메뉴 건너뛰기




Volumn 91, Issue 5, 2006, Pages 1811-1822

Chromophore structure in the photocycle of the cyanobacterial phytochrome Cph1

Author keywords

[No Author keywords available]

Indexed keywords

HYDROGEN; PHYTOCHROME;

EID: 33748450550     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.084335     Document Type: Article
Times cited : (51)

References (53)
  • 1
    • 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
  • 2
    • 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
  • 3
    • 4344699140 scopus 로고    scopus 로고
    • Evolution of cyanobacterial and plant phytochromes
    • Lamparter, T. 2004. Evolution of cyanobacterial and plant phytochromes. FEBS Lett. 573:1-5.
    • (2004) FEBS Lett. , vol.573 , pp. 1-5
    • Lamparter, T.1
  • 4
    • 0000663949 scopus 로고
    • Detection, assay and preliminary purification of the pigment controlling photoresponsive developments 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 developments of plants. Proc. Natl. Acad. Sci. USA. 45:1703-1708.
    • (1959) Proc. Natl. Acad. Sci. USA , vol.45 , pp. 1703-1708
    • Butler, W.L.1    Norris, K.H.2    Siegelman, H.W.3    Hendricks, S.B.4
  • 5
    • 0013250040 scopus 로고
    • Photochemistry of 124 kilodalton Avena phytochrome under constant illumination in vitro
    • Kelly, J. M., and J. C. Lagarias. 1985. Photochemistry of 124 kilodalton Avena phytochrome under constant illumination in vitro. Biochemistry. 24:6003-6010.
    • (1985) Biochemistry , vol.24 , pp. 6003-6010
    • Kelly, J.M.1    Lagarias, J.C.2
  • 6
    • 84989743888 scopus 로고
    • Comparative photochemical analysis of highly purified 124 kilodalton oat and rye phytochromes in vitro
    • Lagarias, J. C., J. M. Kelly, K. L. Cyr, and W. O. Smith Jr. 1987. Comparative photochemical analysis of highly purified 124 kilodalton oat and rye phytochromes in vitro. Photochem. Photobiol. 46:5-13.
    • (1987) Photochem. Photobiol. , vol.46 , pp. 5-13
    • Lagarias, J.C.1    Kelly, J.M.2    Cyr, K.L.3    Smith Jr., W.O.4
  • 8
    • 0036154249 scopus 로고    scopus 로고
    • Ultrafast dynamics of phytochrome from the cyanobacterium synechocystis, reconstituted with phycocyanobilin and phycoerythrobilin
    • Heyne, K., J. Herbst, D. Stehlik, B. Esteban, T. Lamparter, J. Hughes, and R. Diller. 2002. Ultrafast dynamics of phytochrome from the cyanobacterium synechocystis, reconstituted with phycocyanobilin and phycoerythrobilin. Biophys. J. 82:1004-1016.
    • (2002) Biophys. J. , vol.82 , pp. 1004-1016
    • Heyne, K.1    Herbst, J.2    Stehlik, D.3    Esteban, B.4    Lamparter, T.5    Hughes, J.6    Diller, R.7
  • 9
    • 3242747592 scopus 로고    scopus 로고
    • Photoactive yellow protein, bacteriophytochrome, and sensory rhodopsin in purple phototrophic bacteria
    • Kyndt, J. A., T. E. Meyer, and M. A. Cusanovich. 2004. Photoactive yellow protein, bacteriophytochrome, and sensory rhodopsin in purple phototrophic bacteria. Photochem. Photobiol. Sci. 3:519-530.
    • (2004) Photochem. Photobiol. Sci. , vol.3 , pp. 519-530
    • Kyndt, J.A.1    Meyer, T.E.2    Cusanovich, M.A.3
  • 10
    • 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
  • 11
    • 0026649545 scopus 로고
    • Phytochrome assembly. Defining chromophore structural requirements for covalent attachment and photoreversibility
    • Li, L., and 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
  • 12
    • 0014301122 scopus 로고
    • Phycocyanobilin. Structure and exchange studies by nuclear magnetic resonance and its mode of attachment in phycocyanin. A model for phytochrome
    • Crespi, H. L., U. Smith, and J. J. Katz. 1968. Phycocyanobilin. Structure and exchange studies by nuclear magnetic resonance and its mode of attachment in phycocyanin. A model for phytochrome. Biochemistry. 7:2232-2242.
    • (1968) Biochemistry , vol.7 , pp. 2232-2242
    • Crespi, H.L.1    Smith, U.2    Katz, J.J.3
  • 13
    • 0002644398 scopus 로고
    • Diastereoselective synthesis of phycocyanobilin-cysteine adducts
    • Bishop, J. E., J. O. Nagy, J. F. O'Connell, and H. Rapoport. 1991. Diastereoselective synthesis of phycocyanobilin-cysteine adducts. J. Am. Chem. Soc. 118:8024-8035.
    • (1991) J. Am. Chem. Soc. , vol.118 , pp. 8024-8035
    • Bishop, J.E.1    Nagy, J.O.2    O'Connell, J.F.3    Rapoport, H.4
  • 14
    • 0031694127 scopus 로고    scopus 로고
    • Protonated 2,3-dihydrobilindiones - Models for the chromophores of phycocyanin and the red-absorbing form of phytochrome
    • Stanek, M., and K. Grubmayr. 1998. Protonated 2,3-dihydrobilindiones - Models for the chromophores of phycocyanin and the red-absorbing form of phytochrome. Chem. Eur. J. 4:1653-1659.
    • (1998) Chem. Eur. J. , vol.4 , pp. 1653-1659
    • Stanek, M.1    Grubmayr, K.2
  • 15
    • 0003318951 scopus 로고
    • Geometry versus basicity of bilatrienes: Stretched and helical protonated biliverdins
    • Krois, D. 1991. Geometry versus basicity of bilatrienes: stretched and helical protonated biliverdins. Monatsh. Chem. 122:495-506.
    • (1991) Monatsh. Chem. , vol.122 , pp. 495-506
    • Krois, D.1
  • 17
    • 0037418282 scopus 로고    scopus 로고
    • The pair of bacteriophytochromes from Agrobacterium tumefaciens are histidine kinases with opposing photobiological properties
    • Karniol, B., and R. D. Vierstra. 2003. The pair of bacteriophytochromes from Agrobacterium tumefaciens are histidine kinases with opposing photobiological properties. Proc. Natl. Acad. Sci. USA. 100:2807-2812.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 2807-2812
    • Karniol, B.1    Vierstra, R.D.2
  • 18
    • 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
  • 20
    • 0039090711 scopus 로고
    • Chromophore structure of the physiologically active form Pfr. of phytochrome
    • Rudiger, W. T., F. Tummler, E. Cmiel, and S. Schneider. 1983. Chromophore structure of the physiologically active form Pfr. of phytochrome. Proc. Natl. Acad. Sci. USA. 80:6244-6248.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 6244-6248
    • Rudiger, W.T.1    Tummler, F.2    Cmiel, E.3    Schneider, S.4
  • 21
    • 0034646178 scopus 로고    scopus 로고
    • Probing the photoreaction mechanism of phytochrome through analysis of resonance Raman vibrational spectra of recombinant analogues
    • Andel 3rd, F., 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
  • 23
    • 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. Gartner, and 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    Gartner, W.4    Siebert, F.5
  • 24
    • 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, and 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
  • 25
    • 11244336639 scopus 로고    scopus 로고
    • Determination of the chromophore structures in the photoinduced reaction cycle of phytochrome
    • Mroginski, M. A., D. H. Murgida, D. von Stetten, C. Kneip, F. Mark, and P. Hildebrandt. 2004. Determination of the chromophore structures in the photoinduced reaction cycle of phytochrome. J. Am. Chem. Soc. 126:16734-16735.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 16734-16735
    • Mroginski, M.A.1    Murgida, D.H.2    Von Stetten, D.3    Kneip, C.4    Mark, F.5    Hildebrandt, P.6
  • 27
    • 10644265997 scopus 로고    scopus 로고
    • Harnessing phytochrome's glowing potential
    • Fischer, A. J., and J. C. Lagarias. 2004. Harnessing phytochrome's glowing potential. Proc. Natl. Acad. Sci. USA. 101:17334-17339.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 17334-17339
    • Fischer, A.J.1    Lagarias, J.C.2
  • 29
    • 0035845489 scopus 로고    scopus 로고
    • Genetic engineering of phytochrome biosynthesis in bacteria
    • Gambetta, G. A., and J. C. Lagarias. 2001. Genetic engineering of phytochrome biosynthesis in bacteria. Proc. Natl. Acad. Sci. USA. 98:10566-10571.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10566-10571
    • Gambetta, G.A.1    Lagarias, J.C.2
  • 30
    • 0028789214 scopus 로고
    • Partial inhibition of protein synthesis accelerates the synthesis of porphyrin in heme-deficient mutants of Escherichia coli
    • Nakayashiki, T., K. Nishimura, R. Tanaka, and H. Inokuchi. 1995. Partial inhibition of protein synthesis accelerates the synthesis of porphyrin in heme-deficient mutants of Escherichia coli. Mol. Gen. Genet. 249:139-146.
    • (1995) Mol. Gen. Genet. , vol.249 , pp. 139-146
    • Nakayashiki, T.1    Nishimura, K.2    Tanaka, R.3    Inokuchi, H.4
  • 31
    • 0036667415 scopus 로고    scopus 로고
    • A whole genome view of prokaryotic haem biosynthesis
    • Panek, H., and M. R. O'Brian. 2002. A whole genome view of prokaryotic haem biosynthesis. Microbiology. 148:2273-2282.
    • (2002) Microbiology , vol.148 , pp. 2273-2282
    • Panek, H.1    O'Brian, M.R.2
  • 32
    • 0032913203 scopus 로고    scopus 로고
    • 13C NMR assignments of the heme resonances of rat liver outer mitochondrial membrane cytochrome b5
    • 13C NMR assignments of the heme resonances of rat liver outer mitochondrial membrane cytochrome b5. J. Biol. Inorg. Chem. 4:87-98.
    • (1999) J. Biol. Inorg. Chem. , vol.4 , pp. 87-98
    • Rivera, M.1    Qiu, F.2    Bunce, R.A.3    Stark, R.E.4
  • 33
    • 0031612759 scopus 로고    scopus 로고
    • 13C-edited 1H NMR experiment for making resonance assignments in the active site of heme proteins
    • 13C-edited 1H NMR experiment for making resonance assignments in the active site of heme proteins. J. Magn. Reson. 130:76-81.
    • (1998) J. Magn. Reson. , vol.130 , pp. 76-81
    • Qiu, F.1    Rivera, M.2    Stark, R.E.3
  • 34
    • 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
  • 35
    • 0037291310 scopus 로고    scopus 로고
    • The 1.45 Å three-dimensional structure of C-phycocyanin from the thermophilic cyanobacterium Synechococcus elongatus
    • Nield, J., P. J. Rizkallah, J. Barber, and N. E. Chayen. 2003. The 1.45 Å three-dimensional structure of C-phycocyanin from the thermophilic cyanobacterium Synechococcus elongatus. J. Struct. Biol. 141:149-155.
    • (2003) J. Struct. Biol. , vol.141 , pp. 149-155
    • Nield, J.1    Rizkallah, P.J.2    Barber, J.3    Chayen, N.E.4
  • 38
    • 10644250257 scopus 로고
    • Inhomogeneous electron gas
    • Hohenberg, P., and W. Khon. 1964. Inhomogeneous electron gas. Phys. Rev. 136:B864-B871.
    • (1964) Phys. Rev. , vol.136
    • Hohenberg, P.1    Khon, W.2
  • 39
    • 0042113153 scopus 로고
    • Self-consistent equations including exchange and correlation effects
    • Khon, W., and L. J. Sham. 1965. Self-consistent equations including exchange and correlation effects. Phys. Rev. 140:A1133-A1138.
    • (1965) Phys. Rev. , vol.140
    • Khon, W.1    Sham, L.J.2
  • 40
    • 0000719180 scopus 로고
    • Quantum theory of interatomic currents in aromatic compounds
    • London, F. 1937. Quantum theory of interatomic currents in aromatic compounds. J. Phys. Radium. 8:397-409.
    • (1937) J. Phys. Radium. , vol.8 , pp. 397-409
    • London, F.1
  • 41
    • 40749094858 scopus 로고
    • Self-consistent perturbation theory of diamagnetism. I. A gauge-invariant lcao linear combination of atomic orbitals. Method for NMR chemical shifts
    • Ditchfield, R. 1974. Self-consistent perturbation theory of diamagnetism. I. A gauge-invariant lcao linear combination of atomic orbitals. Method for NMR chemical shifts. Mol. Phys. 27:789-807.
    • (1974) Mol. Phys. , vol.27 , pp. 789-807
    • Ditchfield, R.1
  • 42
    • 11744305193 scopus 로고
    • Efficient implementation of the gauge-independent atomic orbital method for NMR chemical shift calculations
    • Wolinski, K., J. F. Hinton, and P. Pulay. 1990. Efficient implementation of the gauge-independent atomic orbital method for NMR chemical shift calculations. J. Am. Chem. Soc. 112:8251-8260.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 8251-8260
    • Wolinski, K.1    Hinton, J.F.2    Pulay, P.3
  • 43
    • 9644286821 scopus 로고    scopus 로고
    • Comparison of different theory models and basis sets in the calculation of 13C NMR chemical shifts of natural products. Magnetic resonance in chemistry
    • Cimino, P., L. Gomez-Paloma, D. Duca, R. Riccio, and G. Bifulco. 2004. Comparison of different theory models and basis sets in the calculation of 13C NMR chemical shifts of natural products. Magnetic resonance in chemistry. Magn. Reson. Chem. 42:S26-S33.
    • (2004) Magn. Reson. Chem. , vol.42
    • Cimino, P.1    Gomez-Paloma, L.2    Duca, D.3    Riccio, R.4    Bifulco, G.5
  • 44
    • 0030570285 scopus 로고    scopus 로고
    • Treatment of electronic excitations within the adiabatic approximation of time-dependent density functional theory
    • Bauernschmitt, R., and R. Ahlrichs. 1996. Treatment of electronic excitations within the adiabatic approximation of time-dependent density functional theory. Chem. Phys. Lett. 256:454-464.
    • (1996) Chem. Phys. Lett. , vol.256 , pp. 454-464
    • Bauernschmitt, R.1    Ahlrichs, R.2
  • 45
    • 0000287603 scopus 로고    scopus 로고
    • Molecular excitation energies to high-lying bound states from timedependent density-functional response theory: Characterization and correction of the time-dependent local density approximation ionization threshold
    • Casida, M. E., C. Jamorski, K. C. Casida, and D. R. Salahub. 1998. Molecular excitation energies to high-lying bound states from timedependent density-functional response theory: characterization and correction of the time-dependent local density approximation ionization threshold. J. Chem. Phys. 108:4439-4449.
    • (1998) J. Chem. Phys. , vol.108 , pp. 4439-4449
    • Casida, M.E.1    Jamorski, C.2    Casida, K.C.3    Salahub, D.R.4
  • 46
    • 11244326290 scopus 로고    scopus 로고
    • Exchange functionals with improved long-range behavior and adiabatic connection methods without adjustable parameters: The mPW and mPW1PW models
    • Adamo, C., and V. Barone. 1998. Exchange functionals with improved long-range behavior and adiabatic connection methods without adjustable parameters: the mPW and mPW1PW models. J. Chem. Phys. 108:664-675.
    • (1998) J. Chem. Phys. , vol.108 , pp. 664-675
    • Adamo, C.1    Barone, V.2
  • 47
    • 0031595590 scopus 로고    scopus 로고
    • The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of proteins
    • Gardner, K. H., and L. E. Kay. 1998. The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of proteins. Annu. Rev. Biophys. Biomol. Struct. 27:357-406.
    • (1998) Annu. Rev. Biophys. Biomol. Struct. , vol.27 , pp. 357-406
    • Gardner, K.H.1    Kay, L.E.2
  • 48
    • 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
  • 49
    • 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
  • 50
    • 19544383257 scopus 로고    scopus 로고
    • Elemental analysis of proteins by microPIXE
    • Garman, E. F., and G. W. Grime. 2005. Elemental analysis of proteins by microPIXE. Prog. Biophys. Mol. Biol. 89:173-205.
    • (2005) Prog. Biophys. Mol. Biol. , vol.89 , pp. 173-205
    • Garman, E.F.1    Grime, G.W.2
  • 51
    • 0036110408 scopus 로고    scopus 로고
    • Fluorescence investigation of the recombinant cyanobacterial phytochrome (Cph1) and its C-terminally truncated monomeric species (Cph1Delta2): 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 (Cph1Delta2): 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
  • 53
    • 21644470824 scopus 로고    scopus 로고
    • Sterically locked synthetic bilin derivatives and phytochrome Agp1 from Agrobacterium tumefaciens form photoinsensitive Pr- and Pfr-like adducts
    • Inomata, K., M. A. Hammam, H. Kinoshita, Y. Murata, H. Khawn, S. Noack, N. Michael, and T. Lamparter. 2005. Sterically locked synthetic bilin derivatives and phytochrome Agp1 from Agrobacterium tumefaciens form photoinsensitive Pr- and Pfr-like adducts. J. Biol. Chem. 280:24491-24497.
    • (2005) J. Biol. Chem. , vol.280 , pp. 24491-24497
    • Inomata, K.1    Hammam, M.A.2    Kinoshita, H.3    Murata, Y.4    Khawn, H.5    Noack, S.6    Michael, N.7    Lamparter, T.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.