Volumn 358, Issue 3, 2006, Pages 686-700

Cytoplasmic Shuttling of Protons in Anabaena Sensory Rhodopsin: Implications for Signaling Mechanism

Author keywords

chromatic adaptation; infrared spectroscopy; photosensory transduction; proton transfers; retinal protein

Indexed keywords

LIPID; PROTON; SCHIFF BASE; SENSORY RHODOPSIN;

EID: 33646056953     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.02.036     Document Type: Article
Times cited : (55)

References (53)
  • 1
    • 84889439782 scopus 로고    scopus 로고
    • Microbial rhodopsins: phylogenetic and functional diversity
    • Briggs W.R., and Spudich J.L. (Eds), Wiley-VCH, Weinheim
    • Spudich J.L., and Jung K.H. Microbial rhodopsins: phylogenetic and functional diversity. In: Briggs W.R., and Spudich J.L. (Eds). Handbook of Photosensory Receptors (2005), Wiley-VCH, Weinheim 1-24
    • (2005) Handbook of Photosensory Receptors , pp. 1-24
    • Spudich, J.L.1    Jung, K.H.2
  • 2
    • 1842531691 scopus 로고    scopus 로고
    • New insights into the evolutionary history of type 1 rhodopsins
    • Ruiz-Gonzalez M.X., and Marin I. New insights into the evolutionary history of type 1 rhodopsins. J. Mol. Evol. 58 (2004) 348-358
    • (2004) J. Mol. Evol. , vol.58 , pp. 348-358
    • Ruiz-Gonzalez, M.X.1    Marin, I.2
  • 3
    • 3242797479 scopus 로고    scopus 로고
    • Fungal rhodopsins and opsin-related proteins: eukaryotic homologues of bacteriorhodopsin with unknown functions
    • Brown L.S. Fungal rhodopsins and opsin-related proteins: eukaryotic homologues of bacteriorhodopsin with unknown functions. Photochem. Photobiol. Sci. 3 (2004) 555-565
    • (2004) Photochem. Photobiol. Sci. , vol.3 , pp. 555-565
    • Brown, L.S.1
  • 4
    • 0034519206 scopus 로고    scopus 로고
    • Retinylidene proteins: structures and functions from archaea to humans
    • Spudich J.L., Yang C., Jung K.H., and Spudich E.N. Retinylidene proteins: structures and functions from archaea to humans. Annu. Rev. Cell Dev. Biol. 16 (2000) 365-392
    • (2000) Annu. Rev. Cell Dev. Biol. , vol.16 , pp. 365-392
    • Spudich, J.L.1    Yang, C.2    Jung, K.H.3    Spudich, E.N.4
  • 5
    • 0034665853 scopus 로고    scopus 로고
    • Bacterial rhodopsin: evidence for a new type of phototrophy in the sea
    • Béjà O., Aravind L., Koonin E.V., Suzuki M.T., Hadd A., Nguyen L.P., et al. Bacterial rhodopsin: evidence for a new type of phototrophy in the sea. Science 289 (2000) 1902-1906
    • (2000) Science , vol.289 , pp. 1902-1906
    • Béjà, O.1    Aravind, L.2    Koonin, E.V.3    Suzuki, M.T.4    Hadd, A.5    Nguyen, L.P.6
  • 7
    • 18744369621 scopus 로고    scopus 로고
    • Leptosphaeria rhodopsin: bacteriorhodopsin-like proton pump from a eucaryote
    • Waschuk S.A., Bezerra Jr. A.G., Shi L., and Brown L.S. Leptosphaeria rhodopsin: bacteriorhodopsin-like proton pump from a eucaryote. Proc. Natl Acad. Sci. USA 102 (2005) 6879-6883
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 6879-6883
    • Waschuk, S.A.1    Bezerra Jr., A.G.2    Shi, L.3    Brown, L.S.4
  • 8
    • 0024289369 scopus 로고
    • Vibrational spectroscopy of bacteriorhodopsin mutants-light-driven proton transport involves protonation changes of aspartic acid residue-85, residue-96, and residue-212
    • Braiman M.S., Mogi T., Marti T., Stern L.J., Khorana H.G., and Rothschild K.J. Vibrational spectroscopy of bacteriorhodopsin mutants-light-driven proton transport involves protonation changes of aspartic acid residue-85, residue-96, and residue-212. Biochemistry 27 (1988) 8516-8520
    • (1988) Biochemistry , vol.27 , pp. 8516-8520
    • Braiman, M.S.1    Mogi, T.2    Marti, T.3    Stern, L.J.4    Khorana, H.G.5    Rothschild, K.J.6
  • 10
    • 0037346546 scopus 로고    scopus 로고
    • Demonstration of a sensory rhodopsin in eubacteria
    • Jung K.H., Trivedi V.D., and Spudich J.L. Demonstration of a sensory rhodopsin in eubacteria. Mol. Microbiol. 47 (2003) 1513-1522
    • (2003) Mol. Microbiol. , vol.47 , pp. 1513-1522
    • Jung, K.H.1    Trivedi, V.D.2    Spudich, J.L.3
  • 11
    • 0037173051 scopus 로고    scopus 로고
    • Two rhodopsins mediate phototaxis to low- and high-intensity light in Chlamydomonas reinhardtii
    • Sineshchekov O.A., Jung K.H., and Spudich J.L. Two rhodopsins mediate phototaxis to low- and high-intensity light in Chlamydomonas reinhardtii. Proc. Natl Acad. Sci. USA 99 (2002) 8689-8694
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 8689-8694
    • Sineshchekov, O.A.1    Jung, K.H.2    Spudich, J.L.3
  • 13
    • 0030906654 scopus 로고    scopus 로고
    • Molecular mechanism of photosignaling by archaeal sensory rhodopsins
    • Hoff W.D., Jung K.H., and Spudich J.L. Molecular mechanism of photosignaling by archaeal sensory rhodopsins. Annu. Rev. Biophys. Biomol. Struct. 26 (1997) 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
  • 14
    • 0034734230 scopus 로고    scopus 로고
    • Proton transport by sensory rhodopsins and its modulation by transducer-binding
    • Sasaki J., and Spudich J.L. Proton transport by sensory rhodopsins and its modulation by transducer-binding. Biochim. Biophys. Acta 1460 (2000) 230-239
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 230-239
    • Sasaki, J.1    Spudich, J.L.2
  • 15
  • 16
    • 17644387239 scopus 로고    scopus 로고
    • Photochromicity of Anabaena sensory rhodopsin, an atypical microbial receptor with a cis-retinal light-adapted form
    • Sineshchekov O.A., Trivedi V.D., Sasaki J., and Spudich J.L. Photochromicity of Anabaena sensory rhodopsin, an atypical microbial receptor with a cis-retinal light-adapted form. J. Biol. Chem. 280 (2005) 14663-14668
    • (2005) J. Biol. Chem. , vol.280 , pp. 14663-14668
    • Sineshchekov, O.A.1    Trivedi, V.D.2    Sasaki, J.3    Spudich, J.L.4
  • 18
    • 0942268739 scopus 로고    scopus 로고
    • RcaE is a complementary chromatic adaptation photoreceptor required for green and red light responsiveness
    • Terauchi K., Montgomery B.L., Grossman A.R., Lagarias J.C., and Kehoe D.M. RcaE is a complementary chromatic adaptation photoreceptor required for green and red light responsiveness. Mol. Microbiol. 51 (2004) 567-577
    • (2004) Mol. Microbiol. , vol.51 , pp. 567-577
    • Terauchi, K.1    Montgomery, B.L.2    Grossman, A.R.3    Lagarias, J.C.4    Kehoe, D.M.5
  • 19
    • 0015730341 scopus 로고
    • Reversible dissociation of the purple complex in bacteriorhodopsin and identification of 13-cis and all-trans- retinal as its chromophores
    • Oesterhelt D., Meentzen M., and Schuhmann L. Reversible dissociation of the purple complex in bacteriorhodopsin and identification of 13-cis and all-trans- retinal as its chromophores. Eur. J. Biochem. 40 (1973) 453-463
    • (1973) Eur. J. Biochem. , vol.40 , pp. 453-463
    • Oesterhelt, D.1    Meentzen, M.2    Schuhmann, L.3
  • 21
    • 0032546920 scopus 로고    scopus 로고
    • Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution
    • Luecke H., Richter H.-T., and Lanyi J.K. Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution. Science 280 (1998) 1934-1937
    • (1998) Science , vol.280 , pp. 1934-1937
    • Luecke, H.1    Richter, H.-T.2    Lanyi, J.K.3
  • 22
    • 0033567092 scopus 로고    scopus 로고
    • Protein, lipid and water organization in bacteriorhodopsin crystals: a molecular view of the purple membrane at 1.9 Å resolution
    • Belrhali H., Nollert P., Royant A., Menzel C., Rosenbusch J.P., Landau E.M., and Pebay-Peyroula E. Protein, lipid and water organization in bacteriorhodopsin crystals: a molecular view of the purple membrane at 1.9 Å resolution. Structure 7 (1999) 909-917
    • (1999) Structure , vol.7 , pp. 909-917
    • Belrhali, H.1    Nollert, P.2    Royant, A.3    Menzel, C.4    Rosenbusch, J.P.5    Landau, E.M.6    Pebay-Peyroula, E.7
  • 23
    • 24944551978 scopus 로고    scopus 로고
    • FTIR spectroscopy of the all-trans form of Anabaena sensory rhodopsin at 77 K: hydrogen bond of a water between the Schiff base and Asp75
    • Furutani Y., Kawanabe A., Jung K.H., and Kandori H. FTIR spectroscopy of the all-trans form of Anabaena sensory rhodopsin at 77 K: hydrogen bond of a water between the Schiff base and Asp75. Biochemistry 44 (2005) 12287-12296
    • (2005) Biochemistry , vol.44 , pp. 12287-12296
    • Furutani, Y.1    Kawanabe, A.2    Jung, K.H.3    Kandori, H.4
  • 24
    • 3242801403 scopus 로고    scopus 로고
    • Light-induced intramolecular charge movements in microbial rhodopsins in intact E. coli cells
    • Sineshchekov O.A., and Spudich J.L. Light-induced intramolecular charge movements in microbial rhodopsins in intact E. coli cells. Photochem. Photobiol. Sci. 3 (2004) 548-554
    • (2004) Photochem. Photobiol. Sci. , vol.3 , pp. 548-554
    • Sineshchekov, O.A.1    Spudich, J.L.2
  • 25
    • 0000736928 scopus 로고
    • Vibrational analysis of the 13-cis-retinal chromophore in dark-adapted bacteriorhodopsin
    • Smith S.O., Pardoen J.A., Lugtenburg J., and Mathies R.A. Vibrational analysis of the 13-cis-retinal chromophore in dark-adapted bacteriorhodopsin. J. Phys. Chem. 91 (1987) 804-819
    • (1987) J. Phys. Chem. , vol.91 , pp. 804-819
    • Smith, S.O.1    Pardoen, J.A.2    Lugtenburg, J.3    Mathies, R.A.4
  • 26
    • 0017389861 scopus 로고
    • On the photocycle and light adaptation of dark-adapted bacteriorhodopsin
    • Kalisky O., Goldschmidt C.R., and Ottolenghi M. On the photocycle and light adaptation of dark-adapted bacteriorhodopsin. Biophys. J. 19 (1977) 185-189
    • (1977) Biophys. J. , vol.19 , pp. 185-189
    • Kalisky, O.1    Goldschmidt, C.R.2    Ottolenghi, M.3
  • 27
    • 0035979995 scopus 로고    scopus 로고
    • Photochemical reaction cycle and proton transfers in Neurospora rhodopsin
    • Brown L.S., Dioumaev A.K., Lanyi J.K., Spudich E.N., and Spudich J.L. Photochemical reaction cycle and proton transfers in Neurospora rhodopsin. J. Biol. Chem. 276 (2001) 32495-32505
    • (2001) J. Biol. Chem. , vol.276 , pp. 32495-32505
    • Brown, L.S.1    Dioumaev, A.K.2    Lanyi, J.K.3    Spudich, E.N.4    Spudich, J.L.5
  • 28
    • 0025292873 scopus 로고
    • Proton transport and M-type intermediate formation by 13-cis-bacteriorhodopsin
    • Kaulen A.D., Drachev L.A., and Zorina V.V. Proton transport and M-type intermediate formation by 13-cis-bacteriorhodopsin. Biochim. Biophys. Acta 1018 (1990) 103-113
    • (1990) Biochim. Biophys. Acta , vol.1018 , pp. 103-113
    • Kaulen, A.D.1    Drachev, L.A.2    Zorina, V.V.3
  • 29
    • 0028783627 scopus 로고
    • The complex extracellular domain regulates the transient deprotonation and reprotonation of the retinal Schiff base during the bacteriorhodopsin photocycle
    • Brown L.S., Váró G., Hatanaka M., Sasaki J., Kandori H., Maeda A., et al. The complex extracellular domain regulates the transient deprotonation and reprotonation of the retinal Schiff base during the bacteriorhodopsin photocycle. Biochemistry 34 (1995) 12903-12911
    • (1995) Biochemistry , vol.34 , pp. 12903-12911
    • Brown, L.S.1    Váró, G.2    Hatanaka, M.3    Sasaki, J.4    Kandori, H.5    Maeda, A.6
  • 30
    • 0030566867 scopus 로고    scopus 로고
    • Kinetic isotope effects reveal an ice-like and a liquid-phase-type intramolecular proton transfer in bacteriorhodopsin
    • Le Coutre J., and Gerwert K. Kinetic isotope effects reveal an ice-like and a liquid-phase-type intramolecular proton transfer in bacteriorhodopsin. FEBS Letters 398 (1996) 333-336
    • (1996) FEBS Letters , vol.398 , pp. 333-336
    • Le Coutre, J.1    Gerwert, K.2
  • 31
    • 0034620606 scopus 로고    scopus 로고
    • Origins of deuterium kinetic isotope effects on the proton transfers of the bacteriorhodopsin photocycle
    • Brown L.S., Needleman R., and Lanyi J.K. Origins of deuterium kinetic isotope effects on the proton transfers of the bacteriorhodopsin photocycle. Biochemistry 39 (2000) 938-945
    • (2000) Biochemistry , vol.39 , pp. 938-945
    • Brown, L.S.1    Needleman, R.2    Lanyi, J.K.3
  • 32
    • 84989748901 scopus 로고
    • Bathoproducts and conformers of all-trans-bacteriorhodopsin and 13-cis-bacteriorhodopsin at 90 K
    • Balashov S.P., Karneyeva N.V., Litvin F.F., and Ebrey T.G. Bathoproducts and conformers of all-trans-bacteriorhodopsin and 13-cis-bacteriorhodopsin at 90 K. Photochem. Photobiol. 54 (1991) 949-953
    • (1991) Photochem. Photobiol. , vol.54 , pp. 949-953
    • Balashov, S.P.1    Karneyeva, N.V.2    Litvin, F.F.3    Ebrey, T.G.4
  • 33
    • 0030904207 scopus 로고    scopus 로고
    • Time-resolved Fourier transform infrared study of structural changes in the last steps of the photocycles of Glu-204 and Leu-93 mutants of bacteriorhodopsin
    • Kandori H., Yamazaki Y., Hatanaka M., Needleman R., Brown L.S., Richter H.-T., et al. Time-resolved Fourier transform infrared study of structural changes in the last steps of the photocycles of Glu-204 and Leu-93 mutants of bacteriorhodopsin. Biochemistry 36 (1997) 5134-5141
    • (1997) Biochemistry , vol.36 , pp. 5134-5141
    • Kandori, H.1    Yamazaki, Y.2    Hatanaka, M.3    Needleman, R.4    Brown, L.S.5    Richter, H.-T.6
  • 34
    • 0031553201 scopus 로고    scopus 로고
    • Infrared difference spectra of the intermediates L, M, N, and O of the bacteriorhodopsin photoreaction obtained by time-resolved attenuated total reflection spectroscopy
    • Zscherp C., and Heberle J. Infrared difference spectra of the intermediates L, M, N, and O of the bacteriorhodopsin photoreaction obtained by time-resolved attenuated total reflection spectroscopy. J. Phys. Chem. B 101 (1997) 10542-10547
    • (1997) J. Phys. Chem. B , vol.101 , pp. 10542-10547
    • Zscherp, C.1    Heberle, J.2
  • 35
    • 0025868156 scopus 로고
    • Fourier transform infrared study of the N intermediate of bacteriorhodopsin
    • Pfefferlé J.M., Maeda A., Sasaki J., and Yoshizawa T. Fourier transform infrared study of the N intermediate of bacteriorhodopsin. Biochemistry 30 (1991) 6548-6556
    • (1991) Biochemistry , vol.30 , pp. 6548-6556
    • Pfefferlé, J.M.1    Maeda, A.2    Sasaki, J.3    Yoshizawa, T.4
  • 36
    • 0025968915 scopus 로고
    • Protein dynamics in the bacteriorhodopsin photocycle:submillisecond Fourier transform infrared spectra of the L-photointermediates, M-photointermediates, and N-photointermediates
    • Braiman M.S., Bousché O., and Rothschild K.J. Protein dynamics in the bacteriorhodopsin photocycle:submillisecond Fourier transform infrared spectra of the L-photointermediates, M-photointermediates, and N-photointermediates. Proc. Natl Acad. Sci. USA 88 (1991) 2388-2392
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 2388-2392
    • Braiman, M.S.1    Bousché, O.2    Rothschild, K.J.3
  • 37
    • 0027429642 scopus 로고
    • A model-independent approach to assigning bacteriorhodopsin's intramolecular reactions to photocycle intermediates
    • Hessling B., Souvignier G., and Gerwert K. A model-independent approach to assigning bacteriorhodopsin's intramolecular reactions to photocycle intermediates. Biophys. J. 65 (1993) 1929-1941
    • (1993) Biophys. J. , vol.65 , pp. 1929-1941
    • Hessling, B.1    Souvignier, G.2    Gerwert, K.3
  • 38
    • 0021943979 scopus 로고
    • Light-driven protonation changes of internal aspartic acids of bacteriorhodopsin: an investigation by static and time-resolved infrared difference spectroscopy using (4-C-13)aspartic acid labeled purple membrane
    • Engelhard M., Gerwert K., Hess B., Kreutz W., and Siebert F. Light-driven protonation changes of internal aspartic acids of bacteriorhodopsin: an investigation by static and time-resolved infrared difference spectroscopy using (4-C-13)aspartic acid labeled purple membrane. Biochemistry 24 (1985) 400-407
    • (1985) Biochemistry , vol.24 , pp. 400-407
    • Engelhard, M.1    Gerwert, K.2    Hess, B.3    Kreutz, W.4    Siebert, F.5
  • 39
    • 0034696409 scopus 로고    scopus 로고
    • FTIR analysis of the SII540 intermediate of sensory rhodopsin II: Asp73 is the Schiff base proton acceptor
    • Bergo V., Spudich E.N., Scott K.L., Spudich J.L., and Rothschild K.J. FTIR analysis of the SII540 intermediate of sensory rhodopsin II: Asp73 is the Schiff base proton acceptor. Biochemistry 39 (2000) 2823-2830
    • (2000) Biochemistry , vol.39 , pp. 2823-2830
    • Bergo, V.1    Spudich, E.N.2    Scott, K.L.3    Spudich, J.L.4    Rothschild, K.J.5
  • 40
    • 14844347271 scopus 로고    scopus 로고
    • Proton binding within a membrane protein by a protonated water cluster
    • Garczarek F., Brown L.S., Lanyi J.K., and Gerwert K. Proton binding within a membrane protein by a protonated water cluster. Proc. Natl Acad. Sci. USA 102 (2005) 3633-3638
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 3633-3638
    • Garczarek, F.1    Brown, L.S.2    Lanyi, J.K.3    Gerwert, K.4
  • 41
    • 0038649076 scopus 로고    scopus 로고
    • Crystallographic structures of the M and N intermediates of bacteriorhodopsin: assembly of a hydrogen-bonded chain of water molecules between asp-96 and the retinal Schiff base
    • Schobert B., Brown L.S., and Lanyi J.K. Crystallographic structures of the M and N intermediates of bacteriorhodopsin: assembly of a hydrogen-bonded chain of water molecules between asp-96 and the retinal Schiff base. J. Mol. Biol. 330 (2003) 553-570
    • (2003) J. Mol. Biol. , vol.330 , pp. 553-570
    • Schobert, B.1    Brown, L.S.2    Lanyi, J.K.3
  • 42
    • 84989674532 scopus 로고
    • Identification of the proton acceptor of Schiff base deprotonation in bacteriorhodopsin: an FTIR study of the mutant Asp85→Glu in its natural lipid environment
    • Fahmy K., Weidlich O., Engelhard M., Tittor J., Oesterhelt D., and Siebert F. Identification of the proton acceptor of Schiff base deprotonation in bacteriorhodopsin: an FTIR study of the mutant Asp85→Glu in its natural lipid environment. Photochem. Photobiol. 56 (1992) 1073-1083
    • (1992) Photochem. Photobiol. , vol.56 , pp. 1073-1083
    • Fahmy, K.1    Weidlich, O.2    Engelhard, M.3    Tittor, J.4    Oesterhelt, D.5    Siebert, F.6
  • 43
    • 0031228099 scopus 로고    scopus 로고
    • His-166 is critical for active site proton transfer and phototaxis signaling by sensory rhodopsin I
    • Zhang X.-N., and Spudich J.L. His-166 is critical for active site proton transfer and phototaxis signaling by sensory rhodopsin I. Biophys. J. 73 (1997) 1518-1523
    • (1997) Biophys. J. , vol.73 , pp. 1518-1523
    • Zhang, X.-N.1    Spudich, J.L.2
  • 44
    • 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. Structural insights into the early steps of receptor-transducer signal transfer in archaeal phototaxis. EMBO J. 20 (2001) 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
  • 45
    • 5644247396 scopus 로고    scopus 로고
    • The cytoplasmic membrane-proximal domain of the HtrII transducer interacts with the E-F loop of photoactivated Natronomonas pharaonis sensory rhodopsin II
    • Yang C.S., Sineshchekov O., Spudich E.N., and Spudich J.L. The cytoplasmic membrane-proximal domain of the HtrII transducer interacts with the E-F loop of photoactivated Natronomonas pharaonis sensory rhodopsin II. J. Biol. Chem. 279 (2004) 42970-42976
    • (2004) J. Biol. Chem. , vol.279 , pp. 42970-42976
    • Yang, C.S.1    Sineshchekov, O.2    Spudich, E.N.3    Spudich, J.L.4
  • 46
    • 0031761606 scopus 로고    scopus 로고
    • Evidence for the specific interaction of a lipid molecule with rhodopsin which is altered in the transition to the active state metarhodopsin II
    • Beck M., Siebert F., and Sakmar T.P. Evidence for the specific interaction of a lipid molecule with rhodopsin which is altered in the transition to the active state metarhodopsin II. FEBS Letters 436 (1998) 304-308
    • (1998) FEBS Letters , vol.436 , pp. 304-308
    • Beck, M.1    Siebert, F.2    Sakmar, T.P.3
  • 47
    • 0035949633 scopus 로고    scopus 로고
    • Coupling of the reisomerization of the retinal, proton uptake, and reprotonation of Asp-96 in the N photointermediate of bacteriorhodopsin
    • Dioumaev A.K., Brown L.S., Needleman R., and Lanyi J.K. Coupling of the reisomerization of the retinal, proton uptake, and reprotonation of Asp-96 in the N photointermediate of bacteriorhodopsin. Biochemistry 40 (2001) 11308-11317
    • (2001) Biochemistry , vol.40 , pp. 11308-11317
    • Dioumaev, A.K.1    Brown, L.S.2    Needleman, R.3    Lanyi, J.K.4
  • 49
    • 0029900082 scopus 로고    scopus 로고
    • Protonatable residues at the cytoplasmic end of transmembrane helix-2 in the signal transducer HtrI control photochemistry and function of sensory rhodopsin I
    • Jung K.H., and Spudich J.L. Protonatable residues at the cytoplasmic end of transmembrane helix-2 in the signal transducer HtrI control photochemistry and function of sensory rhodopsin I. Proc. Natl Acad. Sci. USA 93 (1996) 6557-6561
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 6557-6561
    • Jung, K.H.1    Spudich, J.L.2
  • 50
    • 0035685117 scopus 로고    scopus 로고
    • An archaeal photosignal-transducing module mediates phototaxis in Escherichia coli
    • Jung K.H., Spudich E.N., Trivedi V.D., and Spudich J.L. An archaeal photosignal-transducing module mediates phototaxis in Escherichia coli. J. Bacteriol. 183 (2001) 6365-6371
    • (2001) J. Bacteriol. , vol.183 , pp. 6365-6371
    • Jung, K.H.1    Spudich, E.N.2    Trivedi, V.D.3    Spudich, J.L.4
  • 51
    • 0023931049 scopus 로고
    • Biochemical analysis of spontaneous fepA mutants of Escherichia coli
    • Elish M.E., Pierce J., and Earhart C.F. Biochemical analysis of spontaneous fepA mutants of Escherichia coli. J. Gen. Microbiol. 134 (1988) 1355-1364
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 1355-1364
    • Elish, M.E.1    Pierce, J.2    Earhart, C.F.3
  • 52
    • 3342894772 scopus 로고    scopus 로고
    • FTIR spectroscopy of the K photointermediate of Neurospora rhodopsin: structural changes of the retinal, the protein, and the water molecules after photoisomerization
    • Furutani Y., Bezerra Jr. A.G., Waschuk S., Sumii M., Brown L.S., and Kandori H. FTIR spectroscopy of the K photointermediate of Neurospora rhodopsin: structural changes of the retinal, the protein, and the water molecules after photoisomerization. Biochemistry 43 (2004) 9636-9646
    • (2004) Biochemistry , vol.43 , pp. 9636-9646
    • Furutani, Y.1    Bezerra Jr., A.G.2    Waschuk, S.3    Sumii, M.4    Brown, L.S.5    Kandori, H.6
  • 53
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling
    • Guex N., and Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18 (1997) 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2


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