메뉴 건너뛰기




Volumn 21, Issue 4, 1996, Pages 683-693

Photobiology of microorganisms: How photosensors catch a photon to initialize signalling

Author keywords

[No Author keywords available]

Indexed keywords

RHODOPSIN; PHOTOACTIVE YELLOW PROTEIN; PHYTOCHROME;

EID: 0029743968     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1996.411402.x     Document Type: Review
Times cited : (61)

References (76)
  • 1
    • 0027493250 scopus 로고
    • HY 4 gene of A. thaliana encodes a protein with characteristics of a bluelight photoreceptor
    • Ahmad, M., and Cashmore, A.R. (1993) HY 4 gene of A. thaliana encodes a protein with characteristics of a bluelight photoreceptor. Nature 366: 162-166.
    • (1993) Nature , vol.366 , pp. 162-166
    • Ahmad, M.1    Cashmore, A.R.2
  • 2
    • 0026562057 scopus 로고
    • Behavioral responses in bacteria
    • Armitage, J.P. (1992) Behavioral responses in bacteria. Annu Rev Physiol 54: 683-714.
    • (1992) Annu Rev Physiol , vol.54 , pp. 683-714
    • Armitage, J.P.1
  • 3
    • 0028577744 scopus 로고
    • Complete chemical structure of photoactive yellow protein: Novel thioester-linked 4-hydroxycinnamyl chromophore and photocycle chemistry
    • Baca, M., Borgstahl, G.E.O., Boissinot, M., Burke, P.M., Williams, W.R., Slater, K.A., and Getzoff, E.D. (1994) Complete chemical structure of photoactive yellow protein: novel thioester-linked 4-hydroxycinnamyl chromophore and photocycle chemistry. Biochemistry 33: 14369-14377.
    • (1994) Biochemistry , vol.33 , pp. 14369-14377
    • Baca, M.1    Borgstahl, G.E.O.2    Boissinot, M.3    Burke, P.M.4    Williams, W.R.5    Slater, K.A.6    Getzoff, E.D.7
  • 5
    • 0028089151 scopus 로고
    • Aspartate receptors of Escherichia coli and Salmonella typhimurium bind ligand with negative and half-of-the-sites cooperativity
    • Biemann, H.-P., and Koshland, D.E. (1994) Aspartate receptors of Escherichia coli and Salmonella typhimurium bind ligand with negative and half-of-the-sites cooperativity. Biochemistry 33: 629-634.
    • (1994) Biochemistry , vol.33 , pp. 629-634
    • Biemann, H.-P.1    Koshland, D.E.2
  • 6
    • 0029110488 scopus 로고
    • 1.4Å structure of photoactive yellow protein, a cytosolic photoreceptor: Unusual fold, active site, and chromophore
    • Borgstahl, G.E.O., Williams, D.R., and Getzoff, E.D. (1995) 1.4Å structure of photoactive yellow protein, a cytosolic photoreceptor: unusual fold, active site, and chromophore. Biochemistry 34: 6278-6287.
    • (1995) Biochemistry , vol.34 , pp. 6278-6287
    • Borgstahl, G.E.O.1    Williams, D.R.2    Getzoff, E.D.3
  • 7
    • 0023483526 scopus 로고
    • How carotenoids function in photosynthetic bacteria
    • Cogdell, R.J., and Frank, H.A. (1988) How carotenoids function in photosynthetic bacteria. Biochim Biophys Acta 895: 63-79.
    • (1988) Biochim Biophys Acta , vol.895 , pp. 63-79
    • Cogdell, R.J.1    Frank, H.A.2
  • 10
    • 0020492987 scopus 로고
    • Acid-base equilibrium of the Schiff base in bacteriorhodopsin
    • Druckmann, S., Ottolenghi, M., Pande, J., and Callender, R.H. (1982) Acid-base equilibrium of the Schiff base in bacteriorhodopsin. Biochemistry 21: 4953-4959.
    • (1982) Biochemistry , vol.21 , pp. 4953-4959
    • Druckmann, S.1    Ottolenghi, M.2    Pande, J.3    Callender, R.H.4
  • 12
    • 0024341576 scopus 로고
    • Removal of the 9-methyl group of retinal inhibits signal transduction in the visual process. A fourier transform infrared and biochemical investigation
    • Ganter, G.U.M., Schmid, E.D., Perez-Sala, D., Rando, R.R, and Siebert, F. (1989) Removal of the 9-methyl group of retinal inhibits signal transduction in the visual process. A fourier transform infrared and biochemical investigation. Biochemistry 28: 5954-5962.
    • (1989) Biochemistry , vol.28 , pp. 5954-5962
    • Ganter, G.U.M.1    Schmid, E.D.2    Perez-Sala, D.3    Rando, R.R.4    Siebert, F.5
  • 13
    • 84989674899 scopus 로고
    • Isolation and characterization of the presumed photoreceptor protein of Blepharisma japonicum
    • Gioffré, D., Ghetti, F., Lenci, F., Paradiso, C., Dai, R., and Song, P.-S. (1993) Isolation and characterization of the presumed photoreceptor protein of Blepharisma japonicum. Photochem Photobiol 58: 275-279.
    • (1993) Photochem Photobiol , vol.58 , pp. 275-279
    • Gioffré, D.1    Ghetti, F.2    Lenci, F.3    Paradiso, C.4    Dai, R.5    Song, P.-S.6
  • 14
    • 0023156454 scopus 로고
    • Photosensory behavior in prokaryotes
    • Häder, D.-P. (1987) Photosensory behavior in prokaryotes. Microbiol Rev 51: 1-21.
    • (1987) Microbiol Rev , vol.51 , pp. 1-21
    • Häder, D.-P.1
  • 15
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson, R., Baldwin, J.M., Ceska, T.A., Zemlin, F., Beckmann, E., and Downing, K.H. (1990) Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J Mol Biol 213: 899-929.
    • (1990) J Mol Biol , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 17
    • 84989696264 scopus 로고
    • Low temperature absorbance and fluorescence spectroscopy of the photoactive yellow protein from Ectothiorhodospira halophila
    • Hoff, W.D., Kwa, S.L.S., Van Grondelle, R., and Hellingwerf, K.J. (1992) Low temperature absorbance and fluorescence spectroscopy of the photoactive yellow protein from Ectothiorhodospira halophila. Photochem Photobiol 56: 529-539.
    • (1992) Photochem Photobiol , vol.56 , pp. 529-539
    • Hoff, W.D.1    Kwa, S.L.S.2    Van Grondelle, R.3    Hellingwerf, K.J.4
  • 19
    • 0028318245 scopus 로고
    • The photoactive yellow protein from Ectothiorhodospira halophila as studied with a highly specific polyclonal antiserum: (intra)cellular localization, regulation of expression, and taxonomic distribution of cross-reacting protein
    • Hoff, W.D., Sprenger, W.W., Postma, P.W., Meyer, T.E., Veenhuis, M., Leguijt, T., and Hellingwerf, K.J. (1994b) The photoactive yellow protein from Ectothiorhodospira halophila as studied with a highly specific polyclonal antiserum: (intra)cellular localization, regulation of expression, and taxonomic distribution of cross-reacting protein. J Bacteriol 176: 3920-3927.
    • (1994) J Bacteriol , vol.176 , pp. 3920-3927
    • Hoff, W.D.1    Sprenger, W.W.2    Postma, P.W.3    Meyer, T.E.4    Veenhuis, M.5    Leguijt, T.6    Hellingwerf, K.J.7
  • 22
    • 0030069979 scopus 로고    scopus 로고
    • Chemical reactivity and spectroscopy of the thiol ester-linked ρ-coumaric acid chromophore in the photoactive yellow protein from Ectothiorhodospira halophila
    • Hoff, W.D., Devreese, B.V., Fokkens, R., Nugteren-Roodzant, I.M., Van Beeumen, J.J., Nibbering, N., and Hellingwerf, K.J. (1996) Chemical reactivity and spectroscopy of the thiol ester-linked ρ-coumaric acid chromophore in the photoactive yellow protein from Ectothiorhodospira halophila. Biochemistry 35: 1274-1281.
    • (1996) Biochemistry , vol.35 , pp. 1274-1281
    • Hoff, W.D.1    Devreese, B.V.2    Fokkens, R.3    Nugteren-Roodzant, I.M.4    Van Beeumen, J.J.5    Nibbering, N.6    Hellingwerf, K.J.7
  • 23
    • 0028868422 scopus 로고
    • Reconstitution photoactive yellow protein from apoprotein and ρ-coumaric acid derivates
    • Imamoto, Y., Ito, T., Kataoka, M., and Tokunaga, F. (1995) Reconstitution photoactive yellow protein from apoprotein and ρ-coumaric acid derivates. FEBS Lett 374: 157-160.
    • (1995) FEBS Lett , vol.374 , pp. 157-160
    • Imamoto, Y.1    Ito, T.2    Kataoka, M.3    Tokunaga, F.4
  • 24
    • 0028832513 scopus 로고
    • Resonance Raman evidence that the thioesterlinked chromophore of photoactive yellow protein is deprotonated
    • Kim, M., Mathies, R.A., Hoff, W.D., and Hellingwerf, K.J. (1995) Resonance Raman evidence that the thioesterlinked chromophore of photoactive yellow protein is deprotonated. Biochemistry 34: 12669-12672.
    • (1995) Biochemistry , vol.34 , pp. 12669-12672
    • Kim, M.1    Mathies, R.A.2    Hoff, W.D.3    Hellingwerf, K.J.4
  • 25
    • 0028175609 scopus 로고
    • Frozen' dynamic dimer model for transmembrane signaling in bacterial chemotaxis receptors
    • Kim, S.-H. (1994) 'Frozen' dynamic dimer model for transmembrane signaling in bacterial chemotaxis receptors. Protein Sci 3: 159-165.
    • (1994) Protein Sci , vol.3 , pp. 159-165
    • Kim, S.-H.1
  • 26
    • 0026503938 scopus 로고
    • The third chromophore of DNA photolyase: Trp-277 of Escherichia coli DNA photolyase repairs thymine dimers by direct electron transfer
    • Kim, S.-T., Li, Y.F., and Sancar, A. (1992) The third chromophore of DNA photolyase: Trp-277 of Escherichia coli DNA photolyase repairs thymine dimers by direct electron transfer. Proc Natl Acad Sci USA 89: 900-904.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 900-904
    • Kim, S.-T.1    Li, Y.F.2    Sancar, A.3
  • 27
    • 0029892214 scopus 로고    scopus 로고
    • Sequence evidence for strong conservation of the photoactive yellow proteins from the halophilic phototrophic bacteria Chromatium salexigens and Rhodospinillium salexigens
    • Koh, M., Van Driessche, G., Samyn, B., Hoff, W.D., Meyer, T.E., Cusanovich, M.A., and Van Beeumen, J.J. (1996) Sequence evidence for strong conservation of the photoactive yellow proteins from the halophilic phototrophic bacteria Chromatium salexigens and Rhodospinillium salexigens. Biochemistry 35: 2526-2534.
    • (1996) Biochemistry , vol.35 , pp. 2526-2534
    • Koh, M.1    Van Driessche, G.2    Samyn, B.3    Hoff, W.D.4    Meyer, T.E.5    Cusanovich, M.A.6    Van Beeumen, J.J.7
  • 30
    • 0029964634 scopus 로고    scopus 로고
    • Evidence for trans-cis isomerization of the ρ-coumaric acid chromophore as the photochemical basis of the photocycle of photoactive yellow protein
    • Kort, R., Vonk, H., Xu, X., Hoff, W.D., Crielaard, W., and Hellingwerf, K.J. (1996b) Evidence for trans-cis isomerization of the ρ-coumaric acid chromophore as the photochemical basis of the photocycle of photoactive yellow protein. FEBS Lett 382: 73-78.
    • (1996) FEBS Lett , vol.382 , pp. 73-78
    • Kort, R.1    Vonk, H.2    Xu, X.3    Hoff, W.D.4    Crielaard, W.5    Hellingwerf, K.J.6
  • 31
    • 0025160287 scopus 로고
    • Octopus photoreceptor membranes. Surface charge density and pK of the Schiff base of the pigments
    • Koutalos, Y. Ebrey, T.G., Gilson, H.R., and Honig, B. (1990) Octopus photoreceptor membranes. Surface charge density and pK of the Schiff base of the pigments. Biophys J 58: 493-501.
    • (1990) Biophys J , vol.58 , pp. 493-501
    • Koutalos, Y.1    Ebrey, T.G.2    Gilson, H.R.3    Honig, B.4
  • 32
    • 0026214242 scopus 로고
    • Effect of protonation on the isomerization properties of n-butylamine Schiff base of isomeric retinal as revealed by direct HPLC analyses: Selection of isomerization pathways by retinal proteins
    • Koyama, Y., Kubo, K., Komori, M., Yasuda, H., and Mukai, Y. (1991) Effect of protonation on the isomerization properties of n-butylamine Schiff base of isomeric retinal as revealed by direct HPLC analyses: selection of isomerization pathways by retinal proteins. Photochem Photobiol 54: 433-443.
    • (1991) Photochem Photobiol , vol.54 , pp. 433-443
    • Koyama, Y.1    Kubo, K.2    Komori, M.3    Yasuda, H.4    Mukai, Y.5
  • 33
    • 0028053122 scopus 로고
    • Investigations of the thermal response of laser excited biomolecules
    • Li, P., and Champion, P.M. (1994) Investigations of the thermal response of laser excited biomolecules. Biophys J 66: 430-436.
    • (1994) Biophys J , vol.66 , pp. 430-436
    • Li, P.1    Champion, P.M.2
  • 34
    • 0025114033 scopus 로고
    • Quantitation of photochromism of sensory rhodopsin-l by computerized tracking of Halobacterium halobium cells
    • Marwan, W., and Oesterhelt, D. (1990) Quantitation of photochromism of sensory rhodopsin-l by computerized tracking of Halobacterium halobium cells. J Mol Biol 215: 277-285.
    • (1990) J Mol Biol , vol.215 , pp. 277-285
    • Marwan, W.1    Oesterhelt, D.2
  • 36
    • 0025829307 scopus 로고
    • From femtoseconds to biology: Mechanism of bacteriorhodopsin's light-driven proton pump
    • Mathies, R.A., Lin, S.W., Ames, J.B., and Pollard, W.T. (1991) From femtoseconds to biology: mechanism of bacteriorhodopsin's light-driven proton pump. Annu Rev Biophys Chem 20: 491-518.
    • (1991) Annu Rev Biophys Chem , vol.20 , pp. 491-518
    • Mathies, R.A.1    Lin, S.W.2    Ames, J.B.3    Pollard, W.T.4
  • 37
    • 0022430790 scopus 로고
    • Isolation and characterization of soluble cytochromes, ferredoxins and other chromophoric proteins from the halophilic phototrophic bacterium Ectothiorhodospira halophila
    • Meyer, T.E. (1985) Isolation and characterization of soluble cytochromes, ferredoxins and other chromophoric proteins from the halophilic phototrophic bacterium Ectothiorhodospira halophila. Biochim Biophys Acta 806: 175-183.
    • (1985) Biochim Biophys Acta , vol.806 , pp. 175-183
    • Meyer, T.E.1
  • 38
    • 0023152468 scopus 로고
    • Properties of a water-soluble, yellow protein isolated from a halophilic phototrophic bacterium that has photochemical activity analogous to sensory rhodopsin
    • Meyer, T.E., Yakali, E., Cusanovich, M.A., and Tollin, G. (1987) Properties of a water-soluble, yellow protein isolated from a halophilic phototrophic bacterium that has photochemical activity analogous to sensory rhodopsin. Biochemistry 26: 418-423.
    • (1987) Biochemistry , vol.26 , pp. 418-423
    • Meyer, T.E.1    Yakali, E.2    Cusanovich, M.A.3    Tollin, G.4
  • 39
    • 0025910866 scopus 로고
    • Picosecond decay kinetics and quantum yield of fluorescence of the photoactive yellow protein from the halophilic purple phototrophic bacterium, Ectothiorhodospira halophila
    • Meyer, T.E., Tollin, G., Causgrove, T.P., Cheng, P., and Blankenschip, R.E. (1991) Picosecond decay kinetics and quantum yield of fluorescence of the photoactive yellow protein from the halophilic purple phototrophic bacterium, Ectothiorhodospira halophila. Biophys J 59: 988-991.
    • (1991) Biophys J , vol.59 , pp. 988-991
    • Meyer, T.E.1    Tollin, G.2    Causgrove, T.P.3    Cheng, P.4    Blankenschip, R.E.5
  • 40
    • 0027317603 scopus 로고
    • Ultraviolet resonance raman spectra of pea intact, large, and small phytochromes: Differences in molecular topography of red- And far-red-absorbing forms
    • Mizutani, Y., Tokutomi, S., Kaminaka, S., and Kitagawa, T. (1993) Ultraviolet resonance raman spectra of pea intact, large, and small phytochromes: differences in molecular topography of red- and far-red-absorbing forms. Biochemistry 32: 6916-6922.
    • (1993) Biochemistry , vol.32 , pp. 6916-6922
    • Mizutani, Y.1    Tokutomi, S.2    Kaminaka, S.3    Kitagawa, T.4
  • 41
    • 33847086787 scopus 로고
    • An external point-charge model for bacteriorhodopsin to account for its purple colour
    • Nakanishi, K., Balogh-Nair, V., Arnaboldi, M., Tsujimoto, K., and Honig, B. (1980) An external point-charge model for bacteriorhodopsin to account for its purple colour. J Am Chem Soc 102: 7945-7947.
    • (1980) J Am Chem Soc , vol.102 , pp. 7945-7947
    • Nakanishi, K.1    Balogh-Nair, V.2    Arnaboldi, M.3    Tsujimoto, K.4    Honig, B.5
  • 42
    • 9444269440 scopus 로고
    • Time-resolved photochemical studies of photoactive yellow protein (PYP) crystals
    • Ng, K., Ren, Z., Moffat, K., Borgstahl, G.E.O., McRee, D.E., and Getzoff, E.D. (1993) Time-resolved photochemical studies of photoactive yellow protein (PYP) crystals. Biophys J 64: A373.
    • (1993) Biophys J , vol.64
    • Ng, K.1    Ren, Z.2    Moffat, K.3    Borgstahl, G.E.O.4    McRee, D.E.5    Getzoff, E.D.6
  • 43
    • 0013294455 scopus 로고
    • Blue-light photoreceptors
    • Ninnemann, H. (1980) Blue-light photoreceptors. Bioscience 30: 166-170.
    • (1980) Bioscience , vol.30 , pp. 166-170
    • Ninnemann, H.1
  • 44
    • 0026355963 scopus 로고
    • Phytochrome: A light-activated molecular switch that regulates plant gene expression
    • Quail, P.M. (1991) Phytochrome: a light-activated molecular switch that regulates plant gene expression. Annu Rev Genet 25: 389-409.
    • (1991) Annu Rev Genet , vol.25 , pp. 389-409
    • Quail, P.M.1
  • 45
    • 0001739947 scopus 로고
    • The mechanism of action of glyoxalase
    • Racker, E. (1951) The mechanism of action of glyoxalase. J Biol Chem 190: 685-696.
    • (1951) J Biol Chem , vol.190 , pp. 685-696
    • Racker, E.1
  • 46
    • 0028855555 scopus 로고
    • Macroscopic phototactic behavior of the purple photosynthetic bacterium Rhodospirillum centenum
    • Ragatz, L., Jiang, Z.-Y., Bauer, C.E., and Gest, H. (1995) Macroscopic phototactic behavior of the purple photosynthetic bacterium Rhodospirillum centenum. Arch Microbiol 163: 1-6.
    • (1995) Arch Microbiol , vol.163 , pp. 1-6
    • Ragatz, L.1    Jiang, Z.-Y.2    Bauer, C.E.3    Gest, H.4
  • 47
    • 0027364707 scopus 로고
    • Fourier transform infrared difference spectroscopy of rhodopsin mutants: Light activation of rhodopsin causes hydrogen-binding change in residue aspartic acid-83 during Meta II formation
    • Rath, P., DeCaluwé, L.L.J., Bovee-Geurts, P.H.M., DeGrip, W.J., and Rothschild, K.J. (1993) Fourier transform infrared difference spectroscopy of rhodopsin mutants: light activation of rhodopsin causes hydrogen-binding change in residue aspartic acid-83 during Meta II formation. Biochemistry 32: 10277-10282.
    • (1993) Biochemistry , vol.32 , pp. 10277-10282
    • Rath, P.1    DeCaluwé, L.L.J.2    Bovee-Geurts, P.H.M.3    Degrip, W.J.4    Rothschild, K.J.5
  • 48
    • 0027443076 scopus 로고
    • Formation of the Meta II photointermediate is accompanied by conformational changes in the cytoplasmic surface of rhodopsin
    • Resek, J.F., Farahbakhsh, Z.T., Hubbell, W.L., and Khorana, H.G. (1993) Formation of the Meta II photointermediate is accompanied by conformational changes in the cytoplasmic surface of rhodopsin. Biochemistry 32: 12025-12032.
    • (1993) Biochemistry , vol.32 , pp. 12025-12032
    • Resek, J.F.1    Farahbakhsh, Z.T.2    Hubbell, W.L.3    Khorana, H.G.4
  • 49
    • 0000017956 scopus 로고
    • Quantum yields of the photochromic equilibrium between Bacteriorhodopsin and its Bathointermediate K. Femto- And nanosecond optoacoustic spectroscopy
    • Rohr, M., Gärtner, W., Schweitzer, G., Holzwarth, A.R., and Braslavsky, S.E. (1992) Quantum yields of the photochromic equilibrium between Bacteriorhodopsin and its Bathointermediate K. Femto- and nanosecond optoacoustic spectroscopy. J Phys Chem 96: 6055-6061.
    • (1992) J Phys Chem , vol.96 , pp. 6055-6061
    • Rohr, M.1    Gärtner, W.2    Schweitzer, G.3    Holzwarth, A.R.4    Braslavsky, S.E.5
  • 50
    • 0028962369 scopus 로고
    • Chemotaxis and phototaxis require a CheA histidine kinase in the archaeon Halobacterium salinarium
    • Rudolph, J., and Oesterhelt, D. (1995) Chemotaxis and phototaxis require a CheA histidine kinase in the archaeon Halobacterium salinarium. EMBO J 14: 667-673.
    • (1995) EMBO J , vol.14 , pp. 667-673
    • Rudolph, J.1    Oesterhelt, D.2
  • 56
    • 0029310457 scopus 로고
    • Characterization of a Chlamydomonas reinhardtii gene encoding a protein of the DNA photolyase-blue light photoreceptor family
    • Small, G.D., Min, B., and Lefebre, P.A. (1995) Characterization of a Chlamydomonas reinhardtii gene encoding a protein of the DNA photolyase-blue light photoreceptor family. Plant Mol Biol 28: 443-454.
    • (1995) Plant Mol Biol , vol.28 , pp. 443-454
    • Small, G.D.1    Min, B.2    Lefebre, P.A.3
  • 57
    • 0027324441 scopus 로고
    • Ectothiorhodospira halophila is negatively photoactive, with a wavelength dependence that fits the absorbance spectrum of the photoactive yellow protein
    • Sprenger, W.W., Hoff, W.D., Armitage, J.P., and Hellingwerf, K.J. (1993) Ectothiorhodospira halophila is negatively photoactive, with a wavelength dependence that fits the absorbance spectrum of the photoactive yellow protein. J Bacteriol 175: 3096-3104.
    • (1993) J Bacteriol , vol.175 , pp. 3096-3104
    • Sprenger, W.W.1    Hoff, W.D.2    Armitage, J.P.3    Hellingwerf, K.J.4
  • 58
    • 0024741720 scopus 로고
    • Sensory rhodopsin I and II modulate a methylation/ demethylation system in Halobacterium halobium
    • Spudich, E.N., Takahashi, T., and Spudich, J.L. (1989) Sensory rhodopsin I and II modulate a methylation/ demethylation system in Halobacterium halobium. Proc Natl Acad Sci USA 86: 7746-7750.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 7746-7750
    • Spudich, E.N.1    Takahashi, T.2    Spudich, J.L.3
  • 59
    • 0021756564 scopus 로고
    • Mechanism of colour discrimination by a bacterial sensory rhodopsin
    • Spudich, J.L., and Bogomolni, R.A. (1984) Mechanism of colour discrimination by a bacterial sensory rhodopsin. Nature 312: 509-513.
    • (1984) Nature , vol.312 , pp. 509-513
    • Spudich, J.L.1    Bogomolni, R.A.2
  • 62
    • 0000913267 scopus 로고
    • A new photoreceptor molecule from Stentor coeruleus
    • Tao, N., Orlando, M., Hyon, J.-S., Gross, M., and Song, P.-S. (1993) A new photoreceptor molecule from Stentor coeruleus. J Am Chem Soc 115: 2526-2528.
    • (1993) J Am Chem Soc , vol.115 , pp. 2526-2528
    • Tao, N.1    Orlando, M.2    Hyon, J.-S.3    Gross, M.4    Song, P.-S.5
  • 63
    • 0027716597 scopus 로고
    • Photoactivated conformational changes in rhodopsin: A time-resolved spin label study
    • Toossi, Z., Farahbakhsh, Z.T., Hideg, K., and Hubbell, W. L (1993) Photoactivated conformational changes in rhodopsin: a time-resolved spin label study. Science 262: 1416-1419.
    • (1993) Science , vol.262 , pp. 1416-1419
    • Toossi, Z.1    Farahbakhsh, Z.T.2    Hideg, K.3    Hubbell, W.L.4
  • 64
    • 0021839033 scopus 로고
    • Characterization of the chromophore of the third rhodopsin-like pigment of Halobacterium halobium and its photoproduct
    • Tsuda, M., Nelson, B., Chang, C.-H., Govindjee, R., Ebrey, T.G. (1985) Characterization of the chromophore of the third rhodopsin-like pigment of Halobacterium halobium and its photoproduct. Biophys J 47: 721-724.
    • (1985) Biophys J , vol.47 , pp. 721-724
    • Tsuda, M.1    Nelson, B.2    Chang, C.-H.3    Govindjee, R.4    Ebrey, T.G.5
  • 65
    • 0027271859 scopus 로고
    • The primary structure of a photoactive yellow protein from the phototrophic bacterium Ectothiorhodospira halophila, with evidence for the mass and the binding site of the chromophore
    • Van Beeumen, J., Devreese, B., Van Bun, S., Hoff, W.D., Hellingwerf, K.J., Meyer, T.E., McRee, D.E., and Cusanovich, M.A. (1993) The primary structure of a photoactive yellow protein from the phototrophic bacterium Ectothiorhodospira halophila, with evidence for the mass and the binding site of the chromophore. Protein Sci 2: 1114-1125.
    • (1993) Protein Sci , vol.2 , pp. 1114-1125
    • Van Beeumen, J.1    Devreese, B.2    Van Bun, S.3    Hoff, W.D.4    Hellingwerf, K.J.5    Meyer, T.E.6    McRee, D.E.7    Cusanovich, M.A.8
  • 66
    • 0028918464 scopus 로고
    • Photoinduced volume changes and energy storage associated with the early transformations of the photoactive yellow protein
    • Van Brederode, M.E., Gensch, Th., Hoff, W.D., Hellingwerf, K.J., and Braslavsky, S.E. (1995) Photoinduced volume changes and energy storage associated with the early transformations of the photoactive yellow protein. Biophys J 68: 1101-1109.
    • (1995) Biophys J , vol.68 , pp. 1101-1109
    • Van Brederode, M.E.1    Gensch, T.2    Hoff, W.D.3    Hellingwerf, K.J.4    Braslavsky, S.E.5
  • 68
    • 0029144733 scopus 로고
    • Identification of a chemotaxis operon with two cheY genes in Rhodobacter sphaeroides
    • Ward, M.J., Bell, A.W., Hamblin, P.A., Packer, H.L., and Armitage, J.P. (1995) Identification of a chemotaxis operon with two cheY genes in Rhodobacter sphaeroides. Mol Microbiol 17: 357-366.
    • (1995) Mol Microbiol , vol.17 , pp. 357-366
    • Ward, M.J.1    Bell, A.W.2    Hamblin, P.A.3    Packer, H.L.4    Armitage, J.P.5
  • 69
    • 0028167952 scopus 로고
    • 2+, and conformation of the chemotaxis protein CheY on its binding to the flagellar switch protein FliM
    • 2+, and conformation of the chemotaxis protein CheY on its binding to the flagellar switch protein FliM. Biochemistry 33: 10470-10476.
    • (1994) Biochemistry , vol.33 , pp. 10470-10476
    • Welch, M.1    Oosawa, K.2    Aizawa, S.-I.3    Eisenbach, M.4
  • 70
    • 0028089152 scopus 로고
    • A conformational change associated with the phototransformation of Pisum phytochrome a as probed by fluorescence quenching
    • Wells, T.A., Nakazawa, M.A., Manabe, K., and Song, P.-S. (1994) A conformational change associated with the phototransformation of Pisum phytochrome A as probed by fluorescence quenching. Biochemistry 33: 708-712.
    • (1994) Biochemistry , vol.33 , pp. 708-712
    • Wells, T.A.1    Nakazawa, M.A.2    Manabe, K.3    Song, P.-S.4
  • 71
    • 0027190996 scopus 로고
    • Photoreversible change in the conformation of phytochrome as probed with a covalently bound fluorescent sulfhydryl reagent, N-(9-acridinyl)maleimide
    • Yamamoto, K.T. (1993) Photoreversible change in the conformation of phytochrome as probed with a covalently bound fluorescent sulfhydryl reagent, N-(9-acridinyl)maleimide. Biochim Biophys Acta 1163: 227-233.
    • (1993) Biochim Biophys Acta , vol.1163 , pp. 227-233
    • Yamamoto, K.T.1
  • 72
    • 0025319948 scopus 로고
    • AII-trans/13-cis isomerization of retinal is required for phototaxis signaling by sensory rhodopsins in Halobacterium halobium
    • Van, B., Takahashi, T., Johnson, R., Derguini, F., Nakanishi, K., and Spudich, J.L. (1990) AII-trans/13-cis isomerization of retinal is required for phototaxis signaling by sensory rhodopsins in Halobacterium halobium. Biophys J 57: 807-810.
    • (1990) Biophys J , vol.57 , pp. 807-810
    • Van, B.1    Takahashi, T.2    Johnson, R.3    Derguini, F.4    Nakanishi, K.5    Spudich, J.L.6
  • 73
    • 0025950123 scopus 로고
    • Mechanism of activation of sensory rhodopsin I: Evidence for a steric trigger
    • Van, B., Nakanishi, K., and Spudich, J.L. (1991a) Mechanism of activation of sensory rhodopsin I: evidence for a steric trigger. Proc Natl Acad Sci USA 88: 9412-9416.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 9412-9416
    • Van, B.1    Nakanishi, K.2    Spudich, J.L.3
  • 74
    • 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., Takahasi, T., Johnson, R., and Spudich, J.L. (1991b) 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    Takahasi, T.2    Johnson, R.3    Spudich, J.L.4
  • 75
    • 0027434138 scopus 로고
    • Steric constraints in the retinal binding pocket of sensory rhodopsin I
    • Yan, B., Xie, A., Nienhaus, G.U., Katsuta, Y., and Spudich, J.L. (1993) Steric constraints in the retinal binding pocket of sensory rhodopsin I. Biochemistry 32: 10224-10232.
    • (1993) Biochemistry , vol.32 , pp. 10224-10232
    • Yan, B.1    Xie, A.2    Nienhaus, G.U.3    Katsuta, Y.4    Spudich, J.L.5
  • 76
    • 0029610771 scopus 로고
    • Spectral tuning in bacteriorhodopsin in the absence of counterion and coplanarization effects
    • Yan, B., Spudich, J.L., Mazur, P., Vunnam, S., Derguini, F., and Nakanishi, K. (1995) Spectral tuning in bacteriorhodopsin in the absence of counterion and coplanarization effects. J Biol Chem 270: 29668-29670.
    • (1995) J Biol Chem , vol.270 , pp. 29668-29670
    • Yan, B.1    Spudich, J.L.2    Mazur, P.3    Vunnam, S.4    Derguini, F.5    Nakanishi, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.