메뉴 건너뛰기




Volumn 85, Issue 1, 2009, Pages 239-249

The photoreactions of recombinant phytochrome CphA from the cyanobacterium Calothrix PCC7601: A low-temperature UV-Vis and FTIR study

Author keywords

[No Author keywords available]

Indexed keywords

PHYTOCHROME; RECOMBINANT PROTEIN;

EID: 58349119908     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1751-1097.2008.00426.x     Document Type: Article
Times cited : (16)

References (71)
  • 1
    • 0029110499 scopus 로고
    • Phytochromes: Differential properties, expression patterns and molecular evolution
    • Pratt, L. H. (1995) Phytochromes: Differential properties, expression patterns and molecular evolution. Photochem. Photobiol. 61 (1 10 21.
    • (1995) Photochem. Photobiol. , vol.61 , Issue.1 , pp. 10-21
    • Pratt, L.H.1
  • 3
    • 0032037506 scopus 로고    scopus 로고
    • Different phototransduction kinetics of phytochrome a and phytochrome B in Arabidopsis thaliana
    • Casal, J. J., P. D. Cerdan, R. J. Staneloni L. Cattaneo (1998) Different phototransduction kinetics of phytochrome A and phytochrome B in Arabidopsis thaliana. Plant Physiol. 116, 1533 1538.
    • (1998) Plant Physiol. , vol.116 , pp. 1533-1538
    • Casal, J.J.1    Cerdan, P.D.2    Staneloni, R.J.3    Cattaneo, L.4
  • 4
    • 0032578425 scopus 로고    scopus 로고
    • The phytochrome family: Dissection of functional roles and signalling pathways among family members
    • Quail, P. H. (1998) The phytochrome family: Dissection of functional roles and signalling pathways among family members. Philos. Trans. R. Soc. Lond. B Biol. Sci. 353, 1399 1403.
    • (1998) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.353 , pp. 1399-1403
    • Quail, P.H.1
  • 5
    • 0034609795 scopus 로고    scopus 로고
    • Phytochromes and light signal perception by plants - An emerging synthesis
    • Smith, H. (2000) Phytochromes and light signal perception by plants - an emerging synthesis. Nature 407, 585 591.
    • (2000) Nature , vol.407 , pp. 585-591
    • Smith, H.1
  • 6
    • 1642523086 scopus 로고    scopus 로고
    • Light signals, phytochromes and cross-talk with other environmental cues
    • Franklin, K. A. G. C. Whitelam (2004) Light signals, phytochromes and cross-talk with other environmental cues. J. Exp. Bot. 55, 271 276.
    • (2004) J. Exp. Bot. , vol.55 , pp. 271-276
    • Franklin, K.A.1    Whitelam, G.C.2
  • 7
    • 23944484126 scopus 로고    scopus 로고
    • Phytochromes and shade-avoidance responses in plants
    • Franklin, K. A. G. C. Whitelam (2005) Phytochromes and shade-avoidance responses in plants. Ann. Bot. (Lond) 96, 169 175.
    • (2005) Ann. Bot. (Lond) , vol.96 , pp. 169-175
    • Franklin, K.A.1    Whitelam, G.C.2
  • 8
    • 0022422399 scopus 로고
    • Analysis of cloned cDNA and genomic sequences for phytochrome: Complete amino acid sequences for two gene products expressed in etiolated Avena
    • Hershey, H. P., R. F. Barker, K. B. Idler, J. L. Lissemore P. H. Quail (1985) Analysis of cloned cDNA and genomic sequences for phytochrome: Complete amino acid sequences for two gene products expressed in etiolated Avena. Nucleic Acids Res. 13, 8543 8559.
    • (1985) Nucleic Acids Res. , vol.13 , pp. 8543-8559
    • Hershey, H.P.1    Barker, R.F.2    Idler, K.B.3    Lissemore, J.L.4    Quail, P.H.5
  • 9
  • 10
    • 0028936558 scopus 로고
    • Photobiophysics and photobiochemistry of the heterogeneous phytochrome system
    • Sineshchekov, V. A. (1995) Photobiophysics and photobiochemistry of the heterogeneous phytochrome system. Biochim. Biophys. Acta (BBA) - Bioenerg. 1228, 125 164.
    • (1995) Biochim. Biophys. Acta (BBA) - Bioenerg. , vol.1228 , pp. 125-164
    • Sineshchekov, V.A.1
  • 11
    • 0026951658 scopus 로고
    • Events in the phytochrome molecule after irradiation
    • Rüdiger, W. (1992) Events in the phytochrome molecule after irradiation. Photochem. Photobiol. 56, 803 809.
    • (1992) Photochem. Photobiol. , vol.56 , pp. 803-809
    • Rüdiger, W.1
  • 12
    • 0039090711 scopus 로고
    • Chromophore structure of the physiologically active form (P(fr)) of phytochrome
    • Rüdiger, W., F. Thümmler, E. Cmiel S. Schneider (1983) Chromophore structure of the physiologically active form (P(fr)) of phytochrome. Proc. Natl. Acad. Sci. USA 80, 6244 6248.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 6244-6248
    • Rüdiger, W.1    Thümmler, F.2    Cmiel, E.3    Schneider, S.4
  • 13
    • 0025606743 scopus 로고
    • Resonance Raman analysis of the Pr and Pfr forms of phytochrome
    • Fodor, S. P., J. C. Lagarias R. A. Mathies (1990) Resonance Raman analysis of the Pr and Pfr forms of phytochrome. Biochemistry 29, 11141 11146.
    • (1990) Biochemistry , vol.29 , pp. 11141-11146
    • Fodor, S.P.1    Lagarias, J.C.2    Mathies, R.A.3
  • 15
    • 0033576250 scopus 로고    scopus 로고
    • Protonation state and structural changes of the tetrapyrrole chromophore during the Pr - > Pfr phototransformation of phytochrome: A resonance Raman spectroscopic study
    • Kneip, C., P. Hildebrandt, W. Schlamann, S. E. Braslavsky, F. Mark K. Schaffner (1999) Protonation state and structural changes of the tetrapyrrole chromophore during the Pr - > Pfr phototransformation of phytochrome: A resonance Raman spectroscopic study. Biochemistry 38, 15185 15192.
    • (1999) Biochemistry , vol.38 , pp. 15185-15192
    • Kneip, C.1    Hildebrandt, P.2    Schlamann, W.3    Braslavsky, S.E.4    Mark, F.5    Schaffner, K.6
  • 16
    • 0034646178 scopus 로고    scopus 로고
    • Probing the photoreaction mechanism of phytochrome through analysis of resonance Raman vibrational spectra of recombinant analogues
    • Andel, F. III., J. T. Murphy, J. A. Haas, M. T. McDowell, d. H. van, I. J. Lugtenburg, J. C. Lagarias R. A. Mathies (2000) Probing the photoreaction mechanism of phytochrome through analysis of resonance Raman vibrational spectra of recombinant analogues. Biochemistry 39, 2667 2676.
    • (2000) Biochemistry , vol.39 , pp. 2667-2676
    • Andel Iii., F.1    Murphy, J.T.2    Haas, J.A.3    McDowell, M.T.4    Van, D.H.5    Lugtenburg, I.J.6    Lagarias, J.C.7    Mathies, R.A.8
  • 17
    • 0029116739 scopus 로고
    • Fourier-transform resonance Raman spectroscopy of intermediates of the phytochrome photocycle
    • Matysik, J., P. Hildebrandt, W. Schlamann, S. E. Braslavsky K. Schaffner (1995) Fourier-transform resonance Raman spectroscopy of intermediates of the phytochrome photocycle. Biochemistry 34, 10497 10507.
    • (1995) Biochemistry , vol.34 , pp. 10497-10507
    • Matysik, J.1    Hildebrandt, P.2    Schlamann, W.3    Braslavsky, S.E.4    Schaffner, K.5
  • 18
    • 0029769670 scopus 로고    scopus 로고
    • Fourier-transform infrared spectroscopy of phytochrome: Difference spectra of the intermediates of the photoreactions
    • Foerstendorf, H., E. Mummert, E. Schäfer, H. Scheer F. Siebert (1996) Fourier-transform infrared spectroscopy of phytochrome: Difference spectra of the intermediates of the photoreactions. Biochemistry 35, 10793 10799.
    • (1996) Biochemistry , vol.35 , pp. 10793-10799
    • Foerstendorf, H.1    Mummert, E.2    Schäfer, E.3    Scheer, H.4    Siebert, F.5
  • 19
  • 20
    • 51049098982 scopus 로고    scopus 로고
    • FTIR study of the photoinduced processes of plant phytochrome phyA using isotope-labeled bilins an DFT calculations
    • Schwinté, P., H. Foerstendorf, Z. Hussain, W. Gärtner, M. A. Mroginski, P. Hildebrandt F. Siebert (2008) FTIR study of the photoinduced processes of plant phytochrome phyA using isotope-labeled bilins an DFT calculations. Biophys. J. 95, 1256 1267.
    • (2008) Biophys. J. , vol.95 , pp. 1256-1267
    • Schwinté, P.1    Foerstendorf, H.2    Hussain, Z.3    Gärtner, W.4    Mroginski, M.A.5    Hildebrandt, P.6    Siebert, F.7
  • 21
    • 0033612143 scopus 로고    scopus 로고
    • PKS1, a substrate phosphorylated by phytochrome that modulates light signaling in Arabidopsis
    • Fankhauser, C., K. C. Yeh, J. C. Lagarias, H. Zhang, T. D. Elich J. Chory (1999) PKS1, a substrate phosphorylated by phytochrome that modulates light signaling in Arabidopsis. Science 284, 1539 1541.
    • (1999) Science , vol.284 , pp. 1539-1541
    • Fankhauser, C.1    Yeh, K.C.2    Lagarias, J.C.3    Zhang, H.4    Elich, T.D.5    Chory, J.6
  • 23
    • 0032567039 scopus 로고    scopus 로고
    • PIF3, a phytochrome-interacting factor necessary for normal photoinduced signal transduction, is a novel basic helix-loop-helix protein
    • Ni, M., J. M. Tepperman P. H. Quail (1998) PIF3, a phytochrome- interacting factor necessary for normal photoinduced signal transduction, is a novel basic helix-loop-helix protein. Cell 95, 657 667.
    • (1998) Cell , vol.95 , pp. 657-667
    • Ni, M.1    Tepperman, J.M.2    Quail, P.H.3
  • 24
    • 0041029474 scopus 로고    scopus 로고
    • Direct targeting of light signals to a promoter element-bound transcription factor
    • Martinez-Garcia, J. F., E. Huq P. H. Quail (2000) Direct targeting of light signals to a promoter element-bound transcription factor. Science 288, 859 863.
    • (2000) Science , vol.288 , pp. 859-863
    • Martinez-Garcia, J.F.1    Huq, E.2    Quail, P.H.3
  • 26
    • 4043083523 scopus 로고    scopus 로고
    • Functional analysis of a 450-amino acid N-terminal fragment of phytochrome B in Arabidopsis
    • Oka, Y., T. Matsushita, N. Mochizuki, T. Suzuki, S. Tokutomi A. Nagatani (2004) Functional analysis of a 450-amino acid N-terminal fragment of phytochrome B in Arabidopsis. Plant Cell 16, 2104 2116.
    • (2004) Plant Cell , vol.16 , pp. 2104-2116
    • Oka, Y.1    Matsushita, T.2    Mochizuki, N.3    Suzuki, T.4    Tokutomi, S.5    Nagatani, A.6
  • 29
  • 30
    • 0031194090 scopus 로고    scopus 로고
    • The phytochromes: A biochemical mechanism of signaling in sight?
    • Quail, P. H. (1997) The phytochromes: A biochemical mechanism of signaling in sight? Bioessays 19, 571 579.
    • (1997) Bioessays , vol.19 , pp. 571-579
    • Quail, P.H.1
  • 31
    • 84920143748 scopus 로고    scopus 로고
    • Schäfer, E. F. Nagy (. eds. Springer, Dordrecht, The Netherlands.
    • Schäfer, E. F. Nagy (eds. 2006) Photomorphogenesis in Plants and Bacteria. Springer, Dordrecht, The Netherlands.
    • (2006) Photomorphogenesis in Plants and Bacteria.
  • 32
    • 0024962346 scopus 로고
    • Formation of a photoreversible phycocyanobilin-apophytochrome adduct in vitro
    • Elich, T. D. J. C. Lagarias (1989) Formation of a photoreversible phycocyanobilin-apophytochrome adduct in vitro. J. Biol. Chem. 264, 12902 12908.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12902-12908
    • Elich, T.D.1    Lagarias, J.C.2
  • 33
    • 0026649545 scopus 로고
    • Phytochrome assembly. Defining chromophore structural requirements for covalent attachment and photoreversibility
    • Li, L. J. C. Lagarias (1992) Phytochrome assembly. Defining chromophore structural requirements for covalent attachment and photoreversibility. J. Biol. Chem. 267, 19204 19210.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19204-19210
    • Li, L.1    Lagarias, J.C.2
  • 34
    • 0028566686 scopus 로고
    • Phytochrome assembly in living cells of the yeast Saccharomyces cerevisiae
    • Li, L. J. C. Lagarias (1994) Phytochrome assembly in living cells of the yeast Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 91, 12535 12539.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12535-12539
    • Li, L.1    Lagarias, J.C.2
  • 35
    • 0032479788 scopus 로고    scopus 로고
    • A novel chromophore selectivity modifies the spectral properties of one of the two stable states of the plant photoreceptor phytochrome
    • Lindner, I., B. Knipp, S. Braslavsky, W. Gärtner K. Schaffner (1998) A novel chromophore selectivity modifies the spectral properties of one of the two stable states of the plant photoreceptor phytochrome. Angew. Chem. Int. Ed Engl. 37, 1843 1846.
    • (1998) Angew. Chem. Int. Ed Engl. , vol.37 , pp. 1843-1846
    • Lindner, I.1    Knipp, B.2    Braslavsky, S.3    Gärtner, W.4    Schaffner, K.5
  • 37
    • 0035857548 scopus 로고    scopus 로고
    • Analysis of the Topology of the Chromophore Binding Pocket of Phytochromes by Variation of the Chromophore Substitution Pattern
    • Robben, U., I. Lindner, W. Gärtner K. Schaffner (2001) Analysis of the Topology of the Chromophore Binding Pocket of Phytochromes by Variation of the Chromophore Substitution Pattern. Angew. Chem. Int. Ed Engl. 40, 1048 1050.
    • (2001) Angew. Chem. Int. Ed Engl. , vol.40 , pp. 1048-1050
    • Robben, U.1    Lindner, I.2    Gärtner, W.3    Schaffner, K.4
  • 42
    • 0030865349 scopus 로고    scopus 로고
    • A cyanobacterial phytochrome two-component light sensory system
    • Yeh, K. C., S. H. Wu, J. T. Murphy J. C. Lagarias (1997) A cyanobacterial phytochrome two-component light sensory system. Science 277, 1505 1508.
    • (1997) Science , vol.277 , pp. 1505-1508
    • Yeh, K.C.1    Wu, S.H.2    Murphy, J.T.3    Lagarias, J.C.4
  • 43
    • 27844461604 scopus 로고    scopus 로고
    • A light-sensing knot revealed by the structure of the chromophore-binding domain of phytochrome
    • Wagner, J. R., J. S. Brunzelle, K. T. Forest R. D. Vierstra (2005) A light-sensing knot revealed by the structure of the chromophore-binding domain of phytochrome. Nature 438, 325 331.
    • (2005) Nature , vol.438 , pp. 325-331
    • Wagner, J.R.1    Brunzelle, J.S.2    Forest, K.T.3    Vierstra, R.D.4
  • 44
    • 34547628072 scopus 로고    scopus 로고
    • Crystal structure of the chromophore binding domain of an unusual bacteriophytochrome, RpBphP3, reveals residues that modulate photoconversion
    • Yang, X., E. A. Stojkovic, J. Kuk K. Moffat (2007) Crystal structure of the chromophore binding domain of an unusual bacteriophytochrome, RpBphP3, reveals residues that modulate photoconversion. Proc. Natl. Acad. Sci. USA 104, 12571 12576.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 12571-12576
    • Yang, X.1    Stojkovic, E.A.2    Kuk, J.3    Moffat, K.4
  • 45
    • 0033397947 scopus 로고    scopus 로고
    • Prokaryotes and phytochrome. the connection to chromophores and signaling
    • Hughes, J. T. Lamparter (1999) Prokaryotes and phytochrome. The connection to chromophores and signaling. Plant Physiol. 121, 1059 1068.
    • (1999) Plant Physiol. , vol.121 , pp. 1059-1068
    • Hughes, J.1    Lamparter, T.2
  • 46
    • 33748450550 scopus 로고    scopus 로고
    • Chromophore structure in the photocycle of the cyanobacterial phytochrome Cph1
    • van Thor, J. J., M. Mackeen, I. Kuprov, R. A. Dwek M. R. Wormald (2006) Chromophore structure in the photocycle of the cyanobacterial phytochrome Cph1. Biophys. J. 91, 1811 1822.
    • (2006) Biophys. J. , vol.91 , pp. 1811-1822
    • Van Thor, J.J.1    MacKeen, M.2    Kuprov, I.3    Dwek, R.A.4    Wormald, M.R.5
  • 48
    • 0033819950 scopus 로고    scopus 로고
    • A new appraisal of the prokaryotic origin of eukaryotic phytochromes
    • Herdman, M., T. Coursin, R. Rippka, J. Houmard d. M. Tandeau (2000) A new appraisal of the prokaryotic origin of eukaryotic phytochromes. J. Mol. Evol. 51, 205 213.
    • (2000) J. Mol. Evol. , vol.51 , pp. 205-213
    • Herdman, M.1    Coursin, T.2    Rippka, R.3    Houmard, J.4    Tandeau, D.M.5
  • 49
    • 0034857464 scopus 로고    scopus 로고
    • Characterization of the Cph1 holo-phytochrome from Synechocystis sp. PCC 6803
    • Hübschmann, T., T. Borner, E. Hartmann T. Lamparter (2001) Characterization of the Cph1 holo-phytochrome from Synechocystis sp. PCC 6803. Eur. J. Biochem. 268, 2055 2063.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2055-2063
    • Hübschmann, T.1    Borner, T.2    Hartmann, E.3    Lamparter, T.4
  • 50
    • 34247172164 scopus 로고    scopus 로고
    • Homologous expression of a bacterial phytochrome. the cyanobacterium Fremyella diplosiphon incorporates biliverdin as a genuine, functional chromophore
    • Quest, B., T. Hübschmann, S. Sharda, d. M. Tandeau W. Gärtner (2007) Homologous expression of a bacterial phytochrome. The cyanobacterium Fremyella diplosiphon incorporates biliverdin as a genuine, functional chromophore. FEBS J. 274, 2088 2098.
    • (2007) FEBS J. , vol.274 , pp. 2088-2098
    • Quest, B.1    Hübschmann, T.2    Sharda, S.3    Tandeau, D.M.4    Gärtner, W.5
  • 52
    • 0033772448 scopus 로고    scopus 로고
    • Vibrational spectroscopy as a tool for probing protein function
    • Vogel, R. F. Siebert (2000) Vibrational spectroscopy as a tool for probing protein function. Curr. Opin. Chem. Biol. 4, 518 523.
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 518-523
    • Vogel, R.1    Siebert, F.2
  • 53
    • 27744572616 scopus 로고    scopus 로고
    • Assignments of the Pfr-Pr FTIR difference spectrum of cyanobacterial phytochrome Cph1 using 15N and 13C isotopically labeled phycocyanobilin chromophore
    • van Thor, J. J., N. Fisher P. R. Rich (2005) Assignments of the Pfr-Pr FTIR difference spectrum of cyanobacterial phytochrome Cph1 using 15N and 13C isotopically labeled phycocyanobilin chromophore. J. Phys. Chem. B Condens. Matter Mater. Surf. Interfaces. Biophys. 109, 20597 20604.
    • (2005) J. Phys. Chem. B Condens. Matter Mater. Surf. Interfaces. Biophys. , vol.109 , pp. 20597-20604
    • Van Thor, J.J.1    Fisher, N.2    Rich, P.R.3
  • 54
    • 0034191806 scopus 로고    scopus 로고
    • The photoreactions of recombinant phytochrome from the cyanobacterium Synechocystis: A low-temperature UV-Vis and FT-IR spectroscopic study
    • Foerstendorf, H., T. Lamparter, J. Hughes, W. Gärtner F. Siebert (2000) The photoreactions of recombinant phytochrome from the cyanobacterium Synechocystis: A low-temperature UV-Vis and FT-IR spectroscopic study. Photochem. Photobiol. 71, 655 661.
    • (2000) Photochem. Photobiol. , vol.71 , pp. 655-661
    • Foerstendorf, H.1    Lamparter, T.2    Hughes, J.3    Gärtner, W.4    Siebert, F.5
  • 55
    • 0035846628 scopus 로고    scopus 로고
    • FTIR studies of phytochrome photoreactions reveal the C=O bands of the chromophore: Consequences for its protonation states, conformation, and protein interaction
    • Foerstendorf, H., C. Benda, W. Gärtner, M. Storf, H. Scheer F. Siebert (2001) FTIR studies of phytochrome photoreactions reveal the C=O bands of the chromophore: Consequences for its protonation states, conformation, and protein interaction. Biochemistry 40, 14952 14959.
    • (2001) Biochemistry , vol.40 , pp. 14952-14959
    • Foerstendorf, H.1    Benda, C.2    Gärtner, W.3    Storf, M.4    Scheer, H.5    Siebert, F.6
  • 56
    • 0018512859 scopus 로고
    • Chemical modification of biliprotein chromophores
    • Kufer, W. H. Scheer (1979) Chemical modification of biliprotein chromophores. Z. Naturforsch. [C. ] 34, 776 781.
    • (1979) Z. Naturforsch. [C. ] , vol.34 , pp. 776-781
    • Kufer, W.1    Scheer, H.2
  • 57
    • 21844477536 scopus 로고    scopus 로고
    • Light-dependent dimerisation in the N-terminal sensory module of cyanobacterial phytochrome 1
    • Strauss, H. M., P. Schmieder J. Hughes (2005) Light-dependent dimerisation in the N-terminal sensory module of cyanobacterial phytochrome 1. FEBS Lett. 579, 3970 3974.
    • (2005) FEBS Lett. , vol.579 , pp. 3970-3974
    • Strauss, H.M.1    Schmieder, P.2    Hughes, J.3
  • 59
    • 0035725360 scopus 로고    scopus 로고
    • Phytochrome Cph1 from the cyanobacterium Synechocystis PCC6803. Purification, assembly, and quaternary structure
    • Lamparter, T., B. Esteban J. Hughes (2001) Phytochrome Cph1 from the cyanobacterium Synechocystis PCC6803. Purification, assembly, and quaternary structure. Eur. J. Biochem. 268, 4720 4730.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 4720-4730
    • Lamparter, T.1    Esteban, B.2    Hughes, J.3
  • 60
    • 0037729260 scopus 로고    scopus 로고
    • Fourier transform IR spectroscopy study for new insights into molecular properties and activation mechanisms of visual pigment rhodopsin
    • Vogel, R. F. Siebert (2003) Fourier transform IR spectroscopy study for new insights into molecular properties and activation mechanisms of visual pigment rhodopsin. Biopolymers 72, 133 148.
    • (2003) Biopolymers , vol.72 , pp. 133-148
    • Vogel, R.1    Siebert, F.2
  • 61
    • 84945738848 scopus 로고
    • Absorption Spectra of Phytochrome Intermediates
    • Eilfeld, P. W. Rüdiger (1985) Absorption Spectra of Phytochrome Intermediates. Z. Naturforsch. [C. ] 40c, 109 114.
    • (1985) Z. Naturforsch. [C. ] , vol.40 , pp. 109-114
    • Eilfeld, P.1    Rüdiger, W.2
  • 62
    • 34249728355 scopus 로고    scopus 로고
    • High resolution structure of Deinococcus bacteriophytochrome yields new insights into phytochrome architecture and evolution
    • Wagner, J. R., J. Zhang, J. S. Brunzelle, R. D. Vierstra K. T. Forest (2007) High resolution structure of Deinococcus bacteriophytochrome yields new insights into phytochrome architecture and evolution. J. Biol. Chem. 282, 12298 12309.
    • (2007) J. Biol. Chem. , vol.282 , pp. 12298-12309
    • Wagner, J.R.1    Zhang, J.2    Brunzelle, J.S.3    Vierstra, R.D.4    Forest, K.T.5
  • 63
    • 33751285557 scopus 로고    scopus 로고
    • (15)N MAS NMR Studies of Cph1 phytochrome: Chromophore dynamics and intramolecular signal transduction
    • Rohmer, T., H. Strauss, J. Hughes, H. de Groot, W. Gärtner, P. Schmieder J. Matysik (2006) (15)N MAS NMR Studies of Cph1 phytochrome: Chromophore dynamics and intramolecular signal transduction. J. Phys. Chem. B 110, 20580 20585.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 20580-20585
    • Rohmer, T.1    Strauss, H.2    Hughes, J.3    De Groot, H.4    Gärtner, W.5    Schmieder, P.6    Matysik, J.7
  • 64
    • 33846105959 scopus 로고    scopus 로고
    • Formation of the early photoproduct lumi-R of cyanobacterial phytochrome Cph1 observed by ultrafast mid-infrared spectroscopy
    • van Thor, J. J., K. L. Ronayne M. Towrie (2007) Formation of the early photoproduct lumi-R of cyanobacterial phytochrome Cph1 observed by ultrafast mid-infrared spectroscopy. J. Am. Chem. Soc. 129, 126 132.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 126-132
    • Van Thor, J.J.1    Ronayne, K.L.2    Towrie, M.3
  • 65
    • 0037061953 scopus 로고    scopus 로고
    • Interpretation of Amide I Difference Bands Observed during Protein Reactions Using Site-Directed Isotopically Labeled Bacteriorhodopsin as a Model System
    • Hauser, K., M. Engelhard, N. Friedman, M. Sheves F. Siebert (2002) Interpretation of Amide I Difference Bands Observed during Protein Reactions Using Site-Directed Isotopically Labeled Bacteriorhodopsin as a Model System. J. Phys. Chem. A 106, 3553 3559.
    • (2002) J. Phys. Chem. a , vol.106 , pp. 3553-3559
    • Hauser, K.1    Engelhard, M.2    Friedman, N.3    Sheves, M.4    Siebert, F.5
  • 66
    • 65549154760 scopus 로고    scopus 로고
    • Technical University, Berlin.
    • von Stetten, D. (2008) Thesis. Technical University, Berlin.
    • (2008) Thesis.
    • Von Stetten, D.1
  • 67
    • 45549107695 scopus 로고    scopus 로고
    • Mutational analysis of Deinococcus radiodurans bacteriophytochrome reveals key amino acids necessary for structural integrity and the proton exchange cycle during photoconversion
    • Wagner, J. R., J. Zhang, D. von Stetten, M. Günther, D. H. Murgida, M. A. Mroginski, J. M. Walker, K. T. Forest, P. Hildebrandt R. D. Vierstra (2008) Mutational analysis of Deinococcus radiodurans bacteriophytochrome reveals key amino acids necessary for structural integrity and the proton exchange cycle during photoconversion. J. Biol. Chem. 283, 12212 12226.
    • (2008) J. Biol. Chem. , vol.283 , pp. 12212-12226
    • Wagner, J.R.1    Zhang, J.2    Von Stetten, D.3    Günther, M.4    Murgida, D.H.5    Mroginski, M.A.6    Walker, J.M.7    Forest, K.T.8    Hildebrandt, P.9    Vierstra, R.D.10
  • 70
    • 0026453337 scopus 로고
    • The phototransformation process in phytochrome. I. Ultrafast fluorescence component and kinetic models for the initial Pr - > Pfr transformation steps in native phytochrome
    • Holzwarth, A. R., E. Venuti, S. E. Braslavsky K. Schaffner (1992) The phototransformation process in phytochrome. I. Ultrafast fluorescence component and kinetic models for the initial Pr - > Pfr transformation steps in native phytochrome. Biochim. Biophys. Acta (BBA) - Bioenerg. 1140, 59 68.
    • (1992) Biochim. Biophys. Acta (BBA) - Bioenerg. , vol.1140 , pp. 59-68
    • Holzwarth, A.R.1    Venuti, E.2    Braslavsky, S.E.3    Schaffner, K.4
  • 71
    • 0035830421 scopus 로고    scopus 로고
    • First steps in the phytochrome phototransformation: A comparative femtosecond study on the forward (Pr - > Pfr) and back reaction (Pfr - > Pr)
    • Bischoff, M., G. Hermann, S. Rentsch D. Strehlow (2001) First steps in the phytochrome phototransformation: A comparative femtosecond study on the forward (Pr - > Pfr) and back reaction (Pfr - > Pr). Biochemistry 40, 181 186.
    • (2001) Biochemistry , vol.40 , pp. 181-186
    • Bischoff, M.1    Hermann, G.2    Rentsch, S.3    Strehlow, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.