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Volumn 78, Issue 2, 2003, Pages 205-212

Fluorescence Lifetimes of Protochlorophyllide in Plants with Different Proportions of Short-wavelength and Long-wavelength Protochlorophyllide Spectral Forms

Author keywords

[No Author keywords available]

Indexed keywords

PROTOCHLOROPHYLLIDE;

EID: 10744231144     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1562/0031-8655(2003)078<0205:FLOPIP>2.0.CO;2     Document Type: Article
Times cited : (33)

References (33)
  • 1
    • 0033231384 scopus 로고    scopus 로고
    • Pigment-free NADPH:Protochlorophyllide oxidoreductase from Avena sativa L purification and substrate specificity
    • Klement, H., M. Helfrich, U. Oster, S. Schoch and W. Rüdiger (1999) Pigment-free NADPH:protochlorophyllide oxidoreductase from Avena sativa L purification and substrate specificity. Eur. J. Biochem. 265, 862-874.
    • (1999) Eur. J. Biochem. , vol.265 , pp. 862-874
    • Klement, H.1    Helfrich, M.2    Oster, U.3    Schoch, S.4    Rüdiger, W.5
  • 2
    • 0028895568 scopus 로고
    • A light-dependent complementation system for analysis of NADPH:protochlorophyllide oxidoreductase: Identification and mutagenesis of two conserved residues that are essential for activity
    • Wilks, H. M. and M. P. Timko (1995) A light-dependent complementation system for analysis of NADPH:protochlorophyllide oxidoreductase: identification and mutagenesis of two conserved residues that are essential for activity. Proc. Natl. Acad. Sci USA 92, 724-728.
    • (1995) Proc. Natl. Acad. Sci USA , vol.92 , pp. 724-728
    • Wilks, H.M.1    Timko, M.P.2
  • 3
    • 0026522499 scopus 로고
    • Identification of four universal protochlorophyllide forms in dark-grown leaves by analyses of the 77 K fluorescence emission spectra
    • Böddi, B., M. Ryberg and C. Sundqvist (1992) Identification of four universal protochlorophyllide forms in dark-grown leaves by analyses of the 77 K fluorescence emission spectra. J. Photochem. Photobiol. B: Biol. 12, 389-401.
    • (1992) J. Photochem. Photobiol. B: Biol. , vol.12 , pp. 389-401
    • Böddi, B.1    Ryberg, M.2    Sundqvist, C.3
  • 4
    • 0036443448 scopus 로고    scopus 로고
    • POR structural domains important for the enzyme activity in R. capsulatus complementation system
    • Lebedev, N. and M. P. Timko (2002) POR structural domains important for the enzyme activity in R. capsulatus complementation system. Photosynth. Res. 74, 153-163.
    • (2002) Photosynth. Res. , vol.74 , pp. 153-163
    • Lebedev, N.1    Timko, M.P.2
  • 5
    • 0000630429 scopus 로고
    • On the aggregational states of protochlorophyllide and its protein complexes in wheat etioplasts
    • Böddi, B., A. Lindsten, M. Ryberg and C. Sundqvist (1989) On the aggregational states of protochlorophyllide and its protein complexes in wheat etioplasts. Physiol. Plant. 76, 135-143.
    • (1989) Physiol. Plant. , vol.76 , pp. 135-143
    • Böddi, B.1    Lindsten, A.2    Ryberg, M.3    Sundqvist, C.4
  • 6
    • 0001402677 scopus 로고
    • The effect of cross-linking of the subunits of NADPH-protochlorophyllide oxidoreductase on the aggregation state of protochlorophyllide
    • Wiktorsson, B., S. Engdahl, L. B. Zhong, B. Böddi, M. Ryberg and C. Sundqvist (1993) The effect of cross-linking of the subunits of NADPH-protochlorophyllide oxidoreductase on the aggregation state of protochlorophyllide. Photosynthetica 29, 205-218.
    • (1993) Photosynthetica , vol.29 , pp. 205-218
    • Wiktorsson, B.1    Engdahl, S.2    Zhong, L.B.3    Böddi, B.4    Ryberg, M.5    Sundqvist, C.6
  • 7
    • 0001084795 scopus 로고
    • Localisation of NADPH-protochlorophyllide oxidoreductase in dark-grown wheat (Triticum aestivum) by immuno-electron microscopy before and after tranformation of the prolamellar bodies
    • Ryberg, M. and K. Dehesh (1986) Localisation of NADPH-protochlorophyllide oxidoreductase in dark-grown wheat (Triticum aestivum) by immuno-electron microscopy before and after tranformation of the prolamellar bodies. Physiol. Plant. 66, 616-624.
    • (1986) Physiol. Plant. , vol.66 , pp. 616-624
    • Ryberg, M.1    Dehesh, K.2
  • 8
    • 0000628277 scopus 로고
    • Chlorophyll formation in the YG-6 mutant of Chlorella vulgaris: Spectral characterization of protochlorophyllide phototransformation
    • Shioi, Y. and T. Sasa (1984) Chlorophyll formation in the YG-6 mutant of Chlorella vulgaris: spectral characterization of protochlorophyllide phototransformation. Plant Cell Physiol. 25, 139-149.
    • (1984) Plant Cell Physiol. , vol.25 , pp. 139-149
    • Shioi, Y.1    Sasa, T.2
  • 9
    • 0027142656 scopus 로고
    • Effectiveness of light of different wavelengths to induce chlorophyll biosynthesis in rapidly and slowly greening tissues
    • Virgin, H. I. (1993) Effectiveness of light of different wavelengths to induce chlorophyll biosynthesis in rapidly and slowly greening tissues. Physiol. Plant. 89, 761-766.
    • (1993) Physiol. Plant. , vol.89 , pp. 761-766
    • Virgin, H.I.1
  • 10
    • 85011847403 scopus 로고
    • The polypeptide composition of highly purified prolamellar bodies and prothylakoids from wheat (Trificum aestivum) as revealed by silver staining
    • Lindsten, A., M. Ryberg and C. Sundqvist (1988) The polypeptide composition of highly purified prolamellar bodies and prothylakoids from wheat (Trificum aestivum) as revealed by silver staining. Physiol. Plant. 72, 167-176.
    • (1988) Physiol. Plant. , vol.72 , pp. 167-176
    • Lindsten, A.1    Ryberg, M.2    Sundqvist, C.3
  • 11
    • 0034520142 scopus 로고    scopus 로고
    • Regulation of etioplast pigment-protein complexes, inner membrane architecture, and protochlorophyllide a chemical heterogenity by light-dependent NADPH:protochlorophyllide oxidoreductase A and B
    • Franck, F., U. Sperling, G. Frick, B. Pochert, B. van Cleve, K. Apel and G. A. Armstrong (2000) Regulation of etioplast pigment-protein complexes, inner membrane architecture, and protochlorophyllide a chemical heterogenity by light-dependent NADPH:protochlorophyllide oxidoreductase A and B. Plant Physiol. 124, 1678-1696.
    • (2000) Plant Physiol. , vol.124 , pp. 1678-1696
    • Franck, F.1    Sperling, U.2    Frick, G.3    Pochert, B.4    Van Cleve, B.5    Apel, K.6    Armstrong, G.A.7
  • 12
    • 0032004065 scopus 로고    scopus 로고
    • Etioplast differentiation in Arabidopsis: Both PORA and PORB restore the prolamellar body membrane and photoactive protochlorophyllide-F 655 to the Cop1 photomorphogenic mutant
    • Sperling, V., F. Frank, B. van Cleve, G. Frick, K. Apel and G. A. Armstrong (1998) Etioplast differentiation in Arabidopsis: both PORA and PORB restore the prolamellar body membrane and photoactive protochlorophyllide-F 655 to the Cop1 photomorphogenic mutant. Plant Cell 10, 283-296.
    • (1998) Plant Cell , vol.10 , pp. 283-296
    • Sperling, V.1    Frank, F.2    Van Cleve, B.3    Frick, G.4    Apel, K.5    Armstrong, G.A.6
  • 13
    • 85012866668 scopus 로고
    • The regular ultrastructure of isolated prolamellar bodies depends on the presence of membrane-bound NADPH-protochlorophyllide oxidoteductase
    • Ryberg, M. and C. Sundqvist (1988) The regular ultrastructure of isolated prolamellar bodies depends on the presence of membrane-bound NADPH-protochlorophyllide oxidoteductase. Physiol. Plant. 73, 218-226.
    • (1988) Physiol. Plant. , vol.73 , pp. 218-226
    • Ryberg, M.1    Sundqvist, C.2
  • 14
    • 84989754340 scopus 로고
    • Phototransformation of aggregated forms of protochlorophyllide in isolated etioplast inner membranes
    • Böddi, B., A. Lindsten, M. Ryberg and C. Sundqvist (1990) Phototransformation of aggregated forms of protochlorophyllide in isolated etioplast inner membranes. Photochem. Photobiol. 52, 83-87.
    • (1990) Photochem. Photobiol. , vol.52 , pp. 83-87
    • Böddi, B.1    Lindsten, A.2    Ryberg, M.3    Sundqvist, C.4
  • 15
    • 0015520745 scopus 로고
    • Circular dichroism studies on the structure and the photochemistry of protochlorophyllide and chlorophyllide holochrome
    • Mathis, P. and K. Sauer (1972) Circular dichroism studies on the structure and the photochemistry of protochlorophyllide and chlorophyllide holochrome. Biochim. Biophys. Acta 267, 498-511.
    • (1972) Biochim. Biophys. Acta , vol.267 , pp. 498-511
    • Mathis, P.1    Sauer, K.2
  • 16
    • 0002119280 scopus 로고
    • Structural and functional significance of pigment-protein complexes of chlorophyll precursors
    • (Edited by H. Scheer). CRC Press, Boca Raton
    • Ryberg, M. and C. Sundqvist (1991) Structural and functional significance of pigment-protein complexes of chlorophyll precursors. In Chlorophylls (Edited by H. Scheer), pp. 587-612. CRC Press, Boca Raton.
    • (1991) Chlorophylls , pp. 587-612
    • Ryberg, M.1    Sundqvist, C.2
  • 17
    • 0002195611 scopus 로고
    • Chloroplast lipids and the assembly of membranes
    • (Edited by C. Sundqvist and M. Ryberg). Academic Press, San Diego
    • Selstam, E. and A. Widell-Wigge (1993) Chloroplast lipids and the assembly of membranes. In Pigment-Protein Complexes in Plastids: Synthesis and Assembly (Edited by C. Sundqvist and M. Ryberg), pp. 241-277. Academic Press, San Diego.
    • (1993) Pigment-Protein Complexes in Plastids: Synthesis and Assembly , pp. 241-277
    • Selstam, E.1    Widell-Wigge, A.2
  • 18
    • 0034284724 scopus 로고    scopus 로고
    • The influence of glycerol and chloroplast lipids on the spectral shifts of pigments associated with NADPH:Protochlorophyllide oxidoreductase from Avena sativa L
    • Klement, H., U. Oster and W. Rüdiger (2000) The influence of glycerol and chloroplast lipids on the spectral shifts of pigments associated with NADPH:protochlorophyllide oxidoreductase from Avena sativa L. FEBS Lett. 480, 1-5.
    • (2000) FEBS Lett. , vol.480 , pp. 1-5
    • Klement, H.1    Oster, U.2    Rüdiger, W.3
  • 19
    • 0042049202 scopus 로고
    • Fluorescence lifetime spectra measured after illumination of etiolated been leaves at low temperature
    • Van der Cammen, J. C. M. and J. C. Goedheer (1982) Fluorescence lifetime spectra measured after illumination of etiolated been leaves at low temperature. Photobiochem. Photobiophys. 4, 145-152.
    • (1982) Photobiochem. Photobiophys. , vol.4 , pp. 145-152
    • Van der Cammen, J.C.M.1    Goedheer, J.C.2
  • 20
    • 84989751889 scopus 로고
    • The primary reaction in photoreduction of protochlorophyllide monitored by nanosecond fluorescence measurements
    • Van Bochove, A. C., W. T. Griffiths and R. van Grondelle (1984) The primary reaction in photoreduction of protochlorophyllide monitored by nanosecond fluorescence measurements. Photochem. Photobiol. 39, 101-196.
    • (1984) Photochem. Photobiol. , vol.39 , pp. 101-196
    • Van Bochove, A.C.1    Griffiths, W.T.2    Van Grondelle, R.3
  • 21
    • 0012952497 scopus 로고    scopus 로고
    • Analysis of fluooscence lifetime of protochlorophyllide and chlorophyllide in isolated etioplast membranes measured from multifrequency cross-correlation phase fluorometry
    • Myśliwa-Kurdziel, B., F. Franck and K. Strzatka (1999) Analysis of fluooscence lifetime of protochlorophyllide and chlorophyllide in isolated etioplast membranes measured from multifrequency cross-correlation phase fluorometry. Photochem. Photobiol. 70, 616-623.
    • (1999) Photochem. Photobiol. , vol.70 , pp. 616-623
    • Myśliwa-Kurdziel, B.1    Franck, F.2    Strzatka, K.3
  • 22
    • 0033759099 scopus 로고    scopus 로고
    • The pea light-independent photomorphogenesis I mutant results from partial duplication of COP1 generating an internal promoter and producing two distinct transcripts
    • Sullivan, J. A. and J. C. Gray (2000) The pea light-independent photomorphogenesis I mutant results from partial duplication of COP1 generating an internal promoter and producing two distinct transcripts. Plant Cell 12, 1927-1938.
    • (2000) Plant Cell , vol.12 , pp. 1927-1938
    • Sullivan, J.A.1    Gray, J.C.2
  • 23
    • 0027031107 scopus 로고
    • Initial characterization of a pea mutant with light-independent photomorphogenesis
    • Frances, S., M. J. White, M. D. Edgerton, A. M. Jones, R. C. Elliot and W. F, Thompson (1992) Initial characterization of a pea mutant with light-independent photomorphogenesis. Plant Cell 4, 1519-1530.
    • (1992) Plant Cell , vol.4 , pp. 1519-1530
    • Frances, S.1    White, M.J.2    Edgerton, M.D.3    Jones, A.M.4    Elliot, R.C.5    Thompson, W.F.6
  • 24
    • 0032879989 scopus 로고    scopus 로고
    • Protochlorophyllide, NADPH-protochlorophyllide oxidoreductase, and chlorophyll formation in the lipl mutant of pea
    • Seyyedi, M., M. P. Timko and C. Sundqvist (1999) Protochlorophyllide, NADPH-protochlorophyllide oxidoreductase, and chlorophyll formation in the lipl mutant of pea. Physiol. Plant. 106, 344-354.
    • (1999) Physiol. Plant. , vol.106 , pp. 344-354
    • Seyyedi, M.1    Timko, M.P.2    Sundqvist, C.3
  • 25
    • 84989696263 scopus 로고
    • Chlorophyll synthethase is latent in well preserved prolamellar bodies of etiolated wheat
    • Lindsten, A., C. J. Welch, S. Schoch, M. Ryberg, W. Rüdiger and C. Sundqvist (1990) Chlorophyll synthethase is latent in well preserved prolamellar bodies of etiolated wheat. Physiol. Plant. 80, 277-285.
    • (1990) Physiol. Plant. , vol.80 , pp. 277-285
    • Lindsten, A.1    Welch, C.J.2    Schoch, S.3    Ryberg, M.4    Rüdiger, W.5    Sundqvist, C.6
  • 26
    • 0021512010 scopus 로고
    • Analysis of fluorescence decay kinetics from variable-frequency phase shift and modulation data
    • Lakowicz, J. R., E. Gratton, G. Laczko, H. Cherek and M. Limkeman (1984) Analysis of fluorescence decay kinetics from variable-frequency phase shift and modulation data. Biophys. J. 46, 463-477.
    • (1984) Biophys. J. , vol.46 , pp. 463-477
    • Lakowicz, J.R.1    Gratton, E.2    Laczko, G.3    Cherek, H.4    Limkeman, M.5
  • 29
    • 0014965577 scopus 로고
    • Energy transfer between protochlorophyllide molecules: Evidence for multiple chromophores in the photoactive protochlorophyllide-protein complex in vivo and in vitro
    • Kahn, A., N. K. Boardman and S. W. Thorne (1970) Energy transfer between protochlorophyllide molecules: evidence for multiple chromophores in the photoactive protochlorophyllide-protein complex in vivo and in vitro. J. Mol. Biol. 48, 85-101.
    • (1970) J. Mol. Biol. , vol.48 , pp. 85-101
    • Kahn, A.1    Boardman, N.K.2    Thorne, S.W.3
  • 30
    • 0001836937 scopus 로고    scopus 로고
    • Aggregation of NADPH-protochlorophyllide oxidoreductase-pigment complexes is favoured by protein phosphorylation
    • Wiktorsson, B., M. Ryberg and C. Sundqvist (1996) Aggregation of NADPH-protochlorophyllide oxidoreductase-pigment complexes is favoured by protein phosphorylation. Plant Physiol. 34, 23-34.
    • (1996) Plant Physiol. , vol.34 , pp. 23-34
    • Wiktorsson, B.1    Ryberg, M.2    Sundqvist, C.3
  • 31
    • 0036096504 scopus 로고    scopus 로고
    • The effects of low pH on the properties of protochlorophyllide oxidoreductase and the organization of prolamellar bodies of maize (Zea mays)
    • Selstam, E., J. Schelin, T. Brian and W. P. Williams (2002) The effects of low pH on the properties of protochlorophyllide oxidoreductase and the organization of prolamellar bodies of maize (Zea mays). Eur. J. Biochem. 269, 2336-2346.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2336-2346
    • Selstam, E.1    Schelin, J.2    Brian, T.3    Williams, W.P.4
  • 32
    • 0027360306 scopus 로고
    • Cloning, characterization and import studies on protochlorophyllide reductase from wheat (Triticum aestivum)
    • Teakle, G. R. and W. T. Griffiths (1993) Cloning, characterization and import studies on protochlorophyllide reductase from wheat (Triticum aestivum). Biochem. J. 296, 225-230.
    • (1993) Biochem. J. , vol.296 , pp. 225-230
    • Teakle, G.R.1    Griffiths, W.T.2


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