메뉴 건너뛰기




Volumn 89, Issue 2, 2013, Pages 259-273

Solid-state NMR spectroscopy to probe photoactivation in canonical phytochromes

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; ISOPROTEIN; PHYTOCHROME; PROTON; TETRAPYRROLE DERIVATIVE; VEGETABLE PROTEIN;

EID: 84874724670     PISSN: 00318655     EISSN: 17511097     Source Type: Journal    
DOI: 10.1111/php.12029     Document Type: Review
Times cited : (35)

References (107)
  • 1
    • 0001390901 scopus 로고
    • Light quality, photoperception and plant strategy
    • Smith, H., (1992) Light quality, photoperception and plant strategy. Annu. Rev. Plant Biol. 33, 481-518.
    • (1992) Annu. Rev. Plant Biol. , vol.33 , pp. 481-518
    • Smith, H.1
  • 3
    • 0000663949 scopus 로고
    • Detection, assay, and preliminary purification of the pigment controlling photoresponsive development of plants
    • Butler, W. L., K. H. Norris, H. W. Siegelman, and, S. B. Hendricks, (1959) Detection, assay, and preliminary purification of the pigment controlling photoresponsive development of plants. Proc. Natl. Acad. Sci. U S A 45, 1703-1708.
    • (1959) Proc. Natl. Acad. Sci. U S A , vol.45 , pp. 1703-1708
    • Butler, W.L.1    Norris, K.H.2    Siegelman, H.W.3    Hendricks, S.B.4
  • 6
    • 0030865349 scopus 로고    scopus 로고
    • A cyanobacterial phytochrome two-component light sensory system
    • Yeh, K.-C., S.-H. Wu, J. T. Murphy, and, 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
  • 7
    • 0033601199 scopus 로고    scopus 로고
    • Bacteriophytochromes: Phytochrome-like photoreceptors from nonphotosynthetic eubacteria
    • Davis, S. J., A. V. Vener, and, R. D. Vierstra, (1999) Bacteriophytochromes: Phytochrome-like photoreceptors from nonphotosynthetic eubacteria. Science 286, 2517-2520.
    • (1999) Science , vol.286 , pp. 2517-2520
    • Davis, S.J.1    Vener, A.V.2    Vierstra, R.D.3
  • 8
    • 0036676141 scopus 로고    scopus 로고
    • Phytochrome ancestry: Sensors of bilins and light
    • Montgomery, B. L., and, J. C. Lagarias, (2002) Phytochrome ancestry: Sensors of bilins and light. Trends Plant Sci. 7, 357-366.
    • (2002) Trends Plant Sci. , vol.7 , pp. 357-366
    • Montgomery, B.L.1    Lagarias, J.C.2
  • 9
    • 27144507187 scopus 로고    scopus 로고
    • Phylogenetic analysis of the phytochrome superfamily reveals distinct microbial subfamilies of photoreceptors
    • Karniol, B., J. R. Wagner, J. M. Walker, and, R. D. Vierstra, (2005) Phylogenetic analysis of the phytochrome superfamily reveals distinct microbial subfamilies of photoreceptors. Biochem. J. 392, 103-116.
    • (2005) Biochem. J. , vol.392 , pp. 103-116
    • Karniol, B.1    Wagner, J.R.2    Walker, J.M.3    Vierstra, R.D.4
  • 10
    • 0035856979 scopus 로고    scopus 로고
    • Bacteriophytochromes are photochromic histidine kinases using a biliverdin chromophore
    • Bhoo, S.-H., S. J. Davis, J. Walker, B. Karniol, and, R. D. Vierstra, (2001) Bacteriophytochromes are photochromic histidine kinases using a biliverdin chromophore. Nature 414, 776-779.
    • (2001) Nature , vol.414 , pp. 776-779
    • Bhoo, S.-H.1    Davis, S.J.2    Walker, J.3    Karniol, B.4    Vierstra, R.D.5
  • 13
    • 0034485626 scopus 로고    scopus 로고
    • Novel putative photoreceptor and regulatory genes required for the positive phototactic movement of the unicellular motile cyanobacterium Synechocystis sp. PCC 6803
    • Yoshihara, S., F. Suzuki, H. Fujita, X. X. Geng, and, M. Ikeuchi, (2000) Novel putative photoreceptor and regulatory genes required for the positive phototactic movement of the unicellular motile cyanobacterium Synechocystis sp. PCC 6803. Plant Cell Physiol. 41, 1299-1304.
    • (2000) Plant Cell Physiol. , vol.41 , pp. 1299-1304
    • Yoshihara, S.1    Suzuki, F.2    Fujita, H.3    Geng, X.X.4    Ikeuchi, M.5
  • 15
    • 0000507396 scopus 로고
    • Self-assembly of synthetic phytochrome holoprotein in vitro
    • Lagarias, J. C., and, D. M. Lagarias, (1989) Self-assembly of synthetic phytochrome holoprotein in vitro. Proc. Natl. Acad. Sci. U S A 86, 5778-5780.
    • (1989) Proc. Natl. Acad. Sci. U S A , vol.86 , pp. 5778-5780
    • Lagarias, J.C.1    Lagarias, D.M.2
  • 17
    • 10644231202 scopus 로고    scopus 로고
    • The phytochromes: Spectroscopy and function
    • (Edited by A. Batschauer), Royal Society of Chemistry, Cambridge
    • Gärtner, W., and, S. E. Braslavsky, (2004) The phytochromes: Spectroscopy and function. In Photoreceptors and Light Signalling (Edited by, A. Batschauer,), pp. 136-180. Royal Society of Chemistry, Cambridge.
    • (2004) Photoreceptors and Light Signalling , pp. 136-180
    • Gärtner, W.1    Braslavsky, S.E.2
  • 18
    • 84866449983 scopus 로고    scopus 로고
    • Kurt Schaffner: From organic photochemistry to photobiology
    • Gärtner, W., (2012) Kurt Schaffner: From organic photochemistry to photobiology. Photochem. Photobiol. Sci. 11, 872-880.
    • (2012) Photochem. Photobiol. Sci. , vol.11 , pp. 872-880
    • Gärtner, W.1
  • 19
    • 84945738848 scopus 로고
    • Absorption spectra of phytochrome intermediates
    • Eilfeld, P., and, W. Rüdiger, (1985) Absorption spectra of phytochrome intermediates. Z. Naturforschung 40c, 109-114.
    • (1985) Z. Naturforschung , vol.40 C , pp. 109-114
    • Eilfeld, P.1    Rüdiger, W.2
  • 22
    • 0042068123 scopus 로고    scopus 로고
    • Dimers of the N-terminal domain of phytochrome B are functional in the nucleus
    • Matsushita, T., N. Mochizuki, and, A. Nagatani, (2003) Dimers of the N-terminal domain of phytochrome B are functional in the nucleus. Nature 424, 571-574.
    • (2003) Nature , vol.424 , pp. 571-574
    • Matsushita, T.1    Mochizuki, N.2    Nagatani, A.3
  • 23
    • 78049254337 scopus 로고    scopus 로고
    • Phytochrome: Structural basis for its functions
    • Nagatani, A., (2010) Phytochrome: Structural basis for its functions. Curr. Opin. Plant Biol. 13, 565-570.
    • (2010) Curr. Opin. Plant Biol. , vol.13 , pp. 565-570
    • Nagatani, A.1
  • 24
    • 77953240876 scopus 로고    scopus 로고
    • Phytochrome three-dimensional structures and functions
    • Hughes, J., (2010) Phytochrome three-dimensional structures and functions. Biochem. Soc. Trans. 38, 710-716.
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 710-716
    • Hughes, J.1
  • 25
    • 0009853585 scopus 로고
    • Proposal on the nature of phytochrome action based on the C-terminal sequences of phytochromes
    • Schneider-Poetsch, H. A. W., and, B. Braun, (1991) Proposal on the nature of phytochrome action based on the C-terminal sequences of phytochromes. J. Plant Physiol. 137, 576-580.
    • (1991) J. Plant Physiol. , vol.137 , pp. 576-580
    • Schneider-Poetsch, H.A.W.1    Braun, B.2
  • 26
    • 0026728663 scopus 로고
    • Phytochrome requires the 6-kDa N-terminal domain for full biological activity
    • Cherry, J. R., D. Hondred, J. M. Walker, and, R. D. Vierstra, (1992) Phytochrome requires the 6-kDa N-terminal domain for full biological activity. Proc. Natl. Acad. Sci. U S A 89, 5039-5043.
    • (1992) Proc. Natl. Acad. Sci. U S A , vol.89 , pp. 5039-5043
    • Cherry, J.R.1    Hondred, D.2    Walker, J.M.3    Vierstra, R.D.4
  • 27
    • 33847294249 scopus 로고    scopus 로고
    • The serine-rich N-terminal region of Arabidopsis phytochrome A is required for protein stability
    • Trupkin, S. A., D. Debrieux, A. Hiltbrunner, C. Fankhauser, and, J. J. Casal, (2007) The serine-rich N-terminal region of Arabidopsis phytochrome A is required for protein stability. Plant Mol. Biol. 63, 669-678.
    • (2007) Plant Mol. Biol. , vol.63 , pp. 669-678
    • Trupkin, S.A.1    Debrieux, D.2    Hiltbrunner, A.3    Fankhauser, C.4    Casal, J.J.5
  • 30
    • 0015230703 scopus 로고
    • Isolation and partial characterization of a chromophore-peptide fragment from pepsin digests of phytochrome
    • Fry, K. T., and, F. E. Mumford, (1971) Isolation and partial characterization of a chromophore-peptide fragment from pepsin digests of phytochrome. Biochem. Biophys. Res. Commun. 45, 1466-1473.
    • (1971) Biochem. Biophys. Res. Commun. , vol.45 , pp. 1466-1473
    • Fry, K.T.1    Mumford, F.E.2
  • 31
    • 1642276701 scopus 로고    scopus 로고
    • The biliverdin chromophore binds covalently to a conserved cysteine residue in the N-terminus of Agrobacterium phytochrome Agp1
    • Lamparter, T., M. Carrascal, N. Michael, E. Martinez, G. Rottwinkel, and, J. Abian, (2004) The biliverdin chromophore binds covalently to a conserved cysteine residue in the N-terminus of Agrobacterium phytochrome Agp1. Biochemistry 43, 3659-3669.
    • (2004) Biochemistry , vol.43 , pp. 3659-3669
    • Lamparter, T.1    Carrascal, M.2    Michael, N.3    Martinez, E.4    Rottwinkel, G.5    Abian, J.6
  • 32
    • 0024760523 scopus 로고
    • Novel phytochrome sequences in Arabidopsis thaliana: Structure, evolution, and differential expression of a plant regulatory photoreceptor family
    • Sharrock, R. A., and, P. H. Quail, (1989) Novel phytochrome sequences in Arabidopsis thaliana: Structure, evolution, and differential expression of a plant regulatory photoreceptor family. Genes Dev. 3, 1745-1757.
    • (1989) Genes Dev. , vol.3 , pp. 1745-1757
    • Sharrock, R.A.1    Quail, P.H.2
  • 33
    • 0033993308 scopus 로고    scopus 로고
    • Phytochromes, cryptochromes, phototropin: Photoreceptor interactions in plants
    • Casal, J. J., (2000) Phytochromes, cryptochromes, phototropin: Photoreceptor interactions in plants. Photochem. Photobiol. 71, 1-11.
    • (2000) Photochem. Photobiol. , vol.71 , pp. 1-11
    • Casal, J.J.1
  • 34
    • 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, and, 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
  • 35
    • 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. Stojkovic̈, J. Kuk, and, K. Moffat, (2007) Crystal structure of the chromophore binding domain of an unusual bacteriophytochrome, RpBphP3, reveals residues that modulate photoconversion. Proc. Natl. Acad. Sci. U S A 104, 12571-12576.
    • (2007) Proc. Natl. Acad. Sci. U S A , vol.104 , pp. 12571-12576
    • Yang, X.1    Stojkovic̈, E.A.2    Kuk, J.3    Moffat, K.4
  • 36
    • 55749108535 scopus 로고    scopus 로고
    • The structure of a complete phytochrome sensory module in the Pr ground state
    • Essen, L.-O., J. Mailliet, and, J. Hughes, (2008) The structure of a complete phytochrome sensory module in the Pr ground state. Proc. Natl. Acad. Sci. U S A 105, 14709-14714.
    • (2008) Proc. Natl. Acad. Sci. U S A , vol.105 , pp. 14709-14714
    • Essen, L.-O.1    Mailliet, J.2    Hughes, J.3
  • 37
    • 55749108880 scopus 로고    scopus 로고
    • Crystal structure of Pseudomonas aeruginosa bacteriophytochrome: Photoconversion and signal transduction
    • Yang, X., J. Kuk, and, K. Moffat, (2008) Crystal structure of Pseudomonas aeruginosa bacteriophytochrome: Photoconversion and signal transduction. Proc. Natl. Acad. Sci. U S A 105, 14715-14720.
    • (2008) Proc. Natl. Acad. Sci. U S A , vol.105 , pp. 14715-14720
    • Yang, X.1    Kuk, J.2    Moffat, K.3
  • 38
    • 70349461175 scopus 로고    scopus 로고
    • Conformational differences between the Pfr and Pr states in Pseudomonas aeruginosa bacteriophytochrome
    • Yang, X., J. Kuk, and, K. Moffat, (2009) Conformational differences between the Pfr and Pr states in Pseudomonas aeruginosa bacteriophytochrome. Proc. Natl. Acad. Sci. U S A 106, 15639-15644.
    • (2009) Proc. Natl. Acad. Sci. U S A , vol.106 , pp. 15639-15644
    • Yang, X.1    Kuk, J.2    Moffat, K.3
  • 40
    • 50249177040 scopus 로고    scopus 로고
    • Heteronuclear NMR investigation on the structure and dynamics of the chromophore binding pocket of the cyanobacterial phytochrome Cph1
    • Hahn, J., H. M. Strauss, and, P. Schmieder, (2008) Heteronuclear NMR investigation on the structure and dynamics of the chromophore binding pocket of the cyanobacterial phytochrome Cph1. J. Am. Chem. Soc. 130, 11170-11178.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 11170-11178
    • Hahn, J.1    Strauss, H.M.2    Schmieder, P.3
  • 41
    • 0029116739 scopus 로고
    • Fourier-transform resonance Raman spectroscopy of intermediates of the phytochrome photocycle
    • Matysik, J., P. Hildebrandt, W. Schlamann, S. E. Braslavsky, and, 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
  • 42
    • 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, and, 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
  • 43
    • 60549088102 scopus 로고    scopus 로고
    • Ultrafast excited-state isomerization in phytochrome revealed by femtosecond stimulated Raman spectroscopy
    • Dasgupta, J., R. R. Frontiera, K. C. Taylor, J. C. Lagarias, and, R. A. Mathies, (2009) Ultrafast excited-state isomerization in phytochrome revealed by femtosecond stimulated Raman spectroscopy. Proc. Natl. Acad. Sci. U S A 106, 1784-1789.
    • (2009) Proc. Natl. Acad. Sci. U S A , vol.106 , pp. 1784-1789
    • Dasgupta, J.1    Frontiera, R.R.2    Taylor, K.C.3    Lagarias, J.C.4    Mathies, R.A.5
  • 44
    • 34248359515 scopus 로고    scopus 로고
    • The chromophore structural changes during the photocycle of phytochrome: A combined resonance Raman and quantum chemical approach
    • Mroginski, M. A., D. H. Murgida, and, P. Hildebrandt, (2009) The chromophore structural changes during the photocycle of phytochrome: A combined resonance Raman and quantum chemical approach. Acc. Chem. Res. 40, 258-266.
    • (2009) Acc. Chem. Res. , vol.40 , pp. 258-266
    • Mroginski, M.A.1    Murgida, D.H.2    Hildebrandt, P.3
  • 47
    • 77950258115 scopus 로고    scopus 로고
    • Phytochrome as molecular machine: Revealing chromophore action during the Pfr → Pr photoconversion by magic-angle spinning NMR spectroscopy
    • Rohmer, T., C. Lang, C. Bongards, K. B. S. S. Gupta, J. Neugebauer, J. Hughes, W. Gärtner, and, J. Matysik, (2010) Phytochrome as molecular machine: Revealing chromophore action during the Pfr → Pr photoconversion by magic-angle spinning NMR spectroscopy. J. Am. Chem. Soc. 132, 4431-4437.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 4431-4437
    • Rohmer, T.1    Lang, C.2    Bongards, C.3    Gupta, K.B.S.S.4    Neugebauer, J.5    Hughes, J.6    Gärtner, W.7    Matysik, J.8
  • 49
    • 79952754070 scopus 로고    scopus 로고
    • Two ground state isoforms and a chromophore D-ring photoflip triggering extensive intramolecular changes in a canonical phytochrome
    • Song, C., G. Psakis, C. Lang, J. Mailliet, W. Gärtner, J. Hughes, and, J. Matysik, (2011) Two ground state isoforms and a chromophore D-ring photoflip triggering extensive intramolecular changes in a canonical phytochrome. Proc. Natl. Acad. Sci. U S A 108, 3842-3847.
    • (2011) Proc. Natl. Acad. Sci. U S A , vol.108 , pp. 3842-3847
    • Song, C.1    Psakis, G.2    Lang, C.3    Mailliet, J.4    Gärtner, W.5    Hughes, J.6    Matysik, J.7
  • 50
    • 81555214075 scopus 로고    scopus 로고
    • Temperature-scan crystallography reveals reaction intermediates in bacteriophytochrome
    • Yang, X., R. Zhong, J. Kuk, and, K. Moffat, (2011) Temperature-scan crystallography reveals reaction intermediates in bacteriophytochrome. Nature 479, 428-432.
    • (2011) Nature , vol.479 , pp. 428-432
    • Yang, X.1    Zhong, R.2    Kuk, J.3    Moffat, K.4
  • 52
    • 0031264390 scopus 로고    scopus 로고
    • Large-scale generation of affinity-purified recombinant phytochrome chromopeptide
    • Mozley, D., A. Remberg, and, W. Gärtner, (1997) Large-scale generation of affinity-purified recombinant phytochrome chromopeptide. Photochem. Photobiol. 66, 710-715.
    • (1997) Photochem. Photobiol. , vol.66 , pp. 710-715
    • Mozley, D.1    Remberg, A.2    Gärtner, W.3
  • 53
    • 0035725360 scopus 로고    scopus 로고
    • Phytochrome Cph1 from the cyanobacterium Synechocystis PCC6803. Purification, assembly, and quaternary structure
    • Lamparter, T., B. Esteban, and, 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
  • 54
    • 21844477536 scopus 로고    scopus 로고
    • Light-dependent dimerisation in the N-terminal sensory module of cyanobacterial phytochrome 1
    • Strauss, H. M., P. Schmieder, and, 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
  • 55
    • 20444369555 scopus 로고    scopus 로고
    • Heteronuclear solution-state NMR studies of the chromophore in cyanobacterial phytochrome Cph1
    • Strauss, H. M., J. Hughes, and, P. Schmieder, (2005) Heteronuclear solution-state NMR studies of the chromophore in cyanobacterial phytochrome Cph1. Biochemistry 44, 8244-8250.
    • (2005) Biochemistry , vol.44 , pp. 8244-8250
    • Strauss, H.M.1    Hughes, J.2    Schmieder, P.3
  • 56
    • 0037038365 scopus 로고    scopus 로고
    • Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy
    • Castellani, F., B. van Rossum, A. Diehl, M. Schubert, K. Rehbein, and, H. Oschkinat, (2002) Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy. Nature 420, 98-102.
    • (2002) Nature , vol.420 , pp. 98-102
    • Castellani, F.1    Van Rossum, B.2    Diehl, A.3    Schubert, M.4    Rehbein, K.5    Oschkinat, H.6
  • 57
    • 20944434430 scopus 로고    scopus 로고
    • Protein structure determination by high-resolution solid-state NMR spectroscopy: Application to microcrystalline ubiquitin
    • Zech, S. G., A. J. Wand, and, A. E. McDermott, (2005) Protein structure determination by high-resolution solid-state NMR spectroscopy: Application to microcrystalline ubiquitin. J. Am. Chem. Soc. 127, 8618-8626.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 8618-8626
    • Zech, S.G.1    Wand, A.J.2    McDermott, A.E.3
  • 58
    • 17044380266 scopus 로고    scopus 로고
    • A concept for rapid protein-structure determination by solid-state NMR spectroscopy
    • Lange, A., S. Becker, K. Seidel, K. Giller, O. Pongs, and, M. Baldus, (2005) A concept for rapid protein-structure determination by solid-state NMR spectroscopy. Angew. Chem. Int. Ed. 44, 2089-2092.
    • (2005) Angew. Chem. Int. Ed. , vol.44 , pp. 2089-2092
    • Lange, A.1    Becker, S.2    Seidel, K.3    Giller, K.4    Pongs, O.5    Baldus, M.6
  • 59
    • 36849019979 scopus 로고    scopus 로고
    • NMR studies on fully hydrated membrane proteins, with emphasis on bacteriorhodopsin as a typical and prototype membrane protein
    • Saitô, H., and, A. Naito, (2007) NMR studies on fully hydrated membrane proteins, with emphasis on bacteriorhodopsin as a typical and prototype membrane protein. Biochim. Biophys. Acta 1768, 3145-3161.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 3145-3161
    • Saitô, H.1    Naito, A.2
  • 60
    • 84859912916 scopus 로고    scopus 로고
    • Membrane protein structure and dynamics from NMR spectroscopy
    • Hong, M., Y. Zhang, and, F. Hu, (2012) Membrane protein structure and dynamics from NMR spectroscopy. Annu. Rev. Phys. Chem. 63, 1-24.
    • (2012) Annu. Rev. Phys. Chem. , vol.63 , pp. 1-24
    • Hong, M.1    Zhang, Y.2    Hu, F.3
  • 61
    • 84861384852 scopus 로고    scopus 로고
    • Solid-state NMR spectroscopic study of chromophore-protein interactions in the Pr ground state of plant phytochrome A
    • Song, C., L.-O. Essen, W. Gärtner, J. Hughes, and, J. Matysik, (2012) Solid-state NMR spectroscopic study of chromophore-protein interactions in the Pr ground state of plant phytochrome A. Mol. Plant 5, 698-715.
    • (2012) Mol. Plant , vol.5 , pp. 698-715
    • Song, C.1    Essen, L.-O.2    Gärtner, W.3    Hughes, J.4    Matysik, J.5
  • 65
    • 80053313196 scopus 로고    scopus 로고
    • Spectroscopy and a high-resolution crystal structure of Tyr-263 mutant of cyanobacterial phytochrome Cph1
    • Mailliet, J., G. Psakis, V. Sineshchekov, L.-O. Essen, and, J. Hughes, (2011) Spectroscopy and a high-resolution crystal structure of Tyr-263 mutant of cyanobacterial phytochrome Cph1. J. Mol. Biol. 413, 115-127.
    • (2011) J. Mol. Biol. , vol.413 , pp. 115-127
    • Mailliet, J.1    Psakis, G.2    Sineshchekov, V.3    Essen, L.-O.4    Hughes, J.5
  • 67
    • 0036110408 scopus 로고    scopus 로고
    • Fluorescence investigation of the recombinant cyanobacterial phytochrome (Cph1) and its C-terminally truncated monomeric species (Cph1Δ2): Implication for holoprotein assembly, chromophore-apoprotein interaction and photochemistry
    • Sineshchekov, V., L. Koppel, B. Esteban, J. Hughes, and, T. Lamparter, (2002) Fluorescence investigation of the recombinant cyanobacterial phytochrome (Cph1) and its C-terminally truncated monomeric species (Cph1Δ2): Implication for holoprotein assembly, chromophore-apoprotein interaction and photochemistry. J. Photochem. Photobiol., B 67, 39-50.
    • (2002) J. Photochem. Photobiol., B , vol.67 , pp. 39-50
    • Sineshchekov, V.1    Koppel, L.2    Esteban, B.3    Hughes, J.4    Lamparter, T.5
  • 68
    • 0032006164 scopus 로고    scopus 로고
    • Fluorescence spectroscopy and photochemistry of phytochromes A and B in wild-type, mutant and transgenic strains of Arabidopsis thaliana
    • Sineshchekov, V. A., O. B. Ogorodnikova, P. F. Devlin, and, G. C. Whitelam, (1998) Fluorescence spectroscopy and photochemistry of phytochromes A and B in wild-type, mutant and transgenic strains of Arabidopsis thaliana. J. Photochem. Photobiol., B 42, 133-142.
    • (1998) J. Photochem. Photobiol., B , vol.42 , pp. 133-142
    • Sineshchekov, V.A.1    Ogorodnikova, O.B.2    Devlin, P.F.3    Whitelam, G.C.4
  • 69
    • 33748997393 scopus 로고    scopus 로고
    • Two native pools of phytochrome A in monocots: Evidence from fluorescence investigations of phytochrome mutants of rice
    • Sineshchekov, V., A. Loskovich, N. Inagaki, and, M. Takano, (2006) Two native pools of phytochrome A in monocots: Evidence from fluorescence investigations of phytochrome mutants of rice. Photochem. Photobiol. 82, 1116-1122.
    • (2006) Photochem. Photobiol. , vol.82 , pp. 1116-1122
    • Sineshchekov, V.1    Loskovich, A.2    Inagaki, N.3    Takano, M.4
  • 70
    • 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, and, 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
  • 71
    • 77952688009 scopus 로고    scopus 로고
    • Proton-transfer and hydrogen-bond interactions determine fluorescence quantum yield and photochemical efficiency of bacteriophytochrome
    • Toh, K. C., E. A. Stojkovic̈, I. H. M. van Stokkum, K. Moffat, and, J. T. M. Kennis, (2010) Proton-transfer and hydrogen-bond interactions determine fluorescence quantum yield and photochemical efficiency of bacteriophytochrome. Proc. Natl. Acad. Sci. U S A 107, 9170-9175.
    • (2010) Proc. Natl. Acad. Sci. U S A , vol.107 , pp. 9170-9175
    • Toh, K.C.1    Stojkovic̈, E.A.2    Van Stokkum, I.H.M.3    Moffat, K.4    Kennis, J.T.M.5
  • 73
    • 45549107695 scopus 로고    scopus 로고
    • Mutational analysis of Deinococcus radiodurans bacteriophytochrome reveals key amino acids necessary for the phytochromicity and proton exchange cycle of phytochromes
    • Wagner, J. R., J. Zhang, D. von Stetten, M. Günther, D. H. Murgida, M. A. Mroginski, J. M. Walker, K. T. Forest, P. Hildebrandt, and, R. D. Vierstra, (2008) Mutational analysis of Deinococcus radiodurans bacteriophytochrome reveals key amino acids necessary for the phytochromicity and proton exchange cycle of phytochromes. 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
  • 75
    • 84856719199 scopus 로고    scopus 로고
    • Conformational homogeneity and excited-state isomerization dynamics of the bilin chromophore in phytochrome Cph1 from resonance Raman intensities
    • Spillane, K. M., J. Dasgupta, and, R. A. Mathies, (2012) Conformational homogeneity and excited-state isomerization dynamics of the bilin chromophore in phytochrome Cph1 from resonance Raman intensities. Biophys. J. 102, 709-717.
    • (2012) Biophys. J. , vol.102 , pp. 709-717
    • Spillane, K.M.1    Dasgupta, J.2    Mathies, R.A.3
  • 76
    • 0034734230 scopus 로고    scopus 로고
    • Proton transport by sensory rhodopsin and its modulation by transducer-binding
    • Sasaki, J., and, J. L. Spudich, (2000) Proton transport by sensory rhodopsin and its modulation by transducer-binding. Biochim. Biophys. Acta 1460, 230-239.
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 230-239
    • Sasaki, J.1    Spudich, J.L.2
  • 77
    • 2342460436 scopus 로고    scopus 로고
    • Bacteriorhodopsin
    • Lanyi, J. K., (2004) Bacteriorhodopsin. Annu. Rev. Physiol. 66, 665-688.
    • (2004) Annu. Rev. Physiol. , vol.66 , pp. 665-688
    • Lanyi, J.K.1
  • 78
    • 77952906089 scopus 로고    scopus 로고
    • Structure and activation of the visual pigment rhodopsin
    • Smith, S. O., (2010) Structure and activation of the visual pigment rhodopsin. Annu. Rev. Biophys. 39, 309-328.
    • (2010) Annu. Rev. Biophys. , vol.39 , pp. 309-328
    • Smith, S.O.1
  • 79
    • 43049143068 scopus 로고    scopus 로고
    • Which factors determine the acidity of the phytochromobilin chromophore of plant phytochrome?
    • Borg, O. A., and, B. Durbeej, (2008) Which factors determine the acidity of the phytochromobilin chromophore of plant phytochrome? Phys. Chem. Chem. Phys. 10, 2528-2537.
    • (2008) Phys. Chem. Chem. Phys. , vol.10 , pp. 2528-2537
    • Borg, O.A.1    Durbeej, B.2
  • 80
    • 12144264399 scopus 로고    scopus 로고
    • Light-induced conformational changes of cyanobacterial phytochrome Cph1 probed by limited proteolysis and autophosphorylation
    • Esteban, B., M. Carrascal, J. Abian, and, T. Lamparter, (2005) Light-induced conformational changes of cyanobacterial phytochrome Cph1 probed by limited proteolysis and autophosphorylation. Biochemistry 44, 450-461.
    • (2005) Biochemistry , vol.44 , pp. 450-461
    • Esteban, B.1    Carrascal, M.2    Abian, J.3    Lamparter, T.4
  • 81
    • 0033716604 scopus 로고    scopus 로고
    • Reaction control in bacteriorhodopsin: Impact of Arg82 and Asp85 on the fast retinal isomerization, studied in the second site revertant Arg82Ala/Gly231Cys and various purple and blue forms of bacteriorhodopsin
    • Heyne, K., J. Herbst, B. Dominguez-Herradon, U. Alexiev, and, R. Diller, (2000) Reaction control in bacteriorhodopsin: Impact of Arg82 and Asp85 on the fast retinal isomerization, studied in the second site revertant Arg82Ala/Gly231Cys and various purple and blue forms of bacteriorhodopsin. J. Phys. Chem. B 104, 6053-6058.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 6053-6058
    • Heyne, K.1    Herbst, J.2    Dominguez-Herradon, B.3    Alexiev, U.4    Diller, R.5
  • 85
    • 0030482839 scopus 로고    scopus 로고
    • Resonance Raman analysis of chromophore structure in the Lumi-R photoproduct of phytochrome
    • Andel, F. III, J. C. Lagarias, and, R. A. Mathies, (1996) Resonance Raman analysis of chromophore structure in the Lumi-R photoproduct of phytochrome. Biochemistry 35, 15997-16008.
    • (1996) Biochemistry , vol.35 , pp. 15997-16008
    • Andel Iii, F.1    Lagarias, J.C.2    Mathies, R.A.3
  • 86
    • 59249100338 scopus 로고    scopus 로고
    • Residues clustered in the light-sensing knot of phytochrome B are necessary for conformer-specific binding to signalling partner PIF3
    • Kikis, E. A., Y. Oka, M. E. Hudson, A. Nagatani, and, P. H. Quail, (2009) Residues clustered in the light-sensing knot of phytochrome B are necessary for conformer-specific binding to signalling partner PIF3. PLoS Genet. 5, e1000352.
    • (2009) PLoS Genet. , vol.5
    • Kikis, E.A.1    Oka, Y.2    Hudson, M.E.3    Nagatani, A.4    Quail, P.H.5
  • 87
    • 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, and, 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
  • 89
    • 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, I. van der Hoef, J. Lugtenburg, J. C. Lagarias, and, 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 Der Hoef, I.5    Lugtenburg, J.6    Lagarias, J.C.7    Mathies, R.A.8
  • 90
    • 58349119908 scopus 로고    scopus 로고
    • The photoreactions of recombinant phytochrome CphA from the cyanobacterium Calothrix PCC7601: A low-temperature UV-Vis and FTIR study
    • Schwinté, P., W. Gärtner, S. Sharda, M.-A. Mroginski, P. Hildebrandt, and, F. Siebert, (2009) The photoreactions of recombinant phytochrome CphA from the cyanobacterium Calothrix PCC7601: A low-temperature UV-Vis and FTIR study. Photochem. Photobiol. 85, 239-249.
    • (2009) Photochem. Photobiol. , vol.85 , pp. 239-249
    • Schwinté, P.1    Gärtner, W.2    Sharda, S.3    Mroginski, M.-A.4    Hildebrandt, P.5    Siebert, F.6
  • 91
    • 33751332610 scopus 로고
    • Discovery of a neutral-to-ionic phase transition in organic materials
    • Torrance, J. B., J. E. Vazquez, J. J. Mayerle, and, V. Y. Lee, (1981) Discovery of a neutral-to-ionic phase transition in organic materials. Phys. Rev. Lett. 46, 253-257.
    • (1981) Phys. Rev. Lett. , vol.46 , pp. 253-257
    • Torrance, J.B.1    Vazquez, J.E.2    Mayerle, J.J.3    Lee, V.Y.4
  • 93
    • 0022443111 scopus 로고
    • Domain wall picture of the neutral-ionic transition in TTF-chloranil
    • Nagaosa, N., (1986) Domain wall picture of the neutral-ionic transition in TTF-chloranil. Solid State Commun. 57, 179-183.
    • (1986) Solid State Commun. , vol.57 , pp. 179-183
    • Nagaosa, N.1
  • 94
    • 78650885619 scopus 로고    scopus 로고
    • Engineered photoreceptors as novel optogenetic tools
    • Möglich, A., and, K. Moffat, (2010) Engineered photoreceptors as novel optogenetic tools. Photochem. Photobiol. Sci. 9, 1286-1300.
    • (2010) Photochem. Photobiol. Sci. , vol.9 , pp. 1286-1300
    • Möglich, A.1    Moffat, K.2
  • 95
    • 0030601588 scopus 로고    scopus 로고
    • Excited state dynamics of bacteriorhodopsin revealed by transient stimulated emission spectra
    • Haran, G., K. Wynne, A. Xie, Q. He, M. Chance, and, R. M. Hochstrasser, (1996) Excited state dynamics of bacteriorhodopsin revealed by transient stimulated emission spectra. Chem. Phys. Lett. 261, 389-395.
    • (1996) Chem. Phys. Lett. , vol.261 , pp. 389-395
    • Haran, G.1    Wynne, K.2    Xie, A.3    He, Q.4    Chance, M.5    Hochstrasser, R.M.6
  • 96
    • 0001862310 scopus 로고
    • Cis-trans Photoisomerization of stilbenes and stilbene-like molecules
    • 19, (Edited by D. C. Neckers, D. C. Volman, and G. von Bünau), John Wiley & Sons, Hoboken, NJ
    • Görner, H., and, H. J. Kuhn, (1995) cis-trans Photoisomerization of stilbenes and stilbene-like molecules. In Advances in Photochemistry, Vol. 19, (Edited by, D. C. Neckers, D. C. Volman, and, G. von Bünau,), pp. 1-117. John Wiley & Sons, Hoboken, NJ.
    • (1995) Advances in Photochemistry , pp. 1-117
    • Görner, H.1    Kuhn, H.J.2
  • 101
    • 0036681042 scopus 로고    scopus 로고
    • Introduction to the physics of Brownian motors
    • Reimann, P., and, P. Hänggi, (2002) Introduction to the physics of Brownian motors. Appl. Phys. 75, 169-178.
    • (2002) Appl. Phys. , vol.75 , pp. 169-178
    • Reimann, P.1    Hänggi, P.2
  • 102
    • 64349105027 scopus 로고    scopus 로고
    • Artificial Brownian motors: Controlling transport on the nanoscale
    • Hänggi, P., and, F. Marchesoni, (2009) Artificial Brownian motors: Controlling transport on the nanoscale. Rev. Mod. Phys. 81, 387-442.
    • (2009) Rev. Mod. Phys. , vol.81 , pp. 387-442
    • Hänggi, P.1    Marchesoni, F.2
  • 103
    • 0036179557 scopus 로고    scopus 로고
    • Brownian motors: Noisy transport far from equilibrium
    • Reimann, P., (2002) Brownian motors: Noisy transport far from equilibrium. Phys. Rep. 361, 57-265.
    • (2002) Phys. Rep. , vol.361 , pp. 57-265
    • Reimann, P.1
  • 104
    • 33846152351 scopus 로고    scopus 로고
    • Synthetic molecular motors and mechanical machines
    • Kay, E. R., D. A. Leigh, and, F. Zerbetto, (2007) Synthetic molecular motors and mechanical machines. Angew. Chem. Int. Ed. 46, 72-191.
    • (2007) Angew. Chem. Int. Ed. , vol.46 , pp. 72-191
    • Kay, E.R.1    Leigh, D.A.2    Zerbetto, F.3
  • 106
    • 33847353060 scopus 로고    scopus 로고
    • Making molecular machines work
    • Browne, W. R., and, B. L. Feringa, (2006) Making molecular machines work. Nat. Nanotech. 1, 25-35.
    • (2006) Nat. Nanotech. , vol.1 , pp. 25-35
    • Browne, W.R.1    Feringa, B.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.