메뉴 건너뛰기




Volumn 36, Issue 3, 1996, Pages 263-270

The Shibata shift; effects of in vitro conditions on the spectral blue-shift of chlorophyllide in irradiated isolated prolamellar bodies

Author keywords

Chlorophyllide; Etioplasts; Fluorescence spectrum; NADPH protochlorophyllide oxidoreductase; Prolamellar body; Protochlorophyllide; Shibata shift

Indexed keywords

BOVINE SERUM ALBUMIN; CALCIUM ION; CHLOROPHYLLIDE; EDETIC ACID; GLYCEROL; OXIDOREDUCTASE; PROTOCHLOROPHYLLIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SUCROSE;

EID: 0030484749     PISSN: 10111344     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1011-1344(96)07394-0     Document Type: Article
Times cited : (18)

References (46)
  • 1
    • 77957246491 scopus 로고
    • Spectroscopic studies on chlorophyll formation in intact leaves
    • [1] K. Shibata, Spectroscopic studies on chlorophyll formation in intact leaves, J. Biochem., 44 (1957) 147-173.
    • (1957) J. Biochem. , vol.44 , pp. 147-173
    • Shibata, K.1
  • 2
    • 0011391074 scopus 로고
    • Chloroplast biogenesis XXII. Contribution of short wavelength and long wavelength protochlorophyll species to the greening of higher plants
    • [2] C.E. Cohen and C.A. Rebeiz, Chloroplast biogenesis XXII. Contribution of short wavelength and long wavelength protochlorophyll species to the greening of higher plants, Plant Physiol., 61 (1978) 824-829.
    • (1978) Plant Physiol. , vol.61 , pp. 824-829
    • Cohen, C.E.1    Rebeiz, C.A.2
  • 3
    • 0003052651 scopus 로고
    • Chloroplast biogenesis 34. Spectrofluorometric characterization in situ of the protochlorophyll species in etiolated tissues of higher plants
    • [3] C.E. Cohen and C.A. Rebeiz, Chloroplast biogenesis 34. Spectrofluorometric characterization in situ of the protochlorophyll species in etiolated tissues of higher plants, Plant Physiol., 67 (1981) 98-103.
    • (1981) Plant Physiol. , vol.67 , pp. 98-103
    • Cohen, C.E.1    Rebeiz, C.A.2
  • 4
    • 0011391689 scopus 로고
    • High resolution optical spectra in vivo. Photoactive protochlorophyllide in etiolated leaves at 5K
    • [4] I. Renge, K. Maurig and R. Avarmaa, High resolution optical spectra in vivo. Photoactive protochlorophyllide in etiolated leaves at 5K, Biochim. Biophys. Acta, 766 (1984) 501-504.
    • (1984) Biochim. Biophys. Acta , vol.766 , pp. 501-504
    • Renge, I.1    Maurig, K.2    Avarmaa, R.3
  • 5
    • 0000241452 scopus 로고
    • The formation of a short-wavelength chlorophyllide form at partial phototransformation of protochlorophyllide in etioplast inner membranes
    • [5] B. Böddi, M. Ryberg and C. Sundqvist, The formation of a short-wavelength chlorophyllide form at partial phototransformation of protochlorophyllide in etioplast inner membranes, Photochem. Photobiol., 53 (1991) 667-673.
    • (1991) Photochem. Photobiol. , vol.53 , pp. 667-673
    • Böddi, B.1    Ryberg, M.2    Sundqvist, C.3
  • 6
    • 0026522499 scopus 로고
    • Identification of four universal protochlorophyllide forms in dark-grown leaves by analyses of the 77 K fluorescence emission spectra
    • [6] B. Böddi, M. Ryberg and C. Sundqvist, 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 (1992) 389-401.
    • (1992) J. Photochem. Photobiol. B: Biol. , vol.12 , pp. 389-401
    • Böddi, B.1    Ryberg, M.2    Sundqvist, C.3
  • 7
    • 85011847403 scopus 로고
    • The polypeptide composition of highly purified prolamellar bodies and prothylakoids from wheat (Triticum aestivum) as revealed by silver staining
    • [7] A. Lindsten, M. Ryberg and C. Sundqvist, The polypeptide composition of highly purified prolamellar bodies and prothylakoids from wheat (Triticum aestivum) as revealed by silver staining, Physiol. Plant., 72 (1988) 167-176.
    • (1988) Physiol. Plant. , vol.72 , pp. 167-176
    • Lindsten, A.1    Ryberg, M.2    Sundqvist, C.3
  • 8
    • 0002119280 scopus 로고
    • Structural and functional significance of pigment-protein complexes of chlorophyll precursors
    • H. Scheer (ed.), CRC Press, Boca Raton
    • [8] M. Ryberg and C. Sundqvist, Structural and functional significance of pigment-protein complexes of chlorophyll precursors, in H. Scheer (ed.), Chlorophylls, CRC Press, Boca Raton, 1991, pp. 587-612.
    • (1991) Chlorophylls , pp. 587-612
    • Ryberg, M.1    Sundqvist, C.2
  • 9
    • 0001836937 scopus 로고    scopus 로고
    • Aggregation of NADPH-protochlorophyllide oxidoreductase-pigment complexes is favoured by protein phosphorylation
    • [9] B. Wiktorsson, M. Ryberg and C. Sundqvist, Aggregation of NADPH-protochlorophyllide oxidoreductase-pigment complexes is favoured by protein phosphorylation, Plant Physiol. Biochem., 34 (1996) 23-34.
    • (1996) Plant Physiol. Biochem. , vol.34 , pp. 23-34
    • Wiktorsson, B.1    Ryberg, M.2    Sundqvist, C.3
  • 10
    • 0000640597 scopus 로고
    • +/NADPH control of the protochlorophyllide-, chlorophyllide proteins in cucumber etioplasts
    • +/NADPH control of the protochlorophyllide-, chlorophyllide proteins in cucumber etioplasts, Photobiochem. Photobiophys., 1 (1980) 219-223.
    • (1980) Photobiochem. Photobiophys. , vol.1 , pp. 219-223
    • Hamouri, B.E.1    Sironval, C.2
  • 11
    • 84987044119 scopus 로고
    • Characterization of prolamellar bodies and prothylakoids fractionated from wheat etioplasts
    • [11] M. Ryberg and C. Sundqvist, Characterization of prolamellar bodies and prothylakoids fractionated from wheat etioplasts, Physiol. Plant., 56 (1982) 125-132.
    • (1982) Physiol. Plant. , vol.56 , pp. 125-132
    • Ryberg, M.1    Sundqvist, C.2
  • 12
    • 0000630429 scopus 로고
    • The aggregational state of protochlorophyllide in isolated prolamellar bodies
    • [12] B. Böddi, A. Lindsten, M. Ryberg and C. Sundqvist, The aggregational state of protochlorophyllide in isolated prolamellar bodies, Physiol. Plant., 76 (1989) 135-143.
    • (1989) Physiol. Plant. , vol.76 , pp. 135-143
    • Böddi, B.1    Lindsten, A.2    Ryberg, M.3    Sundqvist, C.4
  • 13
    • 84989754340 scopus 로고
    • Phototransformation of aggregated forms of protochlorophyllide in isolated etioplast inner membranes
    • [13] B. Böddi, A. Lindsten, M. Ryberg and C. Sundqvist, Phototransformation of aggregated forms of protochlorophyllide in isolated etioplast inner membranes, Photochem. Photobiol., 52 (1990) 83-87.
    • (1990) Photochem. Photobiol. , vol.52 , pp. 83-87
    • Böddi, B.1    Lindsten, A.2    Ryberg, M.3    Sundqvist, C.4
  • 14
    • 0014965577 scopus 로고
    • Energy transfer between protochlorophyllide molecules: Evidence for multiple chromophores in the photoactive protochlorophyllide-protein complex in vivo and in vitro
    • [14] A. Kahn, N.K. Boardman and S.W. Thorne, Energy transfer between protochlorophyllide molecules: evidence for multiple chromophores in the photoactive protochlorophyllide-protein complex in vivo and in vitro, J. Mol. Biol., 48 (1970) 85-101.
    • (1970) J. Mol. Biol. , vol.48 , pp. 85-101
    • Kahn, A.1    Boardman, N.K.2    Thorne, S.W.3
  • 15
    • 0015220496 scopus 로고
    • The greening of etiolated bean leaves 1. The initial photoconversion process
    • [15] S.W. Thorne, The greening of etiolated bean leaves 1. The initial photoconversion process, Biochim. Biophys. Acta, 226 (1971) 113-127.
    • (1971) Biochim. Biophys. Acta , vol.226 , pp. 113-127
    • Thorne, S.W.1
  • 16
    • 0000827385 scopus 로고
    • The reduction of protochlorophyllide into chlorophyllide VI. Calculation of the size of the transfer unit and the initial quantum yield of the reduction in vivo
    • [16] C. Sironval, The reduction of protochlorophyllide into chlorophyllide VI. Calculation of the size of the transfer unit and the initial quantum yield of the reduction in vivo, Photosynthetica, 6 (1972) 375-380.
    • (1972) Photosynthetica , vol.6 , pp. 375-380
    • Sironval, C.1
  • 17
    • 0001973937 scopus 로고
    • The Franck-Inoue chlorophyllide microcycle II in vivo and in vitro
    • C. Sironval and M. Brouers (eds.), Martinus Nijhoff/Dr W. Junk Publishers, The Hague
    • [17] C. Sironval, F. Franck, R. Gysembergh, B. Bereza and E. Dujardin, The Franck-Inoue chlorophyllide microcycle II in vivo and in vitro, in C. Sironval and M. Brouers (eds.), Protochlorophyllide reduction and greening, Martinus Nijhoff/Dr W. Junk Publishers, The Hague, 1984, pp. 197-222.
    • (1984) Protochlorophyllide Reduction and Greening , pp. 197-222
    • Sironval, C.1    Franck, F.2    Gysembergh, R.3    Bereza, B.4    Dujardin, E.5
  • 18
    • 84989699852 scopus 로고
    • Temperature dependence of chlorophyll(ide) spectral shifts and photoactive protochlorophyllide regeneration after flash in etiolated barley leaves
    • [18] P. Eullaffroy, R. Salvetat, F. Franck and R. Popovic, Temperature dependence of chlorophyll(ide) spectral shifts and photoactive protochlorophyllide regeneration after flash in etiolated barley leaves, Photochem. Photobiol., 62 (1995) 751-756.
    • (1995) Photochem. Photobiol. , vol.62 , pp. 751-756
    • Eullaffroy, P.1    Salvetat, R.2    Franck, F.3    Popovic, R.4
  • 19
    • 0011481856 scopus 로고
    • Correlation of the 680 to 672 nm spectral shift and the halving of the apparent molecular weight for chlorophyll (ide) holochrome from barley
    • [19] B.M. Stummann, Correlation of the 680 to 672 nm spectral shift and the halving of the apparent molecular weight for chlorophyll (ide) holochrome from barley, Physiol. Plant., 45 (1979) 122-126.
    • (1979) Physiol. Plant. , vol.45 , pp. 122-126
    • Stummann, B.M.1
  • 20
    • 85012866668 scopus 로고
    • The regular ultrastructure of isolated prolamellar bodies depends on the presence of membrane-bound NADPH-protochlorophyllide oxidoreductase
    • [20] M. Ryberg and C. Sundqvist, The regular ultrastructure of isolated prolamellar bodies depends on the presence of membrane-bound NADPH-protochlorophyllide oxidoreductase, Physiol. Plant., 73 (1988) 218-226.
    • (1988) Physiol. Plant. , vol.73 , pp. 218-226
    • Ryberg, M.1    Sundqvist, C.2
  • 21
    • 0001633977 scopus 로고
    • Pigment-protein complexes of illuminated etiolated leaves
    • [21] R.P. Oliver and W.T. Griffiths, Pigment-protein complexes of illuminated etiolated leaves, Plant Physiol., 70 (1982) 1019-1025.
    • (1982) Plant Physiol. , vol.70 , pp. 1019-1025
    • Oliver, R.P.1    Griffiths, W.T.2
  • 22
    • 84981566104 scopus 로고
    • The relation between the phytylation and the 682-672 shift in vivo of chlorophyll a
    • [22] G. Akoyunoglou and G. Michalopoulus, The relation between the phytylation and the 682-672 shift in vivo of chlorophyll a, Physiol. Plant., 25 (1971) 324-329.
    • (1971) Physiol. Plant. , vol.25 , pp. 324-329
    • Akoyunoglou, G.1    Michalopoulus, G.2
  • 25
    • 0011391289 scopus 로고
    • A short-lived intermediate form in the in vivo conversion of protochlorophyllide650 to chlorophyllide684
    • [25] B.A. Bonner, A short-lived intermediate form in the in vivo conversion of protochlorophyllide650 to chlorophyllide684, Plant Physiol., 44 (1969) 739-747.
    • (1969) Plant Physiol. , vol.44 , pp. 739-747
    • Bonner, B.A.1
  • 26
    • 84986980163 scopus 로고
    • Spectral forms of protochlorophyllide in prolamellar bodies and prothylakoids fractionated from wheat etioplasts
    • [26] M. Ryberg and C. Sundqvist, Spectral forms of protochlorophyllide in prolamellar bodies and prothylakoids fractionated from wheat etioplasts, Physiol. Plant., 56 (1982) 133-138.
    • (1982) Physiol. Plant. , vol.56 , pp. 133-138
    • Ryberg, M.1    Sundqvist, C.2
  • 27
    • 0001845010 scopus 로고
    • Factors affecting the photoconversion of protochlorophyllide to chlorophyllide in etioplast membranes isolated from barley
    • [27] P. Brodersen, Factors affecting the photoconversion of protochlorophyllide to chlorophyllide in etioplast membranes isolated from barley, Photosynthetica, 10 (1976) 33-39.
    • (1976) Photosynthetica , vol.10 , pp. 33-39
    • Brodersen, P.1
  • 28
    • 0011489153 scopus 로고
    • Freezing of isolated thylakoid membranes in complex media. VII. The effect of bovine serum albumin
    • [28] K.A. Santarius, Freezing of isolated thylakoid membranes in complex media. VII. The effect of bovine serum albumin, Biochem. Physiol. Pflanzen, 187 (1991) 149-162.
    • (1991) Biochem. Physiol. Pflanzen , vol.187 , pp. 149-162
    • Santarius, K.A.1
  • 29
    • 0016387932 scopus 로고
    • Protein and hydrogen ion control of photochromism in aminoazobenzene compounds
    • [29] R. Lovrien, P. Pesheck and W. Tisel, Protein and hydrogen ion control of photochromism in aminoazobenzene compounds, J. Am. Chem. Soc., 96 (1974) 244-248.
    • (1974) J. Am. Chem. Soc. , vol.96 , pp. 244-248
    • Lovrien, R.1    Pesheck, P.2    Tisel, W.3
  • 30
    • 0020727750 scopus 로고
    • Spectral study of the photochemistry of dipyrrole models for bilirubin bound to human serum albumin
    • [30] A.A. Lamola, S.E. Braslavsky, K. Schaffner and D.A. Lightner, Spectral study of the photochemistry of dipyrrole models for bilirubin bound to human serum albumin, Photochem. Photobiol., 37 (1983) 263-270.
    • (1983) Photochem. Photobiol. , vol.37 , pp. 263-270
    • Lamola, A.A.1    Braslavsky, S.E.2    Schaffner, K.3    Lightner, D.A.4
  • 31
    • 0011480906 scopus 로고
    • Examination of ribosome-like particles in isolated prolamellar bodies
    • [31] A.R. Wellburn, P.H. Quail, and B.E.S. Gunning, Examination of ribosome-like particles in isolated prolamellar bodies, Planta, 134 (1977) 45-52.
    • (1977) Planta , vol.134 , pp. 45-52
    • Wellburn, A.R.1    Quail, P.H.2    Gunning, B.E.S.3
  • 32
    • 0011484253 scopus 로고
    • Prolamellar bodies of oat, wheat and rye: Structure, lipid composition, and adsorption of saponins
    • [32] G. Protoschill-Krebs and J. Kesselmeier, Prolamellar bodies of oat, wheat and rye: Structure, lipid composition, and adsorption of saponins, Protoplasma, 146 (1988) 1-9.
    • (1988) Protoplasma , vol.146 , pp. 1-9
    • Protoschill-Krebs, G.1    Kesselmeier, J.2
  • 33
    • 84989741995 scopus 로고
    • Binding properties of protochlorophyllide oxidoreductase to isolated immobilized prolamellar bodies as revealed by detergent and ion treatments
    • [33] C. Grevby, S. Engdahl, M. Ryberg and C. Sundqvist, Binding properties of protochlorophyllide oxidoreductase to isolated immobilized prolamellar bodies as revealed by detergent and ion treatments, Physiol. Plant., 77 (1989) 493-503.
    • (1989) Physiol. Plant. , vol.77 , pp. 493-503
    • Grevby, C.1    Engdahl, S.2    Ryberg, M.3    Sundqvist, C.4
  • 34
    • 0011436995 scopus 로고
    • Influence of divalent cations and chelators on the structure of prolamellar bodies of Avena sativa
    • [34] K.U. Lachmann and J. Kesselmeier, Influence of divalent cations and chelators on the structure of prolamellar bodies of Avena sativa. Plant Cell Physiol., 30 (1989) 1081-1088.
    • (1989) Plant Cell Physiol. , vol.30 , pp. 1081-1088
    • Lachmann, K.U.1    Kesselmeier, J.2
  • 35
    • 0001578756 scopus 로고
    • Effects of salt wash on the structure of the prolamellar body membrane and the membrane binding of NADPH-protochlorophyllide oxidoreductase
    • [35] A. Widell-Wigge and E. Selstam, Effects of salt wash on the structure of the prolamellar body membrane and the membrane binding of NADPH-protochlorophyllide oxidoreductase, Physiol. Plant., 78 (1990) 315-323.
    • (1990) Physiol. Plant. , vol.78 , pp. 315-323
    • Widell-Wigge, A.1    Selstam, E.2
  • 36
    • 0000117104 scopus 로고
    • On the nature and possible functions of the 673-and 684-mμ forms in vivo of chlorophyll
    • [36] C. Sironval, M.R. Michel-Wolwertz, and A. Madsen, On the nature and possible functions of the 673-and 684-mμ forms in vivo of chlorophyll, Biochim. Biophys. Acta, 94 (1965) 344-354.
    • (1965) Biochim. Biophys. Acta , vol.94 , pp. 344-354
    • Sironval, C.1    Michel-Wolwertz, M.R.2    Madsen, A.3
  • 37
    • 0014005415 scopus 로고
    • The relation between structure and pigments during the first stages of proplastid greening
    • [37] W.L. Butler and W.R. Briggs, The relation between structure and pigments during the first stages of proplastid greening, Biochim. Biophys. Acta, 112 (1966) 45-53.
    • (1966) Biochim. Biophys. Acta , vol.112 , pp. 45-53
    • Butler, W.L.1    Briggs, W.R.2
  • 38
    • 0001084795 scopus 로고
    • Localization of NADPH-protochlorophyllide oxidoreductase in dark-grown wheat (Triticum aestivum) by immuno-electron microscopy before and after transformation of the prolamellar bodies
    • [38] M. Ryberg and K. Dehesh, Localization of NADPH-protochlorophyllide oxidoreductase in dark-grown wheat (Triticum aestivum) by immuno-electron microscopy before and after transformation of the prolamellar bodies, Physiol. Plant., 66 (1986) 616-624.
    • (1986) Physiol. Plant. , vol.66 , pp. 616-624
    • Ryberg, M.1    Dehesh, K.2
  • 39
    • 84989665833 scopus 로고
    • Isolelectric focusing of pigment-protein complexes solubilized from non-irradiated and irradiated prolamellar bodies
    • [39] B. Wiktorsson, M. Ryberg, S. Gough and C. Sundqvist, Isolelectric focusing of pigment-protein complexes solubilized from non-irradiated and irradiated prolamellar bodies, Physiol. Plant., 85 (1992) 659-669.
    • (1992) Physiol. Plant. , vol.85 , pp. 659-669
    • Wiktorsson, B.1    Ryberg, M.2    Gough, S.3    Sundqvist, C.4
  • 40
    • 0001402677 scopus 로고
    • The effects of cross-linking of the subunits of NADPH-protochlorophyllide oxidoreductase on the aggregational state of protochlorophyllide
    • [40] B. Wiktorsson, S. Engdahl, L.B. Zhong, B. Böddi, M. Ryberg and C. Sundqvist, The effects of cross-linking of the subunits of NADPH-protochlorophyllide oxidoreductase on the aggregational state of protochlorophyllide, Photosynthetica, 29 (1993) 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
  • 41
    • 0011390340 scopus 로고
    • Spectral changes of phytochrome in glycerol solutions
    • [41] A.P. Belangé, Spectral changes of phytochrome in glycerol solutions, Physiol. Veg., 12 (1974) 95-105.
    • (1974) Physiol. Veg. , vol.12 , pp. 95-105
    • Belangé, A.P.1
  • 42
    • 0024975322 scopus 로고
    • Surface enhanced resonance Raman scattering (SERRS) as a probe of the structural differences between the Pr and Pfr forms of phytochrome
    • [42] B.N. Rospendowski, D.L. Farrens, T.M. Cotton and P.-S. Song, Surface enhanced resonance Raman scattering (SERRS) as a probe of the structural differences between the Pr and Pfr forms of phytochrome, FEBS Lett., 258 (1989) 1-4.
    • (1989) FEBS Lett. , vol.258 , pp. 1-4
    • Rospendowski, B.N.1    Farrens, D.L.2    Cotton, T.M.3    Song, P.-S.4
  • 43
    • 0024747204 scopus 로고
    • Differential exposure of aromatic amino acids in the red-light-absorbing and far-red-light-absorbing forms of 124-kDa oat phytochrome
    • [43] B.R. Singh, P.-S. Song, P. Eilfeld and W. Rüdiger, Differential exposure of aromatic amino acids in the red-light-absorbing and far-red-light-absorbing forms of 124-kDa oat phytochrome, Eur. J. Biochem., 184 (1989) 715-721.
    • (1989) Eur. J. Biochem. , vol.184 , pp. 715-721
    • Singh, B.R.1    Song, P.-S.2    Eilfeld, P.3    Rüdiger, W.4
  • 44
    • 0025769785 scopus 로고
    • Molecular modelling of phytochrome
    • [44] J.L. Gabriel and K.J. Hoober, Molecular modelling of phytochrome, J. Theor. Biol., 151 (1991) 541-556.
    • (1991) J. Theor. Biol. , vol.151 , pp. 541-556
    • Gabriel, J.L.1    Hoober, K.J.2
  • 45
    • 0000668045 scopus 로고
    • Light-induced breakdown of NADPH-protochlorophyllide oxidoreductase in vitro
    • [45] S.A. Kay and W.T. Griffiths, Light-induced breakdown of NADPH-protochlorophyllide oxidoreductase in vitro, Plant Physiol., 72 (1983) 229-236.
    • (1983) Plant Physiol. , vol.72 , pp. 229-236
    • Kay, S.A.1    Griffiths, W.T.2
  • 46
    • 0016157537 scopus 로고
    • The interaction of a cationic detergent with bovine serum albumin and other proteins
    • [46] Y. Nozaki, J.A. Reynolds and C. Tanford, The interaction of a cationic detergent with bovine serum albumin and other proteins, J. Biol. Chem., 249 (1974) 4452-459.
    • (1974) J. Biol. Chem. , vol.249 , pp. 4452-4459
    • Nozaki, Y.1    Reynolds, J.A.2    Tanford, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.