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Volumn 43, Issue 26, 2004, Pages 8281-8289

Toward an understanding of the mechanism of nonphotochemical quenching in green plants

Author keywords

[No Author keywords available]

Indexed keywords

BYPRODUCTS; CHLOROPHYLL; PHOTOSYNTHESIS; PLANTS (BOTANY); QUENCHING;

EID: 3142546273     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0494020     Document Type: Review
Times cited : (277)

References (76)
  • 1
    • 0037025137 scopus 로고    scopus 로고
    • Rapid regulation of light harvesting and plant fitness in the field
    • Külheim, C., Ågren, J., and Jansson, S. (2002) Rapid regulation of light harvesting and plant fitness in the field, Science 297, 91-93.
    • (2002) Science , vol.297 , pp. 91-93
    • Külheim, C.1    Ågren, J.2    Jansson, S.3
  • 2
    • 0026547142 scopus 로고
    • Too much of a good thing: Light can be bad for photosynthesis
    • Barber, J., and Andersson, B. (1992) Too much of a good thing: light can be bad for photosynthesis, Trends Biochem. Sci. 17, 61-66.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 61-66
    • Barber, J.1    Andersson, B.2
  • 3
    • 0033506468 scopus 로고    scopus 로고
    • Photoprotection revisited: Genetic and molecular approaches
    • Niyogi, K. K. (1999) Photoprotection revisited: genetic and molecular approaches, Annu. Rev. Plant Physiol. Plant Mol. Biol. 50, 333-359.
    • (1999) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.50 , pp. 333-359
    • Niyogi, K.K.1
  • 4
    • 0000873146 scopus 로고
    • Studies on the induction of chlorophyll fluorescence in isolated barley protoplasts. IV. Resolution of non-photochemical quenching
    • Horton, P., and Hague, A. (1988) Studies on the induction of chlorophyll fluorescence in isolated barley protoplasts. IV. Resolution of non-photochemical quenching, Biochim. Biophys. Acta 932, 107-115.
    • (1988) Biochim. Biophys. Acta , vol.932 , pp. 107-115
    • Horton, P.1    Hague, A.2
  • 5
    • 0035028317 scopus 로고    scopus 로고
    • Non-photochemical quenching. A response to excess light energy
    • Müller, P., Li, X.-P., and Niyogi, K. K. (2001) Non-photochemical quenching. A response to excess light energy, Plant Physiol. 125, 1558-1566.
    • (2001) Plant Physiol. , vol.125 , pp. 1558-1566
    • Müller, P.1    Li, X.-P.2    Niyogi, K.K.3
  • 6
    • 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
  • 7
    • 0037069468 scopus 로고    scopus 로고
    • PsbS-dependent enhancement of feedback de-excitation protects photosystem II from photoinhibition
    • Li, X.-P., Müller-Moulé, P., Gilmore, A. M., and Niyogi, K. K. (2002) PsbS-dependent enhancement of feedback de-excitation protects photosystem II from photoinhibition, Proc. Natl. Acad. Sci. U.S.A. 99, 15222-15227.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 15222-15227
    • Li, X.-P.1    Müller-Moulé, P.2    Gilmore, A.M.3    Niyogi, K.K.4
  • 8
    • 0028953463 scopus 로고
    • Xanthophyll cycle-dependent quenching of photosystem II chlorophyll a fluorescence: Formation of a quenching complex with a short fluorescence lifetime
    • Gilmore, A. M., Hazlett, T. L., and Govindjee (1995) Xanthophyll cycle-dependent quenching of photosystem II chlorophyll a fluorescence: formation of a quenching complex with a short fluorescence lifetime, Proc. Natl. Acad. Sci. U.S.A. 92, 2273-2277.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 2273-2277
    • Gilmore, A.M.1    Hazlett, T.L.2    Govindjee3
  • 9
    • 0033587751 scopus 로고    scopus 로고
    • The violaxanthin cycle protects plants from photooxidative damage by more than one mechanism
    • Havaux, M., and Niyogi, K. K. (1999) The violaxanthin cycle protects plants from photooxidative damage by more than one mechanism, Proc. Natl. Acad. Sci. U.S.A. 96, 8762-8767.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 8762-8767
    • Havaux, M.1    Niyogi, K.K.2
  • 10
    • 0030498562 scopus 로고    scopus 로고
    • Using chlorophyll fluorescence to assess the fraction of absorbed light allocated to thermal dissipation of excess excitation
    • Demmig-Adams, B., Adams, W. W., III, Barker, D. H., Logan, B. A., Bowling, D. R., and Verhoeven, A. S. (1996) Using chlorophyll fluorescence to assess the fraction of absorbed light allocated to thermal dissipation of excess excitation, Physiol. Plant. 98, 253-264.
    • (1996) Physiol. Plant. , vol.98 , pp. 253-264
    • Demmig-Adams, B.1    Adams III, W.W.2    Barker, D.H.3    Logan, B.A.4    Bowling, D.R.5    Verhoeven, A.S.6
  • 11
    • 0034467207 scopus 로고    scopus 로고
    • Lhc proteins and the regulation of photosynthetic light harvesting function by xanthophylls
    • Bassi, R., and Caffarri, S. (2000) Lhc proteins and the regulation of photosynthetic light harvesting function by xanthophylls, Photosynth. Res. 64, 243-256.
    • (2000) Photosynth. Res. , vol.64 , pp. 243-256
    • Bassi, R.1    Caffarri, S.2
  • 12
    • 0343851071 scopus 로고    scopus 로고
    • A pigment-binding protein essential for regulation of photosynthetic light harvesting
    • Li, X.-P., Björkman, O., Shih, C., Grossman, A. R., Rosenquist, M., Jansson, S., and Niyogi, K. K. (2000) A pigment-binding protein essential for regulation of photosynthetic light harvesting, Nature 403, 391-395.
    • (2000) Nature , vol.403 , pp. 391-395
    • Li, X.-P.1    Björkman, O.2    Shih, C.3    Grossman, A.R.4    Rosenquist, M.5    Jansson, S.6    Niyogi, K.K.7
  • 13
  • 14
    • 0001938338 scopus 로고    scopus 로고
    • The role of xanthophyll cycle carotenoids in the protection of photosynthesis
    • Demmig-Adams, B., and Adams, W. W., III (1996) The role of xanthophyll cycle carotenoids in the protection of photosynthesis, Trends Plant Sci. 1, 21-26.
    • (1996) Trends Plant Sci. , vol.1 , pp. 21-26
    • Demmig-Adams, B.1    Adams III, W.W.2
  • 15
    • 0030995292 scopus 로고    scopus 로고
    • Mechanistic aspects of xanthophyll cycle-dependent photoprotection in higher plant chloroplasts and leaves
    • Gilmore, A. M. (1997) Mechanistic aspects of xanthophyll cycle-dependent photoprotection in higher plant chloroplasts and leaves, Physiol. Plant. 99, 197-209.
    • (1997) Physiol. Plant. , vol.99 , pp. 197-209
    • Gilmore, A.M.1
  • 16
    • 0022759515 scopus 로고
    • Isolation and characterization of the 10 kDa and 22 kDa polypeptides of higher-plant photosystem 2
    • Ljungberg, U., Akerlund, H. E., and Andersson, B. (1986) Isolation and characterization of the 10 kDa and 22 kDa polypeptides of higher-plant photosystem 2, Eur. J. Biochem. 158, 477-482.
    • (1986) Eur. J. Biochem. , vol.158 , pp. 477-482
    • Ljungberg, U.1    Akerlund, H.E.2    Andersson, B.3
  • 19
    • 0026545775 scopus 로고
    • The single-copy gene psbS codes for a phylogenetically intriguing 22 kDa polypeptide of photosystem II
    • Wedel, N., Klein, R., Ljungberg, U., Andersson, B., and Herrmann, R. G. (1992) The single-copy gene psbS codes for a phylogenetically intriguing 22 kDa polypeptide of photosystem II, FEBS Lett. 314, 61-66.
    • (1992) FEBS Lett. , vol.314 , pp. 61-66
    • Wedel, N.1    Klein, R.2    Ljungberg, U.3    Andersson, B.4    Herrmann, R.G.5
  • 22
    • 0033584940 scopus 로고    scopus 로고
    • Chlorophyll binding to monomeric light-harvesting complex. A mutation analysis of chromophore-binding residues
    • Remelli, R., Varotto, C., Sandoná, D., Croce, R., and Bassi, R. (1999) Chlorophyll binding to monomeric light-harvesting complex. A mutation analysis of chromophore-binding residues, J. Biol. Chem. 274, 33510-33521.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33510-33521
    • Remelli, R.1    Varotto, C.2    Sandoná, D.3    Croce, R.4    Bassi, R.5
  • 23
    • 0033621082 scopus 로고    scopus 로고
    • Mutational analysis of a higher plant antenna protein provides identification of chromophores bound in multiple sites
    • Bassi, R., Croce, R., Cugini, D., and Sandoná, D. (1999) Mutational analysis of a higher plant antenna protein provides identification of chromophores bound in multiple sites, Proc. Natl. Acad. Sci. U.S.A. 96, 10056-10061.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 10056-10061
    • Bassi, R.1    Croce, R.2    Cugini, D.3    Sandoná, D.4
  • 24
    • 0037151045 scopus 로고    scopus 로고
    • Biochemical properties of the PsbS subunit of photosystem II either purified from chloroplast or recombinant
    • Dominici, P., Caffarri, S., Armenante, F., Ceoldo, S., Crimi, M., and Bassi, R. (2002) Biochemical properties of the PsbS subunit of photosystem II either purified from chloroplast or recombinant, J. Biol. Chem. 277, 22750-22758.
    • (2002) J. Biol. Chem. , vol.277 , pp. 22750-22758
    • Dominici, P.1    Caffarri, S.2    Armenante, F.3    Ceoldo, S.4    Crimi, M.5    Bassi, R.6
  • 25
    • 0037058975 scopus 로고    scopus 로고
    • In vitro reconstitution of the activated zeaxanthin state associated with energy dissipation in plants
    • Aspinall-O'Dea, M., Wentworth, M., Pascal, A., Robert, B., Ruban, A., and Horton, P. (2002) In vitro reconstitution of the activated zeaxanthin state associated with energy dissipation in plants, Proc. Natl. Acad. Sci. U.S.A. 99, 16331-16335.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 16331-16335
    • Aspinall-O'Dea, M.1    Wentworth, M.2    Pascal, A.3    Robert, B.4    Ruban, A.5    Horton, P.6
  • 26
    • 0037040876 scopus 로고    scopus 로고
    • Activation of zeaxanthin is an obligatory event in the regulation of photosynthetic light harvesting
    • Ruban, A. V., Pascal, A. A., Robert, B., and Horton, P. (2002) Activation of zeaxanthin is an obligatory event in the regulation of photosynthetic light harvesting, J. Biol. Chem. 277, 7785-7789.
    • (2002) J. Biol. Chem. , vol.277 , pp. 7785-7789
    • Ruban, A.V.1    Pascal, A.A.2    Robert, B.3    Horton, P.4
  • 27
    • 0026801332 scopus 로고
    • The molecular mechanism of the control of excitation energy dissipation in chloroplast membranes. Inhibition of pH-dependent quenching of chlorophyll fluorescence by dicyclohexylcarbodiimide
    • Ruban, A. V., Walters, R. G., and Horton, P. (1992) The molecular mechanism of the control of excitation energy dissipation in chloroplast membranes. Inhibition of pH-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
  • 29
    • 2542444370 scopus 로고    scopus 로고
    • Regulation of photosynthetic light harvesting involves intrathylakoid lumen pH sensing by the PsbS protein
    • Li, X.-P., Gilmore, A. M., Caffarri, S., Bassi, R., Golan, T., Kramer, D., and Niyogi, K. K. (2004) Regulation of photosynthetic light harvesting involves intrathylakoid lumen pH sensing by the PsbS protein, J. Biol. Chem. 279, 22866-22874.
    • (2004) J. Biol. Chem. , vol.279 , pp. 22866-22874
    • Li, X.-P.1    Gilmore, A.M.2    Caffarri, S.3    Bassi, R.4    Golan, T.5    Kramer, D.6    Niyogi, K.K.7
  • 30
    • 0036030182 scopus 로고    scopus 로고
    • Structure-function analysis of photosystem II subunit S (PsbS) in vivo
    • Li, X.-P., Phippard, A., Pasari, J., and Niyogi, K. K. (2002) Structure-function analysis of photosystem II subunit S (PsbS) in vivo, Funct. Plant Biol. 29, 1131-1139.
    • (2002) Funct. Plant Biol. , vol.29 , pp. 1131-1139
    • Li, X.-P.1    Phippard, A.2    Pasari, J.3    Niyogi, K.K.4
  • 31
    • 0033012091 scopus 로고    scopus 로고
    • A guide to the Lhc genes and their relatives in Arabidopsis
    • Jansson, S. (1999) A guide to the Lhc genes and their relatives in Arabidopsis, Trends Plant Sci. 4, 236-240.
    • (1999) Trends Plant Sci. , vol.4 , pp. 236-240
    • Jansson, S.1
  • 32
    • 0028574188 scopus 로고
    • Topological studies of spinach 22 kDa protein of photosystem II
    • Kim, S., Pichersky, E., and Yocum, C. F. (1994) Topological studies of spinach 22 kDa protein of photosystem II, Biochim. Biophys. Acta 1188, 339-348.
    • (1994) Biochim. Biophys. Acta , vol.1188 , pp. 339-348
    • Kim, S.1    Pichersky, E.2    Yocum, C.F.3
  • 33
    • 0034730964 scopus 로고    scopus 로고
    • Supermolecular structure of photosystem II and location of the PsbS protein
    • Nield, J., Funk, C., and Barber, J. (2000) Supermolecular structure of photosystem II and location of the PsbS protein, Philos. Trans. R. Soc. London, Ser. B 355, 1337-1344.
    • (2000) Philos. Trans. R. Soc. London, Ser. B , vol.355 , pp. 1337-1344
    • Nield, J.1    Funk, C.2    Barber, J.3
  • 34
    • 0031028204 scopus 로고    scopus 로고
    • Isolation and biochemical characterisation of monomeric and dimeric photosystem II complexes from spinach and their relevance to the organisation of photosystem II in vivo
    • Hankamer, B., Nield, J., Zheleva, D., Boekema, E., Jansson, S., and Barber, J. (1997) Isolation and biochemical characterisation of monomeric and dimeric photosystem II complexes from spinach and their relevance to the organisation of photosystem II in vivo, Eur. J. Biochem. 243, 422-429.
    • (1997) Eur. J. Biochem. , vol.243 , pp. 422-429
    • Hankamer, B.1    Nield, J.2    Zheleva, D.3    Boekema, E.4    Jansson, S.5    Barber, J.6
  • 35
    • 0030749012 scopus 로고    scopus 로고
    • Screening of chlorina mutants of barley (Hordeum vulgare L.) with antibodies against light-harvesting proteins of PS I and PS II: Absence of specific antenna proteins
    • Bossmann, B., Knoetzel, J., and Jansson, S. (1997) Screening of chlorina mutants of barley (Hordeum vulgare L.) with antibodies against light-harvesting proteins of PS I and PS II: absence of specific antenna proteins, Photosynth. Res. 52, 127-136.
    • (1997) Photosynth. Res. , vol.52 , pp. 127-136
    • Bossmann, B.1    Knoetzel, J.2    Jansson, S.3
  • 36
    • 0032910388 scopus 로고    scopus 로고
    • The biogenesis and assembly of photosynthetic proteins in thylakoid membranes
    • Wollman, F.-A., Minai, L., and Nechushtai, R. (1999) The biogenesis and assembly of photosynthetic proteins in thylakoid membranes, Biochim. Biophys. Acta 1411, 21-85.
    • (1999) Biochim. Biophys. Acta , vol.1411 , pp. 21-85
    • Wollman, F.-A.1    Minai, L.2    Nechushtai, R.3
  • 37
    • 0037181144 scopus 로고    scopus 로고
    • Novel approach reveals localisation and assembly pathway of the PsbS and PsbW proteins into the photosystem II dimer
    • Thidholm, E., Lindström, V., Tisser, C., Robinson, C., Schröder, W. P., and Funk, C. (2002) Novel approach reveals localisation and assembly pathway of the PsbS and PsbW proteins into the photosystem II dimer, FEBS Lett. 513, 217-222.
    • (2002) FEBS Lett. , vol.513 , pp. 217-222
    • Thidholm, E.1    Lindström, V.2    Tisser, C.3    Robinson, C.4    Schröder, W.P.5    Funk, C.6
  • 38
    • 0035861976 scopus 로고    scopus 로고
    • Functional architecture of the major light-harvesting complex from higher plants
    • Formaggio, E., Cinque, G., and Bassi, R. (2001) Functional architecture of the major light-harvesting complex from higher plants, J. Mol. Biol. 314, 1157-1166.
    • (2001) J. Mol. Biol. , vol.314 , pp. 1157-1166
    • Formaggio, E.1    Cinque, G.2    Bassi, R.3
  • 40
    • 0028005184 scopus 로고
    • The effects of illumination on the xanthophyll composition of the photosystem II light harvesting complexes of spinach thylakoid membranes
    • Ruban, A. V., Young, A. J., Pascal, A. A., and Horton, P. (1994) The effects of illumination on the xanthophyll 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
    • Ruban, A.V.1    Young, A.J.2    Pascal, A.A.3    Horton, P.4
  • 41
    • 0035940523 scopus 로고    scopus 로고
    • Time-resolved fluorescence analysis of the photosystem II antenna proteins in detergent micelles and liposomes
    • Moya, I., Silvestri, M., Vallon, O., Cinque, G., and Bassi, R. (2001) Time-resolved fluorescence analysis of the photosystem II antenna proteins in detergent micelles and liposomes, Biochemistry 40, 12552-12561.
    • (2001) Biochemistry , vol.40 , pp. 12552-12561
    • Moya, I.1    Silvestri, M.2    Vallon, O.3    Cinque, G.4    Bassi, R.5
  • 42
    • 0026072865 scopus 로고
    • Control of the light-harvesting function of chloroplast membranes by aggregation of the LHCII chlorophyll protein complex
    • Horton, P., Ruban, A. V., Rees, D., Pascal, A. A., Noctor, G., and Young, A. J. (1991) Control of the light-harvesting function of chloroplast membranes by aggregation of the LHCII chlorophyll protein complex, FEBS Lett. 292, 1-4.
    • (1991) FEBS Lett. , vol.292 , pp. 1-4
    • Horton, P.1    Ruban, A.V.2    Rees, D.3    Pascal, A.A.4    Noctor, G.5    Young, A.J.6
  • 43
    • 0031041572 scopus 로고    scopus 로고
    • A single point mutation (E166Q) prevents dicyclohexylcarbodiimide binding to the photosystem II subunit of CP29
    • Pesaresi, P., Sandoná, D., Giuffra, E., and Bassi, R. (1997) A single point mutation (E166Q) prevents dicyclohexylcarbodiimide binding to the photosystem II subunit of CP29, FEBS Lett. 402, 151-156.
    • (1997) FEBS Lett. , vol.402 , pp. 151-156
    • Pesaresi, P.1    Sandoná, D.2    Giuffra, E.3    Bassi, R.4
  • 44
    • 0037062584 scopus 로고    scopus 로고
    • Chromophore organization in the higher-plant photosystem II antenna protein CP26
    • Croce, R., Canino, G., Ros, F., and Bassi, R. (2002) Chromophore organization in the higher-plant photosystem II antenna protein CP26, Biochemistry 41, 7334-7343.
    • (2002) Biochemistry , vol.41 , pp. 7334-7343
    • Croce, R.1    Canino, G.2    Ros, F.3    Bassi, R.4
  • 45
    • 0037020088 scopus 로고    scopus 로고
    • Dynamics of chromophore binding to Lhc proteins in vivo and in vitro during operation of the xanthophyll cycle
    • Morosinotto, T., Baronio, R., and Bassi, R. (2002) Dynamics of chromophore binding to Lhc proteins in vivo and in vitro during operation of the xanthophyll cycle, J. Biol. Chem. 277, 36913-36920.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36913-36920
    • Morosinotto, T.1    Baronio, R.2    Bassi, R.3
  • 46
    • 0035928785 scopus 로고    scopus 로고
    • Kinetic analysis of nonphotochemical quenching of chlorophyll fluorescence. 1. Isolated chloroplasts
    • Ruban, A. V., Wentworth, M., and Horton, P. (2001) Kinetic analysis of nonphotochemical quenching of chlorophyll fluorescence. 1. Isolated chloroplasts, Biochemistry 40, 9896-9901.
    • (2001) Biochemistry , vol.40 , pp. 9896-9901
    • Ruban, A.V.1    Wentworth, M.2    Horton, P.3
  • 47
    • 0035928839 scopus 로고    scopus 로고
    • Kinetic analysis of nonphotochemical quenching of chlorophyll fluorescence. 2. Isolated light-harvesting complexes
    • Wentworth, M., Ruban, A. V., and Horton, P. (2001) Kinetic analysis of nonphotochemical quenching of chlorophyll fluorescence. 2. Isolated light-harvesting complexes, Biochemistry 40, 9902-9908.
    • (2001) Biochemistry , vol.40 , pp. 9902-9908
    • Wentworth, M.1    Ruban, A.V.2    Horton, P.3
  • 48
    • 0036672384 scopus 로고    scopus 로고
    • A major light-harvesting polypeptide of photosystem II functions in thermal dissipation
    • Elrad, D., Niyogi, K. K., and Grossman, A. R. (2002) A major light-harvesting polypeptide of photosystem II functions in thermal dissipation, Plant Cell 14, 1801-1816.
    • (2002) Plant Cell , vol.14 , pp. 1801-1816
    • Elrad, D.1    Niyogi, K.K.2    Grossman, A.R.3
  • 49
    • 0027215344 scopus 로고
    • Effects of light stress on the expression of early light-inducible proteins in barley
    • Pötter, E., and Kloppstech, K. (1993) Effects 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
    • Pötter, E.1    Kloppstech, K.2
  • 50
    • 0034006740 scopus 로고    scopus 로고
    • An Arabidopsis thaliana protein homologous to cyanobacterial high-light-inducible proteins
    • Jansson, S., Andersson, J., Kim, S. J., and Jackowski, G. (2000) An Arabidopsis thaliana protein homologous to cyanobacterial high-light-inducible proteins, Plant Mol. Biol. 42, 345-351.
    • (2000) Plant Mol. Biol. , vol.42 , pp. 345-351
    • Jansson, S.1    Andersson, J.2    Kim, S.J.3    Jackowski, G.4
  • 51
    • 0027194606 scopus 로고
    • Comparison of chlorophyll fluorescence quenching in leaves of wild-type with a chlorophyll-b-less mutant of barley (Hordeum vulgare L.)
    • Lokstein, H., Härtel, H., Hoffmann, P., and Renger, G. (1993) Comparison of chlorophyll fluorescence quenching in leaves of wild-type with a chlorophyll-b-less mutant of barley (Hordeum vulgare L.), J. Photochem. Photobiol., B 19, 217-225.
    • (1993) J. Photochem. Photobiol., B , vol.19 , pp. 217-225
    • Lokstein, H.1    Härtel, H.2    Hoffmann, P.3    Renger, G.4
  • 52
    • 0028004719 scopus 로고
    • Changes in in-vivo fluorescence quenching in rye and barley as a function of reduced PSII light-harvesting antenna size
    • Falk, S., Król, M., Maxwell, D. P., Rezansoff, D. A., Gray, G. R., and Huner, N. P. A. (1994) Changes in in-vivo fluorescence quenching in rye and barley as a function of reduced PSII light-harvesting antenna size, Physiol. Plant. 91, 551-558.
    • (1994) Physiol. Plant. , vol.91 , pp. 551-558
    • Falk, S.1    Król, M.2    Maxwell, D.P.3    Rezansoff, D.A.4    Gray, G.R.5    Huner, N.P.A.6
  • 53
    • 0002063357 scopus 로고
    • Consequences of LHC-II deficiency for photosynthetic regulation in chlorina mutants of barley
    • Andrews, J. R., Fryer, M. J., and Baker, N. R. (1995) Consequences of LHC-II deficiency for photosynthetic regulation in chlorina mutants of barley, Photosynth. Res. 44, 81-91.
    • (1995) Photosynth. Res. , vol.44 , pp. 81-91
    • Andrews, J.R.1    Fryer, M.J.2    Baker, N.R.3
  • 54
    • 0029861283 scopus 로고    scopus 로고
    • Photosystem II chlorophyll a fluorescence lifetimes and intensity are independent of the antenna size differences between barley wild-type and chlorina mutants: Photochemical quenching and xanthophyll cycle-dependent nonphotochemical quenching of fluorescence
    • Gilmore, A. M., Hazlett, T. L., Debrunner, P. G., and Govindjee (1996) Photosystem II chlorophyll a fluorescence lifetimes and intensity are independent of the antenna size differences between barley wild-type and chlorina mutants: photochemical quenching and xanthophyll cycle-dependent nonphotochemical quenching of fluorescence, Photosynth. Res. 48, 171-187.
    • (1996) Photosynth. Res. , vol.48 , pp. 171-187
    • Gilmore, A.M.1    Hazlett, T.L.2    Debrunner, P.G.3    Govindjee4
  • 55
    • 0032573152 scopus 로고    scopus 로고
    • Altered xanthophyll compositions adversely affect chlorophyll accumulation and nonphotochemical quenching in Arabidopsis mutants
    • Pogson, B. J., Niyogi, K. K., Björkman, O., and DellaPenna, D. (1998) Altered xanthophyll compositions adversely affect chlorophyll accumulation and nonphotochemical quenching in Arabidopsis mutants, Proc. Natl. Acad. Sci. U.S.A. 95, 13324-13329.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 13324-13329
    • Pogson, B.J.1    Niyogi, K.K.2    Björkman, O.3    DellaPenna, D.4
  • 56
    • 0001235208 scopus 로고
    • Dynamics and mechanism of singlet energy transfer between carotenoids and chlorophylls: Light harvesting and nonphotochemical fluorescence quenching
    • (Murata, N., Ed.), Kluwer Academic, Dordrecht, The Netherlands
    • Owens, T. G., Shreve, A. P., and Albrecht, A. C. (1992) Dynamics and mechanism of singlet energy transfer between carotenoids and chlorophylls: light harvesting and nonphotochemical fluorescence quenching, in Research in Photosynthesis (Murata, N., Ed.) pp 179-186, Kluwer Academic, Dordrecht, The Netherlands.
    • (1992) Research in Photosynthesis , pp. 179-186
    • Owens, T.G.1    Shreve, A.P.2    Albrecht, A.C.3
  • 57
    • 0028156508 scopus 로고
    • Photophysics of the carotenoids associated with the xanthophyll cycle in photosynthesis
    • Frank, H. A., Cua, A., Chynwat, V., Young, A., Gosztola, D., and Wasielewski, M. R. (1994) Photophysics of the carotenoids associated with the xanthophyll cycle in photosynthesis, Photosynth. Res. 41, 389-395.
    • (1994) Photosynth. Res. , vol.41 , pp. 389-395
    • Frank, H.A.1    Cua, A.2    Chynwat, V.3    Young, A.4    Gosztola, D.5    Wasielewski, M.R.6
  • 62
    • 0001431040 scopus 로고    scopus 로고
    • Two-photon excitation spectrum of light-harvesting complex II and fluorescence upconversion after one- and two-photon excitation of the carotenoids
    • Walla, P. J., Yom, J., Krueger, B. P., and Fleming, G. R. (2000) Two-photon excitation spectrum of light-harvesting complex II and fluorescence upconversion after one- and two-photon excitation of the carotenoids, J. Phys. Chem. B 104, 4799-4806.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 4799-4806
    • Walla, P.J.1    Yom, J.2    Krueger, B.P.3    Fleming, G.R.4
  • 63
    • 0034300084 scopus 로고    scopus 로고
    • Identifying the pathways of energy transfer between carotenoids and chlorophylls in LHCII and CP29. A multicolor, femtosecond pump-probe study
    • Gradinaru, C. C., van Stokkum, I. H. M., Pascal, A. A., van Grondelle, R., and van Amerongen, H. (2000) Identifying the pathways of energy transfer between carotenoids and chlorophylls in LHCII and CP29. A multicolor, femtosecond pump-probe study, J. Phys. Chem. B 104, 9330-9342.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 9330-9342
    • Gradinaru, C.C.1    Van Stokkum, I.H.M.2    Pascal, A.A.3    Van Grondelle, R.4    Van Amerongen, H.5
  • 65
    • 0037381881 scopus 로고    scopus 로고
    • Energy transfer pathways in the minor antenna complex CP29 of photosystem II: A femtosecond study of carotenoid to chlorophyll transfer on mutant and WT complexes
    • Croce, R., Müller, M. G., Caffarri, S., Bassi, R., and Holzwarth, A. R. (2003) Energy transfer pathways in the minor antenna complex CP29 of photosystem II: a femtosecond study of carotenoid to chlorophyll transfer on mutant and WT complexes, Biophys. J. 84, 2517-2532.
    • (2003) Biophys. J. , vol.84 , pp. 2517-2532
    • Croce, R.1    Müller, M.G.2    Caffarri, S.3    Bassi, R.4    Holzwarth, A.R.5
  • 68
    • 0038718069 scopus 로고    scopus 로고
    • Charge-transfer state as a possible signature of a zeaxanthin-chlorophyll dimer in the non-photochemical quenching process in green plants
    • Dreuw, A., Fleming, G. R., and Head-Gordon, M. (2003) Charge-transfer state as a possible signature of a zeaxanthin-chlorophyll dimer in the non-photochemical quenching process in green plants, J. Phys. Chem. B 107, 6500-6503.
    • (2003) J. Phys. Chem. B , vol.107 , pp. 6500-6503
    • Dreuw, A.1    Fleming, G.R.2    Head-Gordon, M.3
  • 70
    • 0000692897 scopus 로고
    • Concentration quenching in chlorophyll
    • Beddard, G. S., and Porter, G. (1976) Concentration quenching in chlorophyll, Nature 260, 366-367.
    • (1976) Nature , vol.260 , pp. 366-367
    • Beddard, G.S.1    Porter, G.2
  • 72
    • 0042558799 scopus 로고    scopus 로고
    • Selective interaction between xanthophylls and chlorophylls in LHCII probed by femtosecond transient absorption spectroscopy
    • Gradinaru, C. C., van Grondelle, R., and van Amerongen, H. (2003) Selective interaction between xanthophylls and chlorophylls in LHCII probed by femtosecond transient absorption spectroscopy, J. Phys. Chem. B 107, 3938-3943.
    • (2003) J. Phys. Chem. B , vol.107 , pp. 3938-3943
    • Gradinaru, C.C.1    Van Grondelle, R.2    Van Amerongen, H.3
  • 73
    • 0035131660 scopus 로고    scopus 로고
    • Understanding the energy transfer function of LHCII, the major light-harvesting complex of green plants
    • van Amerongen, H., and van Grondelle, R. (2001) Understanding the energy transfer function of LHCII, the major light-harvesting complex of green plants, J. Phys. Chem. B 105, 604-617.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 604-617
    • Van Amerongen, H.1    Van Grondelle, R.2
  • 74
    • 0037447051 scopus 로고    scopus 로고
    • Evidence for direct carotenoid involvement in the regulation of photosynthetic light harvesting
    • Ma, Y.-Z., Holt, N. E., Li, X.-P., Niyogi, K. K., and Fleming, G. R. (2003) Evidence for direct carotenoid involvement in the regulation of photosynthetic light harvesting, Proc. Natl. Acad. Sci. U.S.A. 100, 4377-4382.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 4377-4382
    • Ma, Y.-Z.1    Holt, N.E.2    Li, X.-P.3    Niyogi, K.K.4    Fleming, G.R.5
  • 75
    • 0034696586 scopus 로고    scopus 로고
    • Mechanism of nonphotochemical quenching in green plants: Energies of the lowest excited singlet states of violaxanthin and zeaxanthin
    • Frank, H. A., Bautista, J. A., Josue, J. S., and Young, A. J. (2000) Mechanism of nonphotochemical quenching in green plants: energies of the lowest excited singlet states of violaxanthin and zeaxanthin, Biochemistry 39, 2831-2837.
    • (2000) Biochemistry , vol.39 , pp. 2831-2837
    • Frank, H.A.1    Bautista, J.A.2    Josue, J.S.3    Young, A.J.4
  • 76
    • 0037118373 scopus 로고    scopus 로고
    • 1 excited-state energies of xanthophylls by low-temperature fluorescence spectroscopy
    • 1 excited-state energies of xanthophylls by low-temperature fluorescence spectroscopy, J. Phys. Chem. A 106, 4815-4824.
    • (2002) J. Phys. Chem. A , vol.106 , pp. 4815-4824
    • Josue, J.S.1    Frank, H.A.2


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