메뉴 건너뛰기




Volumn 100, Issue 4, 1997, Pages 769-779

Novel aspects of chlorophyll a/b-binding proteins

Author keywords

Light harvesting; Photoprotection; Photosynthesis

Indexed keywords


EID: 0030870674     PISSN: 00319317     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1399-3054.1997.1000404.x     Document Type: Article
Times cited : (78)

References (105)
  • 1
    • 0030776273 scopus 로고    scopus 로고
    • ELIPs - Light-induced stress proteins
    • Adamska, I. 1997. ELIPs - Light-induced stress proteins. -Physiol. Plant. 100: 794-805.
    • (1997) Physiol. Plant , vol.100 , pp. 794-805
    • Adamska, I.1
  • 2
    • 0026556851 scopus 로고
    • Protein phosphorylation in regulation of photosynthesis
    • Allen, J. F. 1992. Protein phosphorylation in regulation of photosynthesis. - Biochim. Biophys. Acta 1098: 275-335.
    • (1992) Biochim. Biophys. Acta , vol.1098 , pp. 275-335
    • Allen, J.F.1
  • 3
    • 84989674556 scopus 로고
    • Thylakoid protein phosphorylation, state 1-state 2 transitions, and photosystem stoichiometry adjustment: Redox control at multiple levels of gene expression
    • _ 1995. Thylakoid protein phosphorylation, state 1-state 2 transitions, and photosystem stoichiometry adjustment: Redox control at multiple levels of gene expression. - Physiol. Plant. 93: 196-205.
    • (1995) Physiol. Plant , vol.93 , pp. 196-205
  • 4
    • 0030869955 scopus 로고    scopus 로고
    • Redox signalling and the structural basis of regulation of photosynthesis by protein phosphorylation
    • _ & Nilsson, A. 1997. Redox signalling and the structural basis of regulation of photosynthesis by protein phosphorylation. - Physiol. Plant. 100: 863-868.
    • (1997) Physiol. Plant. , vol.100 , pp. 863-868
    • Nilsson, A.1
  • 5
    • 36849155728 scopus 로고
    • Chloroplast protein phosphorylation couples plastoquinone redox state to distribution of excitation energy between photosystems
    • _, Bennet, J., Steinback, K. E. & Arntzen, C. J. 1981. Chloroplast protein phosphorylation couples plastoquinone redox state to distribution of excitation energy between photosystems. - Nature 291: 21-25.
    • (1981) Nature , vol.291 , pp. 21-25
    • Bennet, J.1    Steinback, K.E.2    Arntzen, C.J.3
  • 6
    • 0030767058 scopus 로고    scopus 로고
    • Proteolytic activities and proteases of plant chloroplasts
    • Andersson, B. & Aro, E.-M. 1997. Proteolytic activities and proteases of plant chloroplasts. - Physiol. Plant. 100: 780-793.
    • (1997) Physiol. Plant. , vol.100 , pp. 780-793
    • Andersson, B.1    Aro, E.-M.2
  • 8
    • 0026541431 scopus 로고
    • A supramolecular antenna complex from photosystem II membranes
    • Bassi, R. & Dainese, P. 1992. A supramolecular antenna complex from photosystem II membranes. - Eur. J. Biochem. 204: 317-326.
    • (1992) Eur. J. Biochem. , vol.204 , pp. 317-326
    • Bassi, R.1    Dainese, P.2
  • 10
    • 0345173281 scopus 로고
    • Changes in the organization of stroma membranes induced by in vivo state 1-state 2 transition
    • _, Giacometti, G. M. & Simpson, D. J. 1988. Changes in the organization of stroma membranes induced by in vivo state 1-state 2 transition. - Biochim. Biophys. Acta 1060: 271-283.
    • (1988) Biochim. Biophys. Acta , vol.1060 , pp. 271-283
    • Giacometti, G.M.1    Simpson, D.J.2
  • 11
    • 0024740838 scopus 로고
    • Two-dimensional crystals of the photosystem II reaction center complex from higher plants
    • _, Ghiretti Magaldi, A., Tognon, G., Giacometti, G. M. & Miller, K. 1989. Two-dimensional crystals of the photosystem II reaction center complex from higher plants. - Eur. J. Cell Biol. 50: 84-93.
    • (1989) Eur. J. Cell Biol. , vol.50 , pp. 84-93
    • Ghiretti Magaldi, A.1    Tognon, G.2    Giacometti, G.M.3    Miller, K.4
  • 12
    • 84989692351 scopus 로고
    • Chlorophyll binding proteins with antenna function in higher plants and green algae
    • _, Rigoni, F. & Giacometti, G. M. 1990. Chlorophyll binding proteins with antenna function in higher plants and green algae. - Photochem. Photobiol. 52: 1187-1206.
    • (1990) Photochem. Photobiol. , vol.52 , pp. 1187-1206
    • Rigoni, F.1    Giacometti, G.M.2
  • 13
    • 0027476540 scopus 로고
    • Carotenoid-binding proteins of photosystem II
    • _, Pineau, B., Dainese, P. & Marquardt, J. 1993. Carotenoid-binding proteins of photosystem II. - Eur. J. Biochem. 212: 297-303.
    • (1993) Eur. J. Biochem. , vol.212 , pp. 297-303
    • Pineau, B.1    Dainese, P.2    Marquardt, J.3
  • 14
    • 1842381765 scopus 로고    scopus 로고
    • Biochemistry and molecular biology of pigment binding proteins
    • Light as Energy Source and Information Carrier in Plant Physiology (R. C. Jennings, ed.). Plenum Press, New York, NY. ISBN 0-306-45383-5
    • _, Giuffra, E., Croce, R., Dainese, P. & Bergantino, E. 1996. Biochemistry and molecular biology of pigment binding proteins. - In Light as Energy Source and Information Carrier in Plant Physiology (R. C. Jennings, ed.), pp. 41-64. Proceeding of the NATO Advanced Study Institute. Plenum Press, New York, NY. ISBN 0-306-45383-5.
    • (1996) Proceeding of the NATO Advanced Study Institute , pp. 41-64
    • Giuffra, E.1    Croce, R.2    Dainese, P.3    Bergantino, E.4
  • 15
    • 0005323080 scopus 로고
    • Concentration quenching of chlorophyll fluorescence in bilayer lipid vesicles and liposomes
    • Beddard, G. S., Carlin, S. E. & Porter, G. 1976. Concentration quenching of chlorophyll fluorescence in bilayer lipid vesicles and liposomes. - Chem. Phys. Lett. 43: 27-32.
    • (1976) Chem. Phys. Lett. , vol.43 , pp. 27-32
    • Beddard, G.S.1    Carlin, S.E.2    Porter, G.3
  • 16
    • 0019925148 scopus 로고
    • Biosynthesis of chlorophyll a/b binding polypeptides in wild type and the chlorina f2 mutant of barley
    • Bellemare, G. S., Bartlett, G. & Chua, N. H. 1982. Biosynthesis of chlorophyll a/b binding polypeptides in wild type and the chlorina f2 mutant of barley. - J. Biol. Chem. 257: 7762-7767.
    • (1982) J. Biol. Chem. , vol.257 , pp. 7762-7767
    • Bellemare, G.S.1    Bartlett, G.2    Chua, N.H.3
  • 17
    • 0028988014 scopus 로고
    • A post-translational modification of the photosystem II subunit CP29 protects maize from cold stress
    • Bergantino, E., Dainese, P., Cerovic, Z., Sechi, S. & Bassi, R. 1995. A post-translational modification of the photosystem II subunit CP29 protects maize from cold stress. - J. Biol. Chem. 270: 8474-8481.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8474-8481
    • Bergantino, E.1    Dainese, P.2    Cerovic, Z.3    Sechi, S.4    Bassi, R.5
  • 18
    • 1842314261 scopus 로고    scopus 로고
    • The photosystem II subunit CP29 can be phosphorylated in both C3 and C4 plants as suggested by sequence analysis
    • In press
    • _, Sandonà, D., Cugini, D. & Bassi, R. 1997. The photosystem II subunit CP29 can be phosphorylated in both C3 and C4 plants as suggested by sequence analysis. - Plant Mol. Biol. (In press).
    • (1997) Plant Mol. Biol.
    • Sandonà, D.1    Cugini, D.2    Bassi, R.3
  • 19
    • 0001848758 scopus 로고
    • Regulation of photosynthetic light energy capture, conversion and dissipaton in leaves of higher plants
    • E. D. Schulze and M. Caldwell, eds. Springer-Verlag, New York, NY
    • Björkman, O. & Demming-Adams, B. 1993. Regulation of photosynthetic light energy capture, conversion and dissipaton in leaves of higher plants. - In Ecological Studies (E. D. Schulze and M. Caldwell, eds), Vol. 100, pp. 14-47. Springer-Verlag, New York, NY.
    • (1993) Ecological Studies , vol.100 , pp. 14-47
    • Björkman, O.1    Demming-Adams, B.2
  • 20
    • 0025219925 scopus 로고
    • The structure of spinach photosystem I studied by electron microscopy
    • Boekema, E. J., Wynn, R. M. & Malkin, R. 1990. The structure of spinach photosystem I studied by electron microscopy. -Biochim. Biophys, Acta 1017: 49-56.
    • (1990) Biochim. Biophys, Acta , vol.1017 , pp. 49-56
    • Boekema, E.J.1    Wynn, R.M.2    Malkin, R.3
  • 22
    • 0018787380 scopus 로고
    • A quantitative study of the slow decline of chlorophyll a fluorescence in isolated chloroplasts
    • Briantais, J. M., Vernotte, C., Picaud, M. & Krause, G. H. 1979. A quantitative study of the slow decline of chlorophyll a fluorescence in isolated chloroplasts. - Biochim. Biophys. Acta 548: 128-138.
    • (1979) Biochim. Biophys. Acta , vol.548 , pp. 128-138
    • Briantais, J.M.1    Vernotte, C.2    Picaud, M.3    Krause, G.H.4
  • 23
    • 0001473449 scopus 로고
    • Aggregate size of the light-harvesting chlorophyll a/b protein in detergent solution
    • Butler, P. J. G. & Kühlbrandt, W. 1988. Aggregate size of the light-harvesting chlorophyll a/b protein in detergent solution. - Proc. Natl. Acad. Sci. USA 85: 3797-3801.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 3797-3801
    • Butler, P.J.G.1    Kühlbrandt, W.2
  • 24
    • 1842331565 scopus 로고    scopus 로고
    • Femtosecond transient absorption study of carotenoid to chlorophyll energy transfer in the light harvesting complex of photosystem II
    • Connelly, J. P., Muller, M., Bassi, R., Croce, R. & Holzwarth, A. R. 1997. Femtosecond transient absorption study of carotenoid to chlorophyll energy transfer in the light harvesting complex of photosystem II. - Biochemistry 36: 281-287.
    • (1997) Biochemistry , vol.36 , pp. 281-287
    • Connelly, J.P.1    Muller, M.2    Bassi, R.3    Croce, R.4    Holzwarth, A.R.5
  • 25
    • 0029739337 scopus 로고    scopus 로고
    • Conformational changes induced by phosphorylation in the photosystem II subunit CP29
    • Croce, R., Breton, J. & Bassi, R. 1996. Conformational changes induced by phosphorylation in the photosystem II subunit CP29. - Biochemistry 35: 11142-11148.
    • (1996) Biochemistry , vol.35 , pp. 11142-11148
    • Croce, R.1    Breton, J.2    Bassi, R.3
  • 26
    • 0028168064 scopus 로고
    • A molecular mechanism for qE-quenching
    • Crofts, A. R. & Yerkes, C. T. 1994. A molecular mechanism for qE-quenching. - FEBS Lett. 352: 265-270.
    • (1994) FEBS Lett. , vol.352 , pp. 265-270
    • Crofts, A.R.1    Yerkes, C.T.2
  • 27
    • 0025837874 scopus 로고
    • Subunit stoichiometry of the chloroplast photosystem II antenna system and aggregation state of the component chlorophyll a/b binding proteins
    • Dainese, P. & Bassi, R. 1991. Subunit stoichiometry of the chloroplast photosystem II antenna system and aggregation state of the component chlorophyll a/b binding proteins. - J. Biol. Chem. 266: 8136-8142.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8136-8142
    • Dainese, P.1    Bassi, R.2
  • 28
    • 0028587976 scopus 로고
    • Light regulated translation of chloroplast messenger RNAs through redox potential
    • Danon, A. & Mayfield, S. P. 1994. Light regulated translation of chloroplast messenger RNAs through redox potential. - Science 266: 1717-1719.
    • (1994) Science , vol.266 , pp. 1717-1719
    • Danon, A.1    Mayfield, S.P.2
  • 29
    • 0029670893 scopus 로고    scopus 로고
    • Exciton equilibration and photosystem II exciton dynamics: A fluorescence study on photosystem II membrane particles of spinach
    • Dau, H. & Sauer, K. 1996. Exciton equilibration and photosystem II exciton dynamics: A fluorescence study on photosystem II membrane particles of spinach. - Biochim. Biophys. Acta 1273: 175-190.
    • (1996) Biochim. Biophys. Acta , vol.1273 , pp. 175-190
    • Dau, H.1    Sauer, K.2
  • 30
    • 0025187594 scopus 로고
    • Carotenoids and photoprotection in plants. A role for the xanthophyll zeaxanthin
    • Demmig-Adams, B. 1990. Carotenoids and photoprotection in plants. A role for the xanthophyll zeaxanthin. - Biochim. Biophys. Acta 1020: 1-24.
    • (1990) Biochim. Biophys. Acta , vol.1020 , pp. 1-24
    • Demmig-Adams, B.1
  • 31
    • 0011057045 scopus 로고
    • Isolation and characterisation of a new minor chlorophyll a/b protein complex (CP24) from spinach
    • Dunahay, T. G. & Staehelin, L. A. 1986. Isolation and characterisation of a new minor chlorophyll a/b protein complex (CP24) from spinach. - Plant Physiol. 80: 429-434.
    • (1986) Plant Physiol. , vol.80 , pp. 429-434
    • Dunahay, T.G.1    Staehelin, L.A.2
  • 32
    • 0028865421 scopus 로고
    • Light intensity regulation of CAB gene transcription is signaled by the redox state of the plastoquinone pool
    • Escoubas, J. M., Lomas, M., La Roche, J. & Falkowski, P. G. 1995. Light intensity regulation of CAB gene transcription is signaled by the redox state of the plastoquinone pool. Proc. Natl. Acad. Sci. USA 92: 10237-10241.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10237-10241
    • Escoubas, J.M.1    Lomas, M.2    La Roche, J.3    Falkowski, P.G.4
  • 33
    • 0030774584 scopus 로고    scopus 로고
    • The xanthophyll cycle, its regulation and components
    • Eskling, M., Arvidsson, P.-O. & Åkerlund, H.-E. 1997. The xanthophyll cycle, its regulation and components. - Physiol. Plant. 100: 806-816.
    • (1997) Physiol. Plant. , vol.100 , pp. 806-816
    • Eskling, M.1    Arvidsson, P.-O.2    Åkerlund, H.-E.3
  • 34
    • 0029858001 scopus 로고    scopus 로고
    • Crystallisation and identification of an assembly defect of recombinant antenna complexes produced in transgenic tobacco plants
    • Flachman, R. & Kühlbrandt, W. 1996. Crystallisation and identification of an assembly defect of recombinant antenna complexes produced in transgenic tobacco plants. - Proc. Nati. Acad. Sci. USA 93: 14966-14971.
    • (1996) Proc. Nati. Acad. Sci. USA , vol.93 , pp. 14966-14971
    • Flachman, R.1    Kühlbrandt, W.2
  • 36
    • 0028218997 scopus 로고
    • The intrinsic 22 kJDa protein is a chlorophyll-binding subunit of photosystem II
    • Funk, C., Schröder, W. P., Green, B. R., Renger, G. & Andersson, B. 1994. The intrinsic 22 kJDa protein is a chlorophyll-binding subunit of photosystem II. - FEBS Lett. 342: 261-266.
    • (1994) FEBS Lett. , vol.342 , pp. 261-266
    • Funk, C.1    Schröder, W.P.2    Green, B.R.3    Renger, G.4    Andersson, B.5
  • 38
    • 0030774348 scopus 로고    scopus 로고
    • Redox-controlled thylakoid protein phosphorylation. News and views
    • _, Zer, H. & Ohad, I. 1997. Redox-controlled thylakoid protein phosphorylation. News and views. - Physiol. Plant. 100: 869-885.
    • (1997) Physiol. Plant. , vol.100 , pp. 869-885
    • Zer, H.1    Ohad, I.2
  • 39
    • 85023704649 scopus 로고
    • The relationship between the quantum yield of photosynthetic electron transport and quenching of chlorophyll fluorescence
    • Genty, B., Briantais, J. M. & Baker, N. R. 1989. The relationship between the quantum yield of photosynthetic electron transport and quenching of chlorophyll fluorescence. - Biochim. Biophys. Acta 990: 87-92.
    • (1989) Biochim. Biophys. Acta , vol.990 , pp. 87-92
    • Genty, B.1    Briantais, J.M.2    Baker, N.R.3
  • 40
    • 0029967212 scopus 로고    scopus 로고
    • Reconstitution and pigment-binding properties of recombinant CP29
    • Giuffra, E., Cugini, D., Croce, R. & Bassi, R. 1996. Reconstitution and pigment-binding properties of recombinant CP29. -Eur. J. Biochem. 238: 112-120.
    • (1996) Eur. J. Biochem. , vol.238 , pp. 112-120
    • Giuffra, E.1    Cugini, D.2    Croce, R.3    Bassi, R.4
  • 42
    • 0025897315 scopus 로고
    • Chlorophyll a/b binding proteins: An extended family
    • _, Pichersky, E. & Kloppstech, K. 1991. Chlorophyll a/b binding proteins: An extended family. - Trends Biochem. Sci. 16: 181-186.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 181-186
    • Pichersky, E.1    Kloppstech, K.2
  • 43
    • 0023656044 scopus 로고
    • The early light-inducible proteins of barley: Characterisation of two families of nuclear-coded chloroplast proteins
    • Grimm, B. & Kloppstech, K. 1987. The early light-inducible proteins of barley: characterisation of two families of nuclear-coded chloroplast proteins. - Eur. J. Biochem. 167: 493-499.
    • (1987) Eur. J. Biochem. , vol.167 , pp. 493-499
    • Grimm, B.1    Kloppstech, K.2
  • 44
    • 0024766999 scopus 로고
    • Transiently expressed early light-inducible thylakoid proteins share trans-membrane domains with light-harvesting chlorophyll binding proteins
    • _, Kruse, E. & Kloppstech, K. 1989. Transiently expressed early light-inducible thylakoid proteins share trans-membrane domains with light-harvesting chlorophyll binding proteins. - Plant Mol. Biol. 13: 583-593.
    • (1989) Plant Mol. Biol. , vol.13 , pp. 583-593
    • Kruse, E.1    Kloppstech, K.2
  • 45
    • 85006828126 scopus 로고
    • The reversible, light-induced, conversion of xantophylls in the chloroplast
    • Hager, A. 1975. The reversible, light-induced, conversion of xantophylls in the chloroplast. - Ber. Dtsch. Bot. Ges. 88: 27-44.
    • (1975) Ber. Dtsch. Bot. Ges. , vol.88 , pp. 27-44
    • Hager, A.1
  • 46
    • 0028004703 scopus 로고
    • Localisation of the xantophyll-cycle enzyme violaxanthin de-epoxidase within the thylakoid lumen and abolition of its mobility by a (light-dependent) pH decrease
    • _ & Holocher, K. 1994. Localisation of the xantophyll-cycle enzyme violaxanthin de-epoxidase within the thylakoid lumen and abolition of its mobility by a (light-dependent) pH decrease. - Planta 192: 581-589.
    • (1994) Planta , vol.192 , pp. 581-589
    • Holocher, K.1
  • 47
    • 0000133898 scopus 로고
    • Organization and stability of polypeptides associated vith the chlorophyll a-b light-harvesting complex of photosystem II
    • Harrison, M. A. & Melis, A. 1992. Organization and stability of polypeptides associated vith the chlorophyll a-b light-harvesting complex of photosystem II. - Plant Cell Physiol. 33: 627-637.
    • (1992) Plant Cell Physiol. , vol.33 , pp. 627-637
    • Harrison, M.A.1    Melis, A.2
  • 48
    • 0028049588 scopus 로고
    • Trimerization and crystallization of reconstituted light-harvesting chlorophyll a/b complex
    • Hobe, S., Prytulla, S., Kühlbrandt, W. & Paulsen, H. 1994. Trimerization and crystallization of reconstituted light-harvesting chlorophyll a/b complex. - EMBO J. 13: 3423-3429.
    • (1994) EMBO J. , vol.13 , pp. 3423-3429
    • Hobe, S.1    Prytulla, S.2    Kühlbrandt, W.3    Paulsen, H.4
  • 49
    • 0028920225 scopus 로고
    • N-proximal sequence motif in light-harvesting chlorophyll a-c-binding protein of dinoflagellates: A putative polyprotein
    • _, Foster, R., Klinger, J. & Paulsen, H. 1995. N-proximal sequence motif in light-harvesting chlorophyll a-c-binding protein of dinoflagellates: A putative polyprotein. - FEBS Lett. 363: 175-178.
    • (1995) FEBS Lett. , vol.363 , pp. 175-178
    • Foster, R.1    Klinger, J.2    Paulsen, H.3
  • 51
    • 0000076793 scopus 로고
    • Excited-state kinetics in chlorophyll systems and its relationship to the functional organization of the photosystems
    • H. Scheer. ed. CRC Press, Boca Raton. FL. ISBN 0-8493-6842-1
    • Holzwarth, A. R. 1991. Excited-state kinetics in chlorophyll systems and its relationship to the functional organization of the photosystems. - In Chlorophylls (H. Scheer. ed.). pp. 1125-1151. CRC Press, Boca Raton. FL. ISBN 0-8493-6842-1.
    • (1991) Chlorophylls , pp. 1125-1151
    • Holzwarth, A.R.1
  • 52
    • 0008323838 scopus 로고
    • Exciton dynamics in antennae and reaction centers of photosystem I and II
    • N. Murata. ed. Kluver Academic Publishers, Dordrecht. ISBN 0-7923-2073-5
    • _ 1992. Exciton dynamics in antennae and reaction centers of photosystem I and II. - In Research in Photosynthesis (N. Murata. ed.), Vol. I, pp. 187-194. Kluver Academic Publishers, Dordrecht. ISBN 0-7923-2073-5.
    • (1992) Research in Photosynthesis , vol.1 , pp. 187-194
  • 53
    • 0001157047 scopus 로고
    • The role of LHCII in energy quenching
    • N. R. Baker and J. R. Bowyer, eds. Bios Scientific Publishers, Oxford
    • Horton, P. & Ruban, A. 1994. The role of LHCII in energy quenching. - In Photoinhibition of Photosynthesis (N. R. Baker and J. R. Bowyer, eds), pp. 111-128. Bios Scientific Publishers, Oxford.
    • (1994) Photoinhibition of Photosynthesis , pp. 111-128
    • Horton, P.1    Ruban, A.2
  • 55
    • 1642606238 scopus 로고
    • 6/f ATPase activity
    • P. Mathis, ed. Kluwer Academic Publishers, Dordrecht, ISBN 0-7923-3862-6
    • 6/f ATPase activity. - In Photosynthesis: From Light to Biosphere (P. Mathis, ed.), Vol. 4, pp. 417-420. Kluwer Academic Publishers, Dordrecht, ISBN 0-7923-3862-6.
    • (1995) Photosynthesis: from Light to Biosphere , vol.4 , pp. 417-420
    • Hurry, V.M.1
  • 56
    • 0025133235 scopus 로고
    • Dicyclohexylcarbodiimide binding proteins related to the short circuit of the proton-pumping activity of photosystem II
    • Jahns, P. & Junge, W 1990. Dicyclohexylcarbodiimide binding proteins related to the short circuit of the proton-pumping activity of photosystem II. - Eur. J. Biochem. 193: 731-736.
    • (1990) Eur. J. Biochem. , vol.193 , pp. 731-736
    • Jahns, P.1    Junge, W.2
  • 57
    • 0007964786 scopus 로고
    • The photosynthetic water oxidase: Its proton pumping activity is short-circuited within the protein by DCCD
    • _, Polle, A. & Junge, W. 1988. The photosynthetic water oxidase: Its proton pumping activity is short-circuited within the protein by DCCD. - EMBO J. 7: 589-594.
    • (1988) EMBO J. , vol.7 , pp. 589-594
    • Polle, A.1    Junge, W.2
  • 58
    • 0028058268 scopus 로고
    • The light-harvesting chlorophyll a/b-binding proteins
    • Jansson, S. 1994. The light-harvesting chlorophyll a/b-binding proteins. - Biochim. Biophys. Acta 1184: 1-19.
    • (1994) Biochim. Biophys. Acta , vol.1184 , pp. 1-19
    • Jansson, S.1
  • 60
    • 1842311454 scopus 로고    scopus 로고
    • Nearest neighbour analysis of higher plant photosystem I holocomplex
    • In press
    • _, Andersen, B. & Scheller, H. V. 1997. Nearest neighbour analysis of higher plant photosystem I holocomplex. - Plant Physiol. (In press).
    • (1997) Plant Physiol.
    • Andersen, B.1    Scheller, H.V.2
  • 61
    • 0025318977 scopus 로고
    • Excitation energy transfer from the chlorophyll spectral forms to photosystem II reaction centres: A fluorescence induction study
    • Jennings, R. C., Zucchelli, G. & Garlaschi, F. M. 1990. Excitation energy transfer from the chlorophyll spectral forms to photosystem II reaction centres: A fluorescence induction study. - Biochim. Biophys. Acta 1016: 259-265.
    • (1990) Biochim. Biophys. Acta , vol.1016 , pp. 259-265
    • Jennings, R.C.1    Zucchelli, G.2    Garlaschi, F.M.3
  • 62
    • 0027231960 scopus 로고
    • Distribution of the chlorophyll spectral forms in the chlorophyll-protein complexes of photosystem II antenna
    • _, Bassi, R., Garlaschi, F. M., Dainese, P. & Zucchelli, G. 1993. Distribution of the chlorophyll spectral forms in the chlorophyll-protein complexes of photosystem II antenna. -Biochemistry 32: 3203-3210.
    • (1993) Biochemistry , vol.32 , pp. 3203-3210
    • Bassi, R.1    Garlaschi, F.M.2    Dainese, P.3    Zucchelli, G.4
  • 64
    • 0001722176 scopus 로고
    • ΔpH-dependent chlorophyll fluorescence quenching indicating a mechanism of protection against photoinhibition of chloroplasts
    • Krause, G. H. & Behrendt, U. 1986. ΔpH-dependent chlorophyll fluorescence quenching indicating a mechanism of protection against photoinhibition of chloroplasts. - FEBS Lett. 200: 298-302.
    • (1986) FEBS Lett. , vol.200 , pp. 298-302
    • Krause, G.H.1    Behrendt, U.2
  • 65
    • 84944509463 scopus 로고
    • Energy-dependent chlorophyll fluorescence quenching in chloroplasts correlates with quantum yield of photosynthesis
    • _ & Laasch, H. 1987. Energy-dependent chlorophyll fluorescence quenching in chloroplasts correlates with quantum yield of photosynthesis. - Z. Naturforsch. 42c: 582-584.
    • (1987) Z. Naturforsch. , vol.42 C , pp. 582-584
    • Laasch, H.1
  • 66
    • 0028147508 scopus 로고
    • Atomic model of plant light-harvesting complex by electron crystallography
    • Kühlbrandt, W., Wang, D. N. & Fujiyoshi, Y. 1994. Atomic model of plant light-harvesting complex by electron crystallography. - Nature 367: 614-621.
    • (1994) Nature , vol.367 , pp. 614-621
    • Kühlbrandt, W.1    Wang, D.N.2    Fujiyoshi, Y.3
  • 67
    • 0029852006 scopus 로고    scopus 로고
    • The C-terminal domain of light-harvesting chlorophyll-a/b-binding protein is involved in the stabilisation of trimeric light-harvesting complex
    • Kuttkat, A., Hartmann, A., Hobe, S. & Paulsen, H. 1996. The C-terminal domain of light-harvesting chlorophyll-a/b-binding protein is involved in the stabilisation of trimeric light-harvesting complex. - Eur. J. Biochem. 242: 288-292.
    • (1996) Eur. J. Biochem. , vol.242 , pp. 288-292
    • Kuttkat, A.1    Hartmann, A.2    Hobe, S.3    Paulsen, H.4
  • 68
    • 0000549133 scopus 로고
    • Photosynthetic control, 'energy dependent' quenching of chlorophyll fluorescence and photophosphorylation under influence of tertiary amine
    • Laasch, H. & Weis, E. 1989. Photosynthetic control, 'energy dependent' quenching of chlorophyll fluorescence and photophosphorylation under influence of tertiary amine. - Photosynth. Res. 22: 137-146.
    • (1989) Photosynth. Res. , vol.22 , pp. 137-146
    • Laasch, H.1    Weis, E.2
  • 69
    • 0025895060 scopus 로고
    • Coregulation of a gene homologous to early light-induced genes in higher plants and beta-carotene biosynthesis in the alga Dunaliella bardawii
    • Lers, A., Levy, H. & Zamir, A. 1991. Coregulation of a gene homologous to early light-induced genes in higher plants and beta-carotene biosynthesis in the alga Dunaliella bardawii. -J. Biol. Chem. 266: 13698-13705.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13698-13705
    • Lers, A.1    Levy, H.2    Zamir, A.3
  • 70
    • 0028999894 scopus 로고
    • Regulation by redoxpoise in chloroplasts
    • Levings, C. S. III & Siedow, J. N 1995. Regulation by redoxpoise in chloroplasts. - Science 268: 695-696.
    • (1995) Science , vol.268 , pp. 695-696
    • Levings III, C.S.1    Siedow, J.N.2
  • 71
    • 0027169050 scopus 로고
    • Formation and characterization of two-dimensional crystal of photosystem II
    • Lyon, M. K., Marr, K. M. & Furcinitti, P. S. 1993. Formation and characterization of two-dimensional crystal of photosystem II. - J. Struct. Biol. 110: 133-140.
    • (1993) J. Struct. Biol. , vol.110 , pp. 133-140
    • Lyon, M.K.1    Marr, K.M.2    Furcinitti, P.S.3
  • 72
    • 0018782257 scopus 로고
    • Resolution of the light-harvesting chlorophyll a/b protein of Vicia faba chloroplasts into different chlorophyll-protein complexes
    • Machold, O. & Meister, A. 1979. Resolution of the light-harvesting chlorophyll a/b protein of Vicia faba chloroplasts into different chlorophyll-protein complexes. - Biochim. Biophys. Acta 546: 472-480.
    • (1979) Biochim. Biophys. Acta , vol.546 , pp. 472-480
    • Machold, O.1    Meister, A.2
  • 73
    • 0031403568 scopus 로고    scopus 로고
    • Cold-resistant and cold-sensitive maize lines differ in the phosphorylation of the photosystem II subunit CP29
    • In press
    • Mauro, S., Dainese, P., Lannoy, R. & Bassi, R. 1997. Cold-resistant and cold-sensitive maize lines differ in the phosphorylation of the photosystem II subunit CP29. - Plant Physiol. (In press).
    • (1997) Plant Physiol.
    • Mauro, S.1    Dainese, P.2    Lannoy, R.3    Bassi, R.4
  • 74
    • 0000116657 scopus 로고
    • Structural and functional organisation of the photosystems in spinach chloroplasts: Antenna size, relative electron transport capacity and chlorophyll composition
    • Melis, A. & Andersson, J. M. 1983. Structural and functional organisation of the photosystems in spinach chloroplasts: Antenna size, relative electron transport capacity and chlorophyll composition. - Biochim. Biophys. Acta 724: 473-484.
    • (1983) Biochim. Biophys. Acta , vol.724 , pp. 473-484
    • Melis, A.1    Andersson, J.M.2
  • 76
    • 0000761598 scopus 로고
    • Mechanism of nonphotochemical chlorophyll fluorescence quenching. I. the role of de-epoxidized xanthophylls and sequestered thylakoid membrane protons as probed by dibucaine
    • Mohanty, N. & Yamamoto, H. Y. 1995. Mechanism of nonphotochemical chlorophyll fluorescence quenching. I. The role of de-epoxidized xanthophylls and sequestered thylakoid membrane protons as probed by dibucaine. - Aust. J. Plant Physiol. 22: 231-238.
    • (1995) Aust. J. Plant Physiol. , vol.22 , pp. 231-238
    • Mohanty, N.1    Yamamoto, H.Y.2
  • 78
    • 0027788078 scopus 로고
    • Modulation of ΔpH-dependent nonphotochemical quenching of chlorophyll fluorescence in spinach chloroplasts
    • Noctor, G., Ruban, A. V. & Horton, P. 1993. Modulation of ΔpH-dependent nonphotochemical quenching of chlorophyll fluorescence in spinach chloroplasts. - Biochim. Biophys. Acta 1183: 339-344.
    • (1993) Biochim. Biophys. Acta , vol.1183 , pp. 339-344
    • Noctor, G.1    Ruban, A.V.2    Horton, P.3
  • 79
    • 0027452052 scopus 로고
    • Lipid-protein interaction in crystals of plant light-harvesting complex
    • Nussberger, S., Dorr, K., Wang, D. N. & Kühlbrandt, W. 1993. Lipid-protein interaction in crystals of plant light-harvesting complex. - J. Mol. Biol. 234: 347-356.
    • (1993) J. Mol. Biol. , vol.234 , pp. 347-356
    • Nussberger, S.1    Dorr, K.2    Wang, D.N.3    Kühlbrandt, W.4
  • 80
    • 0002062355 scopus 로고
    • Excitation energy transfer between chlorophylls and carotenoids. A proposed molecular mechanism for non-photochemical quenching
    • N. R. Baker and J. R. Bowyer, eds. Bios Scientific Publishers, Oxford. ISBN 1-872748-03-1
    • Owens, T. G. 1994. Excitation energy transfer between chlorophylls and carotenoids. A proposed molecular mechanism for non-photochemical quenching. - In Photoinhibition of Photosynthesis (N. R. Baker and J. R. Bowyer, eds), pp. 95-109. Bios Scientific Publishers, Oxford. ISBN 1-872748-03-1.
    • (1994) Photoinhibition of Photosynthesis , pp. 95-109
    • Owens, T.G.1
  • 81
    • 0028796714 scopus 로고
    • Chlorophyll a/b-binding proteins
    • Paulsen, H. 1995. Chlorophyll a/b-binding proteins. - Photo- chem. Photobiol. 62: 367-382.
    • (1995) Photo- Chem. Photobiol. , vol.62 , pp. 367-382
    • Paulsen, H.1
  • 82
    • 0001456147 scopus 로고
    • Reconstitution of pigment-containing complexes from light-harvesting chlorophyll a/b-binding protein overexpressed in Escherichia coli
    • _, Rümler, U. & Rüdiger W. 1990. Reconstitution of pigment-containing complexes from light-harvesting chlorophyll a/b-binding protein overexpressed in Escherichia coli. - Planta 181: 204-211.
    • (1990) Planta , vol.181 , pp. 204-211
    • Rümler, U.1    Rüdiger, W.2
  • 83
    • 0031041572 scopus 로고    scopus 로고
    • A single point mutation (E166Q) prevents dicychlohexylcarbodiimide binding to the photosystem II subunit CP29
    • Pesaresi, P., Sandonà, D., Giuffra, E. & Bassi, R. 1997. A single point mutation (E166Q) prevents dicychlohexylcarbodiimide binding to the photosystem II subunit CP29. - FEBS Lett. 402: 151-156.
    • (1997) FEBS Lett. , vol.402 , pp. 151-156
    • Pesaresi, P.1    Sandonà, D.2    Giuffra, E.3    Bassi, R.4
  • 84
    • 0026056608 scopus 로고
    • Biochemical composition and organisation of higher plant photosystem II light harvesting pigment-proteins
    • Peter, G. F. & Thornber, J. P. 1991. Biochemical composition and organisation of higher plant photosystem II light harvesting pigment-proteins. - J. Biol. Chem. 266: 16745-16754.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16745-16754
    • Peter, G.F.1    Thornber, J.P.2
  • 85
    • 0000784913 scopus 로고    scopus 로고
    • The light-harvesting chlorophyll a/b binding polypeptides and their genes in angiosperm and gymnosperm species
    • D. R. Ort and C. F. Yokum, eds. Kluwer Academic Publishers, Dordrecht
    • Pichersky, E. & Jansson, S. 1996. The light-harvesting chlorophyll a/b binding polypeptides and their genes in angiosperm and gymnosperm species - In Oxygenic Photosyntesis: The Light Reactions (D. R. Ort and C. F. Yokum, eds), pp. 507-521. Kluwer Academic Publishers, Dordrecht
    • (1996) Oxygenic Photosyntesis: the Light Reactions , pp. 507-521
    • Pichersky, E.1    Jansson, S.2
  • 86
    • 0000683917 scopus 로고
    • Reconstitution of chlorophyll a/b light harvesting complexes: Xanthophyll-dependent assembly and energy transfer
    • Plumley, F. G. & Schmidt, G. W. 1987. Reconstitution of chlorophyll a/b light harvesting complexes: Xanthophyll-dependent assembly and energy transfer. - Proc. Natl. Acad. Sci. USA 84: 146-150.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 146-150
    • Plumley, F.G.1    Schmidt, G.W.2
  • 87
    • 0027215344 scopus 로고
    • Effect of light stress on the expression of early light-inducible proteins in barley
    • Potter, E. & Kloppstech, K. 1993. Effect of light stress on the expression of early light-inducible proteins in barley. - Eur. J. Biochem. 214: 779-786.
    • (1993) Eur. J. Biochem. , vol.214 , pp. 779-786
    • Potter, E.1    Kloppstech, K.2
  • 88
    • 0029670313 scopus 로고    scopus 로고
    • How does photosystem 2 split water? the structural basis of efficient energy conversion
    • Rögner, M., Boekema, E. J. & Barber, J. 1996. How does photosystem 2 split water? The structural basis of efficient energy conversion. - Trends Biochem. Sci. 21: 44-49.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 44-49
    • Rögner, M.1    Boekema, E.J.2    Barber, J.3
  • 89
    • 0026801332 scopus 로고
    • The molecular mechanism of the control of excitation energy dissipation in chloroplast membranes. Inhibition of ΔpH-dependent quenching of chlorophyll fluorescence by dicyclohexylcarbodiimide
    • Ruban, A. V., Walters, R. G. & Horton, P. 1992. The molecular mechanism of the control of excitation energy dissipation in chloroplast membranes. Inhibition of ΔpH-dependent quenching of chlorophyll fluorescence by dicyclohexylcarbodiimide. - FEBS Lett. 309: 175-179.
    • (1992) FEBS Lett. , vol.309 , pp. 175-179
    • Ruban, A.V.1    Walters, R.G.2    Horton, P.3
  • 90
    • 0028005184 scopus 로고
    • The effect of illumination on the xantophyll composition of the photosystem II light harvesting complexes of spinach thylakoid membranes
    • _, Young, A. J., Pascal, A. A. & Horton, P. 1994. The effect of illumination on the xantophyll composition of the photosystem II light harvesting complexes of spinach thylakoid membranes. - Plant Physiol. 104: 227-234.
    • (1994) Plant Physiol. , vol.104 , pp. 227-234
    • Young, A.J.1    Pascal, A.A.2    Horton, P.3
  • 91
    • 0028346592 scopus 로고
    • Three dimensional structure of the higher-plant photosystem II reaction centre and evidence for its dimeric organization in vivo
    • Santini, C., Tidu, V., Tognon, G., Ghiretti Magaldi, A. & Bassi, R. 1994. Three dimensional structure of the higher-plant photosystem II reaction centre and evidence for its dimeric organization in vivo. - Eur. J. Biochem. 221: 307-315.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 307-315
    • Santini, C.1    Tidu, V.2    Tognon, G.3    Ghiretti Magaldi, A.4    Bassi, R.5
  • 92
    • 0016424772 scopus 로고
    • Light-induced deepoxidation of violaxanthin in lettuce chloroplasts. IV. the effects of electron-transport conditions on violaxanthin availability
    • Siefermann, D. & Yamamoto, H. Y. 1975. Light-induced deepoxidation of violaxanthin in lettuce chloroplasts. IV. The effects of electron-transport conditions on violaxanthin availability. - Biochem. Biophys. Res. Commun. 62: 456-461.
    • (1975) Biochem. Biophys. Res. Commun. , vol.62 , pp. 456-461
    • Siefermann, D.1    Yamamoto, H.Y.2
  • 93
    • 0027423711 scopus 로고
    • Redox titration of multiple protein phosphorylations in pea chloroplast thylakoids
    • Silverstein, T., Cheng, L. & Allen, J. F. 1993. Redox titration of multiple protein phosphorylations in pea chloroplast thylakoids. - Biochim. Biophys. Acta 1183: 215-220.
    • (1993) Biochim. Biophys. Acta , vol.1183 , pp. 215-220
    • Silverstein, T.1    Cheng, L.2    Allen, J.F.3
  • 94
    • 0030590883 scopus 로고    scopus 로고
    • A 'CK2' site is reversibly phosphorylated in the PSII subunit CP29
    • Testi, M. G., Croce, R., Polverino de Laureto, P. & Bassi, R. 1996. A 'CK2' site is reversibly phosphorylated in the PSII subunit CP29. - FEBS Lett. 399: 245-250.
    • (1996) FEBS Lett. , vol.399 , pp. 245-250
    • Testi, M.G.1    Croce, R.2    Polverino De Laureto, P.3    Bassi, R.4
  • 95
    • 0014051710 scopus 로고
    • Studies on the nature of the chloroplast lamella. I. Preparation and some properties of two chlorophyll-protein complexes
    • Thornber, J. P., Gregory, R. P. F., Smith, C. A. & Bailey, J. L. 1967. Studies on the nature of the chloroplast lamella. I. Preparation and some properties of two chlorophyll-protein complexes. - Biochemistry 6: 391-396.
    • (1967) Biochemistry , vol.6 , pp. 391-396
    • Thornber, J.P.1    Gregory, R.P.F.2    Smith, C.A.3    Bailey, J.L.4
  • 96
    • 0002214359 scopus 로고
    • Lipid composition of chlorophyll-protein complexes: Specific enrichment in trans-hexadecenoic acid of an oligomeric form of light harvesting chlorophyll a/b protein
    • Tremolieres, A., Dubacq, J. P., Ambard-Bretteville, F. & Remy, R. 1981. Lipid composition of chlorophyll-protein complexes: Specific enrichment in trans-hexadecenoic acid of an oligomeric form of light harvesting chlorophyll a/b protein. - FEBS Lett. 130: 27-31.
    • (1981) FEBS Lett. , vol.130 , pp. 27-31
    • Tremolieres, A.1    Dubacq, J.P.2    Ambard-Bretteville, F.3    Remy, R.4
  • 98
    • 0000476702 scopus 로고
    • DCCD binds to lumen-exposed glutamate residues in LHCIIc
    • P. Mathis, ed. Kluwer Academic Publishers, Dordrecht. ISBN 0-7923-3862-6
    • Walters, R. G. & Horton, P. 1995. DCCD binds to lumen-exposed glutamate residues in LHCIIc. - In Photosynthesis: From Light to Biosphere (P. Mathis, ed.), Vol. 1, pp. 299-302. Kluwer Academic Publishers, Dordrecht. ISBN 0-7923-3862-6.
    • (1995) Photosynthesis: from Light to Biosphere , vol.1 , pp. 299-302
    • Walters, R.G.1    Horton, P.2
  • 99
    • 0028606092 scopus 로고
    • Higher plant light-harvesting complexes LHCIIa and LHCIIc are bound by dicyclohexylcarbodiimide during inhibition of energy dissipation
    • _, Ruban, A. V. & Horton, P. 1994. Higher plant light-harvesting complexes LHCIIa and LHCIIc are bound by dicyclohexylcarbodiimide during inhibition of energy dissipation. -Eur. J. Biochem. 226: 1063-1069.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 1063-1069
    • Ruban, A.V.1    Horton, P.2
  • 100
    • 0030462465 scopus 로고    scopus 로고
    • Identification of proton-active residues in a higher plant light harvesting complex
    • _, Ruban, A. V. & Horton, P. 1996. Identification of proton-active residues in a higher plant light harvesting complex. - Proc. Natl. Acad. Sci. USA 93: 14204-14209.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14204-14209
    • Ruban, A.V.1    Horton, P.2
  • 101
    • 0026635621 scopus 로고
    • Involvement of a chloroplast Hps70 heat shock protein in the integration of a protein (light-harvesting complex protein precursor) into the thylakoid membrane
    • Yalowsky, S., Paulsen, H., Michaeli, D., Chitnis, P. R. & Nechushtai, R. 1992. Involvement of a chloroplast Hps70 heat shock protein in the integration of a protein (light-harvesting complex protein precursor) into the thylakoid membrane. -Proc. Natl. Acad. Sci. USA 89: 5616-5619.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5616-5619
    • Yalowsky, S.1    Paulsen, H.2    Michaeli, D.3    Chitnis, P.R.4    Nechushtai, R.5
  • 102
    • 0000882260 scopus 로고    scopus 로고
    • Carotenoids: Localisation and function
    • D. R. Ort and C. F. Yokum, eds. Kluwer Academic Publishers, Dordrecht
    • Yamamoto, H. & Bassi, R. 1996. Carotenoids: Localisation and function - In Oxygenic Photosyntesis: The Light Reactions (D. R. Ort and C. F. Yokum, eds), pp. 539-563. Kluwer Academic Publishers, Dordrecht.
    • (1996) Oxygenic Photosyntesis: the Light Reactions , pp. 539-563
    • Yamamoto, H.1    Bassi, R.2
  • 103
    • 0002968987 scopus 로고
    • Effect of chloroplast lipids on violaxanthin de-epoxidase activity
    • M. Avron, ed. Elsevier, Amsterdam
    • _, Chenchin, E. & Yamada, D. K. 1974. Effect of chloroplast lipids on violaxanthin de-epoxidase activity. - In Proceedings of the 3rd International Congress on Photosynhesis (M. Avron, ed.), Vol. III, pp. 1999-2006. Elsevier, Amsterdam.
    • (1974) Proceedings of the 3rd International Congress on Photosynhesis , vol.3 , pp. 1999-2006
    • Chenchin, E.1    Yamada, D.K.2
  • 104
    • 0026594337 scopus 로고
    • Independent fluorescence emission of the chlorophyll spectral forms in higher plants photosystem II
    • Zucchelli, G., Jennings, R. C. & Garlaschi, F. M. 1992. Independent fluorescence emission of the chlorophyll spectral forms in higher plants photosystem II. - Biochim. Biophys. Acta 1099: 163-169.
    • (1992) Biochim. Biophys. Acta , vol.1099 , pp. 163-169
    • Zucchelli, G.1    Jennings, R.C.2    Garlaschi, F.M.3
  • 105
    • 0027994396 scopus 로고
    • Gaussian decomposition of absorption and linear dichroism spectra of outer antenna complexes of photosystem II
    • _, Dainese, P., Jennings, R. C., Breton, J., Garlaschi, F. M. & Bassi, R. 1994. Gaussian decomposition of absorption and linear dichroism spectra of outer antenna complexes of photosystem II. - Biochemistry 33: 8982-8990.
    • (1994) Biochemistry , vol.33 , pp. 8982-8990
    • Dainese, P.1    Jennings, R.C.2    Breton, J.3    Garlaschi, F.M.4    Bassi, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.