메뉴 건너뛰기




Volumn 37, Issue 1, 2004, Pages 13-20

Photoreceptor Proteins, "Star Actors of Modern Times": A Review of the Functional Dynamics in the Structure of Representative Members of Six Different Photoreceptor Families

Author keywords

[No Author keywords available]

Indexed keywords

BLUF PROTEIN; CRYPTOCHROME; FLAVOPROTEIN; PARA COUMARIC ACID; PHOTOTROPIN; PHYTOCHROME; PHYTOCHROMOBILIN; PIGMENT; PROTEIN; QUERCETIN; RETINAL; RHODOPSIN; UNCLASSIFIED DRUG; VISUAL PROTEINS AND PIGMENTS; XANTHOPSIN;

EID: 1642453927     PISSN: 00014842     EISSN: None     Source Type: Journal    
DOI: 10.1021/ar020219d     Document Type: Article
Times cited : (337)

References (69)
  • 3
    • 0030906654 scopus 로고    scopus 로고
    • Molecular mechanism of photosignaling by archaeal sensory rhodopsins
    • Hoff, W. D.; Jung, K. H.; Spudich, J. L. Molecular mechanism of photosignaling by archaeal sensory rhodopsins. Annu. Rev. Biophys. Biomol. Struct. 1997, 26, 223-258.
    • (1997) Annu. Rev. Biophys. Biomol. Struct. , vol.26 , pp. 223-258
    • Hoff, W.D.1    Jung, K.H.2    Spudich, J.L.3
  • 4
    • 0032578425 scopus 로고    scopus 로고
    • The phytochrome family: Dissection of functional roles and signalling pathways among family members
    • Quail, P. H. The phytochrome family: dissection of functional roles and signalling pathways among family members. Philos. Trans. R. Soc. London B: Biol. Sci. 1998, 353, 1399-1403.
    • (1998) Philos. Trans. R. Soc. London B: Biol. Sci. , vol.353 , pp. 1399-1403
    • Quail, P.H.1
  • 6
    • 0027493250 scopus 로고
    • HY4 gene of A thaliana encodes a protein with characteristics of a blue-light photoreceptor
    • Ahmad, M.; Cashmore, A. R. HY4 gene of A thaliana encodes a protein with characteristics of a blue-light photoreceptor. Nature 1993, 366, 162-166.
    • (1993) Nature , vol.366 , pp. 162-166
    • Ahmad, M.1    Cashmore, A.R.2
  • 7
    • 0031470701 scopus 로고    scopus 로고
    • Arabidopsis NPH1: A protein kinase with a putative redox-sensing domain
    • Huala, E.; Oeller, P. W.; Liscum, E.; Han, I. S.; Larsen, E.; Briggs, W. R. Arabidopsis NPH1: a protein kinase with a putative redox-sensing domain. Science 1997, 278, 2120-2123.
    • (1997) Science , vol.278 , pp. 2120-2123
    • Huala, E.1    Oeller, P.W.2    Liscum, E.3    Han, I.S.4    Larsen, E.5    Briggs, W.R.6
  • 8
    • 0036804709 scopus 로고    scopus 로고
    • BLUF a novel FAD-binding domain involved in sensory transduction in microorganisms
    • Gomelsky, M.; Klug, G. BLUF: a novel FAD-binding domain involved in sensory transduction in microorganisms. Trends Biochem. Sci. 2002, 27, 497-500.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 497-500
    • Gomelsky, M.1    Klug, G.2
  • 9
    • 0036016438 scopus 로고    scopus 로고
    • Photoexcited structure of a plant photoreceptor domain reveals a light-driven molecular switch
    • Crosson, S.; Moffat, K. Photoexcited structure of a plant photoreceptor domain reveals a light-driven molecular switch. Plant Cell 2002, 14, 1067-1075.
    • (2002) Plant Cell , vol.14 , pp. 1067-1075
    • Crosson, S.1    Moffat, K.2
  • 10
    • 0035853757 scopus 로고    scopus 로고
    • Blue light sensing in higher plants
    • Christie, J. M.; Briggs, W. R. Blue light sensing in higher plants. J. Biol. Chem. 2001, 276, 11457-11460.
    • (2001) J. Biol. Chem. , vol.276 , pp. 11457-11460
    • Christie, J.M.1    Briggs, W.R.2
  • 11
    • 0035146338 scopus 로고    scopus 로고
    • Photoreceptors in plant photomorphogenesis to date. Five phytochromes, two cryptochromes, one phototropin, and one superchrome
    • Briggs, W. R.; Olney, M. A. Photoreceptors in plant photomorphogenesis to date. Five phytochromes, two cryptochromes, one phototropin, and one superchrome. Plant Physiol. 2001, 125, 85-88.
    • (2001) Plant Physiol. , vol.125 , pp. 85-88
    • Briggs, W.R.1    Olney, M.A.2
  • 12
    • 0036427580 scopus 로고    scopus 로고
    • The molecular basis of sensing and responding to light in microorganisms
    • Hellingwerf, K. J. The molecular basis of sensing and responding to light in microorganisms. Antonie Van Leeuwenhoek 2002, 81, 51-59.
    • (2002) Antonie Van Leeuwenhoek , vol.81 , pp. 51-59
    • Hellingwerf, K.J.1
  • 13
    • 0037173051 scopus 로고    scopus 로고
    • Two rhodopsins mediate phototaxis to low- and high-intensity light in Chlamydomonas reinhardtii
    • Sineshchekov, O. A.; Jung, K. H.; Spudich, J. L. Two rhodopsins mediate phototaxis to low- and high-intensity light in Chlamydomonas reinhardtii. Proc. Natl. Acad. Sci. U.S.A. 2002, 99, 8689-8694.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 8689-8694
    • Sineshchekov, O.A.1    Jung, K.H.2    Spudich, J.L.3
  • 15
    • 0033607149 scopus 로고    scopus 로고
    • A eukaryotic protein, NOP-1, binds retinal to form an archaeal rhodopsin-like photochemically reactive pigment
    • Bieszke, J. A.; Spudich, E. N.; Scott, K. L.; Borkovich, K. A.; Spudich, J. L. A eukaryotic protein, NOP-1, binds retinal to form an archaeal rhodopsin-like photochemically reactive pigment. Biochemistry 1999, 38, 14138-14145.
    • (1999) Biochemistry , vol.38 , pp. 14138-14145
    • Bieszke, J.A.1    Spudich, E.N.2    Scott, K.L.3    Borkovich, K.A.4    Spudich, J.L.5
  • 17
    • 0037346546 scopus 로고    scopus 로고
    • Demonstration of a sensory rhodopsin in eubacteria
    • Jung, K. H.; Trivedi, V. D.; Spudich, J. L. Demonstration of a sensory rhodopsin in eubacteria. Mol. Microbiol. 2003, 47, 1513-1522.
    • (2003) Mol. Microbiol. , vol.47 , pp. 1513-1522
    • Jung, K.H.1    Trivedi, V.D.2    Spudich, J.L.3
  • 20
    • 0016842810 scopus 로고
    • Three-dimensional model of purple membrane obtained by electron microscopy
    • Henderson, R.; Unwin, P. N. Three-dimensional model of purple membrane obtained by electron microscopy. Nature 1975, 257, 28-32.
    • (1975) Nature , vol.257 , pp. 28-32
    • Henderson, R.1    Unwin, P.N.2
  • 21
    • 0037008526 scopus 로고    scopus 로고
    • Femtosecond infrared spectroscopy of bacteriorhodopsin chromophore isomerization
    • Herbst, J.; Heyne, K.; Diller, R. Femtosecond infrared spectroscopy of bacteriorhodopsin chromophore isomerization. Science 2002, 297, 822-825.
    • (2002) Science , vol.297 , pp. 822-825
    • Herbst, J.1    Heyne, K.2    Diller, R.3
  • 22
    • 0034671339 scopus 로고    scopus 로고
    • Light-induced rotation of a transmembrane alpha-helix in bacteriorhodopsin
    • Xiao, W.; Brown, L. S.; Needleman, R.; Lanyi, J. K.; Shin, Y. K. Light-induced rotation of a transmembrane alpha-helix in bacteriorhodopsin. J. Mol. Biol. 2000, 304, 715-721.
    • (2000) J. Mol. Biol. , vol.304 , pp. 715-721
    • Xiao, W.1    Brown, L.S.2    Needleman, R.3    Lanyi, J.K.4    Shin, Y.K.5
  • 23
    • 0033536594 scopus 로고    scopus 로고
    • Structural changes in bacteriorhodopsin during ion transport at 2 angstrom resolution
    • Luecke, H.; Schobert, B.; Richter, H. T.; Cartailler, J. P.; Lanyi, J. K. Structural changes in bacteriorhodopsin during ion transport at 2 angstrom resolution. Science 1999, 286, 255-261.
    • (1999) Science , vol.286 , pp. 255-261
    • Luecke, H.1    Schobert, B.2    Richter, H.T.3    Cartailler, J.P.4    Lanyi, J.K.5
  • 24
    • 0036971196 scopus 로고    scopus 로고
    • Crystallographic structure of the K intermediate of bacteriorhodopsin: Conservation of free energy after photoisomerization of the retinal
    • Schobert, B.; Cupp-Vickery, J.; Hornak, V.; Smith, S.; Lanyi, J. Crystallographic structure of the K intermediate of bacteriorhodopsin: conservation of free energy after photoisomerization of the retinal. J. Mol. Biol. 2002, 321, 715-726.
    • (2002) J. Mol. Biol. , vol.321 , pp. 715-726
    • Schobert, B.1    Cupp-Vickery, J.2    Hornak, V.3    Smith, S.4    Lanyi, J.5
  • 25
    • 0036968773 scopus 로고    scopus 로고
    • Crystallographic structure of the retinal and the protein after deprotonation of the Schiff base: The switch in the bacteriorhodopsin photocycle
    • Lanyi, J.; Schobert, B. Crystallographic structure of the retinal and the protein after deprotonation of the Schiff base: the switch in the bacteriorhodopsin photocycle. J. Mol. Biol. 2002, 321, 727-737.
    • (2002) J. Mol. Biol. , vol.321 , pp. 727-737
    • Lanyi, J.1    Schobert, B.2
  • 27
    • 0035846382 scopus 로고    scopus 로고
    • Nature of the surface crossing process in bacteriorhodopsin: Computer simulations of the quantum dynamics of the primary photochemical event
    • Warshel, A.; Chu, Z. T. Nature of the surface crossing process in bacteriorhodopsin: Computer simulations of the quantum dynamics of the primary photochemical event. J. Phys. Chem. B 2001, 105, 9857-9871.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 9857-9871
    • Warshel, A.1    Chu, Z.T.2
  • 28
    • 0035336676 scopus 로고    scopus 로고
    • Activation of rhodopsin: New insights from structural and biochemical studies
    • Okada, T.; Ernst, O. P.; Palczewski, K.; Hofmann, K. P. Activation of rhodopsin: new insights from structural and biochemical studies. Trends Biochem. Sci. 2001, 26, 318-324.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 318-324
    • Okada, T.1    Ernst, O.P.2    Palczewski, K.3    Hofmann, K.P.4
  • 30
    • 0030295130 scopus 로고    scopus 로고
    • Nuclear localization activity of phytochrome B
    • Sakamoto, K.; Nagatani, A. Nuclear localization activity of phytochrome B. Plant J. 1996, 10, 859-868.
    • (1996) Plant J. , vol.10 , pp. 859-868
    • Sakamoto, K.1    Nagatani, A.2
  • 31
    • 0032506138 scopus 로고    scopus 로고
    • Eukaryotic phytochromes: Light-regulated serine/threonine protein kinases with histidine kinase ancestry
    • Yeh, K. C.; Lagarias, J. C. Eukaryotic phytochromes: light-regulated serine/threonine protein kinases with histidine kinase ancestry. Proc. Natl. Acad. Sci. U.S.A. 1998, 95, 13976-13981.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 13976-13981
    • Yeh, K.C.1    Lagarias, J.C.2
  • 32
    • 0029040034 scopus 로고
    • Phytochromes: Photosensory perception and signal transduction
    • Quail, P. H.; Boylan, M. T.; Parks, B. M.; Short, T. W.; Xu, Y.; Wagner, D. Phytochromes: photosensory perception and signal transduction. Science 1995, 268, 675-680.
    • (1995) Science , vol.268 , pp. 675-680
    • Quail, P.H.1    Boylan, M.T.2    Parks, B.M.3    Short, T.W.4    Xu, Y.5    Wagner, D.6
  • 34
    • 0033601199 scopus 로고    scopus 로고
    • Bacteriophytochromes: Phytochrome-like photoreceptors from nonphotosynthetic eubacteria
    • Davis, S. J.; Vener, A. V.; Vierstra, R. D. Bacteriophytochromes: phytochrome-like photoreceptors from nonphotosynthetic eubacteria. Science 1999, 286, 2517-2520.
    • (1999) Science , vol.286 , pp. 2517-2520
    • Davis, S.J.1    Vener, A.V.2    Vierstra, R.D.3
  • 36
    • 0033575370 scopus 로고    scopus 로고
    • Bacterial photoreceptor with similarity to photoactive yellow protein and plant phytochromes
    • Jiang, Z.; Swem, L. R.; Rushing, B. G.; Devanathan, S.; Tollin, G.; Bauer, C. E. Bacterial photoreceptor with similarity to photoactive yellow protein and plant phytochromes. Science 1999, 285, 406-409.
    • (1999) Science , vol.285 , pp. 406-409
    • Jiang, Z.1    Swem, L.R.2    Rushing, B.G.3    Devanathan, S.4    Tollin, G.5    Bauer, C.E.6
  • 37
    • 0037015009 scopus 로고    scopus 로고
    • Phytochrome from Agrobacterium tumefaciens has unusual spectral properties and reveals an N-terminal chromophore attachment site
    • Lamparter, T.; Michael, N.; Mittmann, F.; Esteban, B. Phytochrome from Agrobacterium tumefaciens has unusual spectral properties and reveals an N-terminal chromophore attachment site. Proc. Natl. Acad. Sci. U.S.A. 2002, 99, 11628-11633.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 11628-11633
    • Lamparter, T.1    Michael, N.2    Mittmann, F.3    Esteban, B.4
  • 38
    • 0036093923 scopus 로고    scopus 로고
    • The cyanobacterial phytochrome Cph2 inhibits phototaxis towards blue light
    • Wilde, A.; Fiedler, B.; Borner, T. The cyanobacterial phytochrome Cph2 inhibits phototaxis towards blue light. Mol. Microbiol. 2002, 44, 981-988.
    • (2002) Mol. Microbiol. , vol.44 , pp. 981-988
    • Wilde, A.1    Fiedler, B.2    Borner, T.3
  • 39
    • 0034604449 scopus 로고    scopus 로고
    • CikA, a bacteriophytochrome that resets the cyanobacterial circadian clock
    • Schmitz, O.; Katayama, M.; Williams, S. B.; Kondo, T.; Golden, S. S. CikA, a bacteriophytochrome that resets the cyanobacterial circadian clock. Science 2000, 289, 765-768.
    • (2000) Science , vol.289 , pp. 765-768
    • Schmitz, O.1    Katayama, M.2    Williams, S.B.3    Kondo, T.4    Golden, S.S.5
  • 40
    • 0032510475 scopus 로고    scopus 로고
    • Structure at 0.85 A resolution of an early protein photocycle intermediate
    • Genick, U. K.; Soltis, S. M.; Kuhn, P.; Canestrelli, I. L.; Getzoff, E. D. Structure at 0.85 A resolution of an early protein photocycle intermediate. Nature 1998, 392, 206-209.
    • (1998) Nature , vol.392 , pp. 206-209
    • Genick, U.K.1    Soltis, S.M.2    Kuhn, P.3    Canestrelli, I.L.4    Getzoff, E.D.5
  • 41
    • 0027324441 scopus 로고
    • The eubacterium Ectothiorhodospira halophila is negatively phototactic, with a wavelength dependence that fits the absorption spectrum of the photoactive yellow protein
    • Sprenger, W. W.; Hoff, W. D.; Armitage, J. P.; Hellingwerf, K. J. The eubacterium Ectothiorhodospira halophila is negatively phototactic, with a wavelength dependence that fits the absorption spectrum of the photoactive yellow protein. J. Bacteriol. 1993, 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
  • 43
    • 0029964634 scopus 로고    scopus 로고
    • Evidence for trans-cis isomerization of the p-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.; Hellingwerf, K. J. Evidence for trans-cis isomerization of the p-coumaric acid chromophore as the photochemical basis of the photocycle of photoactive yellow protein. FEBS Lett. 1996, 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
  • 44
    • 0030446427 scopus 로고    scopus 로고
    • Glu46 donates a proton to the 4-hydroxycinnamate anion chromophore during the photocycle of photoactive yellow protein
    • Xie, A.; Hoff, W. D.; Kroon, A. R.; Hellingwerf, K. J. Glu46 donates a proton to the 4-hydroxycinnamate anion chromophore during the photocycle of photoactive yellow protein. Biochemistry 1996, 35, 14671-14678.
    • (1996) Biochemistry , vol.35 , pp. 14671-14678
    • Xie, A.1    Hoff, W.D.2    Kroon, A.R.3    Hellingwerf, K.J.4
  • 45
    • 0029950952 scopus 로고    scopus 로고
    • Protein folding thermodynamics applied to the photocycle of the photoactive yellow protein
    • Van Brederode, M. E.; Hoff, W. D.; Van Stokkum, I. H.; Groot, M. L.; Hellingwerf, K. J. Protein folding thermodynamics applied to the photocycle of the photoactive yellow protein. Biophys. J. 1996, 71, 365-380.
    • (1996) Biophys. J. , vol.71 , pp. 365-380
    • Van Brederode, M.E.1    Hoff, W.D.2    Van Stokkum, I.H.3    Groot, M.L.4    Hellingwerf, K.J.5
  • 47
    • 0034660609 scopus 로고    scopus 로고
    • Bacterial cryptochrome and photolyase: Characterization of two photolyase-like genes of Synechocystis sp. PCC6803
    • Hitomi, K.; Okamoto, K.; Daiyasu, H.; Miyashita, H.; Iwai, S.; Toh, H.; Ishiura, M.; Todo, T. Bacterial cryptochrome and photolyase: characterization of two photolyase-like genes of Synechocystis sp. PCC6803. Nucleic Acids Res. 2000, 28, 2353-2362.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 2353-2362
    • Hitomi, K.1    Okamoto, K.2    Daiyasu, H.3    Miyashita, H.4    Iwai, S.5    Toh, H.6    Ishiura, M.7    Todo, T.8
  • 48
    • 0037071862 scopus 로고    scopus 로고
    • Regulation of Arabidopsis cryptochrome 2 by blue-light-dependent phosphorylation
    • Shalitin, D.; Yang, H.; Mockler, T. C.; Maymon, M.; Guo, H.; Whitelam, G. C.; Lin, C. Regulation of Arabidopsis cryptochrome 2 by blue-light-dependent phosphorylation. Nature 2002, 417, 763-767.
    • (2002) Nature , vol.417 , pp. 763-767
    • Shalitin, D.1    Yang, H.2    Mockler, T.C.3    Maymon, M.4    Guo, H.5    Whitelam, G.C.6    Lin, C.7
  • 49
    • 0033617475 scopus 로고    scopus 로고
    • Cryptochromes: Blue light receptors for plants and animals
    • Cashmore, A. R.; Jarillo, J. A.; Wu, Y. J.; Liu, D. Cryptochromes: blue light receptors for plants and animals. Science 1999, 284, 760-765.
    • (1999) Science , vol.284 , pp. 760-765
    • Cashmore, A.R.1    Jarillo, J.A.2    Wu, Y.J.3    Liu, D.4
  • 50
    • 0034214080 scopus 로고    scopus 로고
    • Intraprotein radical transfer during photoactivation of DNA photolyase
    • Aubert, C.; Vos, M. H.; Mathis, P.; Eker, A. P.; Brettel, K. Intraprotein radical transfer during photoactivation of DNA photolyase. Nature 2000, 405, 586-590.
    • (2000) Nature , vol.405 , pp. 586-590
    • Aubert, C.1    Vos, M.H.2    Mathis, P.3    Eker, A.P.4    Brettel, K.5
  • 52
    • 0036275942 scopus 로고    scopus 로고
    • Blue light receptors and signal transduction
    • Lin, C. Blue light receptors and signal transduction. Plant Cell 2002, 14, S207-S225.
    • (2002) Plant Cell , vol.14
    • Lin, C.1
  • 53
    • 0242381326 scopus 로고    scopus 로고
    • Light-induced fluorescence changes in Phycomyces: Evidence for blue light-receptor associated flavosemiquinones
    • Galland, P.; Tolle, N. Light-induced fluorescence changes in Phycomyces: evidence for blue light-receptor associated flavosemiquinones. Planta 2003, 217, 971-982.
    • (2003) Planta , vol.217 , pp. 971-982
    • Galland, P.1    Tolle, N.2
  • 54
    • 0036776294 scopus 로고    scopus 로고
    • Phototropin LOV domains exhibit distinct roles in regulating photoreceptor function
    • Christie, J. M.; Swartz, T. E.; Bogomolni, R. A.; Briggs, W. R. Phototropin LOV domains exhibit distinct roles in regulating photoreceptor function. Plant J. 2002, 32, 205-219.
    • (2002) Plant J. , vol.32 , pp. 205-219
    • Christie, J.M.1    Swartz, T.E.2    Bogomolni, R.A.3    Briggs, W.R.4
  • 55
    • 0037435618 scopus 로고    scopus 로고
    • The LOV Domain Family: Photoresponsive Signaling Modules Coupled to Diverse Output Domains
    • Crosson, S.; Rajagopal, S.; Moffat, K. The LOV Domain Family: Photoresponsive Signaling Modules Coupled to Diverse Output Domains. Biochemistry 2003, 42, 2-10.
    • (2003) Biochemistry , vol.42 , pp. 2-10
    • Crosson, S.1    Rajagopal, S.2    Moffat, K.3
  • 56
    • 0031880316 scopus 로고    scopus 로고
    • Roles in dimerization and blue light photoresponse of the PAS and LOV domains of Neurospora crassa white collar proteins
    • Ballario, P.; Talora, C.; Galli, D.; Linden, H.; Macino G. Roles in dimerization and blue light photoresponse of the PAS and LOV domains of Neurospora crassa white collar proteins. Mol. Microbiol. 1998, 29, 719-729.
    • (1998) Mol. Microbiol. , vol.29 , pp. 719-729
    • Ballario, P.1    Talora, C.2    Galli, D.3    Linden, H.4    Macino, G.5
  • 57
    • 0036224807 scopus 로고    scopus 로고
    • First evidence for phototropin-related blue-light receptors in prokaryotes
    • Losi, A.; Polverini, E.; Quest, B.; Gartner, W. First evidence for phototropin-related blue-light receptors in prokaryotes. Biophys. J. 2002, 82, 2627-2634.
    • (2002) Biophys. J. , vol.82 , pp. 2627-2634
    • Losi, A.1    Polverini, E.2    Quest, B.3    Gartner, W.4
  • 58
    • 2342652526 scopus 로고    scopus 로고
    • P Ab initio Quantum Chemical Investigation of the First Steps of the Photocycle of Phototropin: A Model Study
    • Neiss, C. a. S., P Ab initio Quantum Chemical Investigation of the First Steps of the Photocycle of Phototropin: A Model Study. Photochem. Photobiol. 2003, 77, 101-109.
    • (2003) Photochem. Photobiol. , vol.77 , pp. 101-109
    • Neiss, C.A.S.1
  • 61
    • 0037031561 scopus 로고    scopus 로고
    • AppA is a blue light photoreceptor that antirepresses photosynthesis gene expression in Rhodobacter sphaeroides
    • Masuda, S.; Bauer, C. E. AppA is a blue light photoreceptor that antirepresses photosynthesis gene expression in Rhodobacter sphaeroides. Cell 2002, 110, 613-623.
    • (2002) Cell , vol.110 , pp. 613-623
    • Masuda, S.1    Bauer, C.E.2
  • 62
    • 0036371637 scopus 로고    scopus 로고
    • A single flavoprotein, AppA, integrates both redox and light signals in Rhodobacter sphaeroides
    • Braatsch, S.; Gomelsky, M.; Kuphal, S.; Klug, G. A single flavoprotein, AppA, integrates both redox and light signals in Rhodobacter sphaeroides. Mol. Microbiol. 2002, 45, 827-836.
    • (2002) Mol. Microbiol. , vol.45 , pp. 827-836
    • Braatsch, S.1    Gomelsky, M.2    Kuphal, S.3    Klug, G.4
  • 63
    • 0141844456 scopus 로고    scopus 로고
    • Initial Characterization of the Primary Photochemistry of AppA, a Blue-light-using Flavin Adenine Dinucleotide-domain Containing Transcriptional Antirepressor Protein from Rhodobacter sphaeroides: A Key Role for Reversible Intramolecular Proton Transfer from the Flavin Adenine Dinucleotide Chromophore to a Conserved Tyrosine?
    • Laan, W.; van der Horst, M. A.; van Stokkum, I. H.; Hellingwerf, K. J. Initial Characterization of the Primary Photochemistry of AppA, a Blue-light-using Flavin Adenine Dinucleotide-domain Containing Transcriptional Antirepressor Protein from Rhodobacter sphaeroides: A Key Role for Reversible Intramolecular Proton Transfer from the Flavin Adenine Dinucleotide Chromophore to a Conserved Tyrosine? Photochem. Photobiol.2003, 78, 290-297.
    • (2003) Photochem. Photobiol. , vol.78 , pp. 290-297
    • Laan, W.1    Van Der Horst, M.A.2    Van Stokkum, I.H.3    Hellingwerf, K.J.4
  • 64
    • 0034047356 scopus 로고    scopus 로고
    • The M intermediate of Pharaonis phoborhodopsin is photoactive
    • Balashov, S. P.; Sumi, M.; Kamo, N. The M intermediate of Pharaonis phoborhodopsin is photoactive. Biophys. J. 2000, 78, 3150-3159.
    • (2000) Biophys. J. , vol.78 , pp. 3150-3159
    • Balashov, S.P.1    Sumi, M.2    Kamo, N.3
  • 65
    • 0027462930 scopus 로고
    • A Light-Dependent Branching-Reaction in the Photocycle of the Yellow Protein from Ectothiorhodospira-Halophila
    • Miller, A.; Leigeber, H.; Hoff, W. D.; Hellingwerf, K. J. A Light-Dependent Branching-Reaction in the Photocycle of the Yellow Protein from Ectothiorhodospira-Halophila. Biochim. Biophys. Acta 1993, 1141, 190-196.
    • (1993) Biochim. Biophys. Acta , vol.1141 , pp. 190-196
    • Miller, A.1    Leigeber, H.2    Hoff, W.D.3    Hellingwerf, K.J.4
  • 66
    • 0031772265 scopus 로고    scopus 로고
    • The phenolic recognition profiles of the Agrobacterium tumefaciens VirA protein are broadened by a high level of the sugar binding protein ChvE
    • Peng, W. T.; Lee, Y. W.; Nester, E. W. The phenolic recognition profiles of the Agrobacterium tumefaciens VirA protein are broadened by a high level of the sugar binding protein ChvE. J. Bacteriol. 1998, 180, 5632-5638.
    • (1998) J. Bacteriol. , vol.180 , pp. 5632-5638
    • Peng, W.T.1    Lee, Y.W.2    Nester, E.W.3
  • 68
    • 0035923399 scopus 로고    scopus 로고
    • A molecular movie at 1.8 A resolution displays the photocycle of photoactive yellow protein, a eubacterial blue-light receptor, from nanoseconds to seconds
    • Ren, Z.; Perman, B.; Srajer, V.; Teng, T. Y.; Pradervand, C.; Bourgeois, D.; Schotte, F.; Ursby, T.; Kort, R.; Wulff, M.; Moffat, K. A molecular movie at 1.8 A resolution displays the photocycle of photoactive yellow protein, a eubacterial blue-light receptor, from nanoseconds to seconds. Biochemistry 2001, 40, 13788-13801.
    • (2001) Biochemistry , vol.40 , pp. 13788-13801
    • Ren, Z.1    Perman, B.2    Srajer, V.3    Teng, T.Y.4    Pradervand, C.5    Bourgeois, D.6    Schotte, F.7    Ursby, T.8    Kort, R.9    Wulff, M.10    Moffat, K.11


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.