메뉴 건너뛰기




Volumn , Issue , 2005, Pages 327-342

Influence of high light intensity on photosynthesis: Photoinhibition and energy dissipation

Author keywords

[No Author keywords available]

Indexed keywords


EID: 77950365038     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1201/9781420027877     Document Type: Chapter
Times cited : (4)

References (209)
  • 1
    • 0003050958 scopus 로고
    • Photoinhibition of photosynthesis induced by visible light
    • Powles SB. Photoinhibition of photosynthesis induced by visible light. Annu. Rev. Plant Physiol. 1984; 35:15-44.
    • (1984) Annu. Rev. Plant Physiol. , vol.35 , pp. 15-44
    • Powles, S.B.1
  • 2
    • 0032948239 scopus 로고    scopus 로고
    • Photosystem-II damage and repair cycle in chloroplasts: What modulates the rate of photodamage in vivo
    • Melis A. Photosystem-II damage and repair cycle in chloroplasts: what modulates the rate of photodamage in vivo. Trends Plant Sci. 1999; 4:130-135.
    • (1999) Trends Plant Sci. , vol.4 , pp. 130-135
    • Melis, A.1
  • 3
    • 84989667481 scopus 로고
    • The light-harvesting and protective functions of carotenoids in photosynthetic membranes
    • Siefermann-Harms D. The light-harvesting and protective functions of carotenoids in photosynthetic membranes. Physiol. Plant. 1987; 69:561-568.
    • (1987) Physiol. Plant. , vol.69 , pp. 561-568
    • Siefermann-Harms, D.1
  • 4
    • 84989741847 scopus 로고
    • Energy dissipation and photoprotection mechanisms during chlorophyll photobleaching in thylakoid membranes
    • Miller N, Carpentier R. Energy dissipation and photoprotection mechanisms during chlorophyll photobleaching in thylakoid membranes. Photochem. Photobiol. 1991; 90:465-472.
    • (1991) Photochem. Photobiol. , vol.90 , pp. 465-472
    • Miller, N.1    Carpentier, R.2
  • 5
    • 0033506468 scopus 로고    scopus 로고
    • Photoprotection revisited: Genetic and molecular approach
    • Niyogi KK. Photoprotection revisited: genetic and molecular approach. Annu. Rev. Plant Physiol. Plant Mol. Biol. 1999; 50:333-359.
    • (1999) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.50 , pp. 333-359
    • Niyogi, K.K.1
  • 6
    • 0025187594 scopus 로고
    • Carotenoids and photoprotection: A role for xanthophyll zeaxanthin
    • Demming-Adams B. Carotenoids and photoprotection:a role for xanthophyll zeaxanthin. Biochim. Biophys. Acta 1990; 1020:1-24.
    • (1990) Biochim. Biophys. Acta , vol.1020 , pp. 1-24
    • Demming-Adams, B.1
  • 7
    • 0027489759 scopus 로고
    • A functional model for the role of cytochrome b-559 in the protection against donor and acceptor side photoinhibition
    • Barber J, De Las Rivas J. A functional model for the role of cytochrome b-559 in the protection against donor and acceptor side photoinhibition. Proc. Natl. Acad. Sci. USA. 1993; 90:10942-10946.
    • (1993) Proc. Natl. Acad. Sci. USA. , vol.90 , pp. 10942-10946
    • Barber, J.1    De Las Rivas, J.2
  • 8
    • 0002641372 scopus 로고    scopus 로고
    • Photoinactivation of the two photosystems in oxygenic photosynthesis: Mechanisms and regulation
    • Yunus M, Pathre U, Mohanty P, eds, London: Taylor and Francis
    • Ohad I, Sonoike K, Andersson B. Photoinactivation of the two photosystems in oxygenic photosynthesis:mechanisms and regulation. In: Yunus M, Pathre U, Mohanty P, eds. Probing Photosynthesis. Mechanisms, Regulation and Adaptation. London: Taylor and Francis, 2000:293-309.
    • (2000) Probing Photosynthesis. Mechanisms, Regulation and Adaptation. , pp. 293-309
    • Ohad, I.1    Sonoike, K.2    Andersson, B.3
  • 9
    • 0027199986 scopus 로고
    • Photoinhibition of photosystem II: Inactivation, protein damage and turnover
    • Aro EM, Virgin I, Andersson B. Photoinhibition of photosystem II: inactivation, protein damage and turnover. Biochim. Biophys. Acta 1993; 1143:113-134.
    • (1993) Biochim. Biophys. Acta , vol.1143 , pp. 113-134
    • Aro, E.M.1    Virgin, I.2    Andersson, B.3
  • 12
    • 0026696595 scopus 로고
    • Spectroscopic characterization of triplet forming states in photosystem II
    • Vass I, Styring S. Spectroscopic characterization of triplet forming states in photosystem II. Biochemistry 1992; 31:5957-5963.
    • (1992) Biochemistry , vol.31 , pp. 5957-5963
    • Vass, I.1    Styring, S.2
  • 14
    • 0025336206 scopus 로고
    • Characterization of triplet states in isolated photosystem II reaction centres - oxygen quenching as a mechanism for photodamage
    • Durrant JR, Giorgi LB, Barber J, Klug DR, Porter G. Characterization of triplet states in isolated photosystem II reaction centres - oxygen quenching as a mechanism for photodamage. Biochim. Biophys. Acta 1990; 1071:167-175.
    • (1990) Biochim. Biophys. Acta , vol.1071 , pp. 167-175
    • Durrant, J.R.1    Giorgi, L.B.2    Barber, J.3    Klug, D.R.4    Porter, G.5
  • 15
    • 0025293209 scopus 로고
    • Light-dependent degradation of the D1 protein in photosystem II is accelerated after inhibition of the water splitting reaction
    • Jegershöld C, Virgin I, Stryring S. Light-dependent degradation of the D1 protein in photosystem II is accelerated after inhibition of the water splitting reaction. Biochemistry 1990; 29:6179-6186.
    • (1990) Biochemistry , vol.29 , pp. 6179-6186
    • Jegershöld, C.1    Virgin, I.2    Stryring, S.3
  • 16
    • 0025965385 scopus 로고
    • Fast oxygen-independent degradation of the D1 reaction center protein in photosystem II
    • Jegershöld C, Stryring S. Fast oxygen-independent degradation of the D1 reaction center protein in photosystem II. FEBS Lett. 1991; 280:87-90.
    • (1991) FEBS Lett. , vol.280 , pp. 87-90
    • Jegershöld, C.1    Stryring, S.2
  • 17
    • 0344174159 scopus 로고
    • Inhibition of water splitting increases the susceptibility of photosystem II to photoinhibition
    • Wang WQ, Chapman DJ, Barber J. Inhibition of water splitting increases the susceptibility of photosystem II to photoinhibition. Plant Physiol. 1992; 99:16-20.
    • (1992) Plant Physiol. , vol.99 , pp. 16-20
    • Wang, W.Q.1    Chapman, D.J.2    Barber, J.3
  • 18
    • 0025370526 scopus 로고
    • Kinetics of photoinhibition in hydroxylamine-extracted photosystem II membranes: Relevance to photoactivation and sites of electron donation
    • Blubaugh DJ, Cheniae GM. Kinetics of photoinhibition in hydroxylamine-extracted photosystem II membranes: relevance to photoactivation and sites of electron donation. Biochemistry 1990; 29:5109-5118.
    • (1990) Biochemistry , vol.29 , pp. 5109-5118
    • Blubaugh, D.J.1    Cheniae, G.M.2
  • 19
    • 0025781574 scopus 로고
    • b-Carotene within the isolated photosystem II reaction centre: Photooxidation and irreversible bleaching of this chromophore by oxidised P680
    • Telfer A, De Las Rivas J, Barber J. b-Carotene within the isolated photosystem II reaction centre: photooxidation and irreversible bleaching of this chromophore by oxidised P680. Biochim. Biophys. Acta 1991; 1060:106-114.
    • (1991) Biochim. Biophys. Acta , vol.1060 , pp. 106-114
    • Telfer, A.1    De Las Rivas, J.2    Barber, J.3
  • 20
    • 0037195307 scopus 로고    scopus 로고
    • What is b-carotene doing in the photosystem II reaction centre
    • Telfer A. What is b-carotene doing in the photosystem II reaction centre. Philos. Trans. R. Soc. Lond. B 2002; 357:1431-1440.
    • (2002) Philos. Trans. R. Soc. Lond. B , vol.357 , pp. 1431-1440
    • Telfer, A.1
  • 21
    • 0001294420 scopus 로고
    • Regulation of protein metabolism: Coupling of photosynthetic electron transport to in vivo degradation of the rapidly metabolized 32-kilodalton protein of the chloroplast membrane
    • Mattoo AK, Hoffman-Falk H, Marder JB, Edelman M. Regulation of protein metabolism: coupling of photosynthetic electron transport to in vivo degradation of the rapidly metabolized 32-kilodalton protein of the chloroplast membrane. Proc. Natl. Acad. Sci. USA 1984; 81:1380-1384.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 1380-1384
    • Mattoo, A.K.1    Hoffman-Falk, H.2    Marder, J.B.3    Edelman, M.4
  • 22
    • 0030065188 scopus 로고    scopus 로고
    • Light response of D1 turnover and photosystem II efficiency in the seagrass Zostera capricorni
    • Flanigan YS, Critchley C. Light response of D1 turnover and photosystem II efficiency in the seagrass Zostera capricorni. Planta 1996; 198:319-323.
    • (1996) Planta , vol.198 , pp. 319-323
    • Flanigan, Y.S.1    Critchley, C.2
  • 23
    • 0029921367 scopus 로고    scopus 로고
    • The rate constant of photoinhibition, measured in lincomycin-treated leaves, is directly proportional to light intensity
    • Tyystjärvi E, Aro E-M. The rate constant of photoinhibition, measured in lincomycin-treated leaves, is directly proportional to light intensity. Proc. Natl. Acad. Sci. USA 1996; 93:2213-2218.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2213-2218
    • Tyystjärvi, E.1    Aro, E.-M.2
  • 24
    • 0033105886 scopus 로고    scopus 로고
    • D1-D2 protein degradation in the chloroplast. Complex light saturation kinetics
    • Jansen MAK, Mattoo AK, Edelman M. D1-D2 protein degradation in the chloroplast. Complex light saturation kinetics. Eur. J. Biochem. 1999; 260:527-532.
    • (1999) Eur. J. Biochem. , vol.260 , pp. 527-532
    • Jansen, M.A.K.1    Mattoo, A.K.2    Edelman, M.3
  • 25
    • 0030813946 scopus 로고    scopus 로고
    • Transcriptional and translational adjustments of psbA gene expression in mature chloroplasts during photoinhibition and subsequent repair of photosystem II
    • Kettunen R, Pursiheimo S, Rintamäki E, Van Wijk KJ, Aro E-M. Transcriptional and translational adjustments of psbA gene expression in mature chloroplasts during photoinhibition and subsequent repair of photosystem II. Eur. J. Biochem. 1997; 247:441-448.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 441-448
    • Kettunen, R.1    Pursiheimo, S.2    Rintamäki, E.3    Van Wijk, K.J.4    Aro, E.-M.5
  • 26
    • 0030591449 scopus 로고    scopus 로고
    • Light is required for efficient translation elongation and subsequent integration of the D1-protein into photosystem II
    • Van Wijk KJ, Eichacker L. Light is required for efficient translation elongation and subsequent integration of the D1-protein into photosystem II. FEBS Lett. 1996; 388:89-93.
    • (1996) FEBS Lett. , vol.388 , pp. 89-93
    • Van Wijk, K.J.1    Eichacker, L.2
  • 29
    • 0000433719 scopus 로고    scopus 로고
    • D1 polypeptide degradation may regulate psbA gene expression at transcriptional and translational levels in Synechocystis sp. PCC 6803
    • Tyystjärvi T, Mulo P, Mäenpää P, Aro E-M. D1 polypeptide degradation may regulate psbA gene expression at transcriptional and translational levels in Synechocystis sp. PCC 6803. Photosynth. Res. 1996; 47:111-120.
    • (1996) Photosynth. Res. , vol.47 , pp. 111-120
    • Tyystjärvi, T.1    Mulo, P.2    Mäenpää, P.3    Aro, E.-M.4
  • 30
    • 0030729781 scopus 로고    scopus 로고
    • DNA insertional mutagenesis for the elucidation of a photosystem II repair process in the green alga Chalmydomonas reinhardtii
    • Zhang L, Niyogi KK, Nemson JA, Grossman AR, Melis A. DNA insertional mutagenesis for the elucidation of a photosystem II repair process in the green alga Chalmydomonas reinhardtii. Photosynth. Res. 1997; 53:173-184.
    • (1997) Photosynth. Res. , vol.53 , pp. 173-184
    • Zhang, L.1    Niyogi, K.K.2    Nemson, J.A.3    Grossman, A.R.4    Melis, A.5
  • 31
    • 0028606359 scopus 로고
    • The recovery of photosynthesis from low-temperature photoinhibition is accelerated by the unsaturation of membrane lipids: A mechanism of chilling tolerance
    • Gombos Z, Wada H, Murata N. The recovery of photosynthesis from low-temperature photoinhibition is accelerated by the unsaturation of membrane lipids:a mechanism of chilling tolerance. Proc. Natl. Acad. Sci. USA 1994; 91:8787-8791.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8787-8791
    • Gombos, Z.1    Wada, H.2    Murata, N.3
  • 32
    • 0031177711 scopus 로고    scopus 로고
    • Membrane lipid unsaturation processing of the photosystem II reaction-center protein D1 at low temperature
    • Kanervo E, Tasaka Y, Murata N, Aro E-M. Membrane lipid unsaturation processing of the photosystem II reaction-center protein D1 at low temperature. Plant Physiol. 1997; 114:841-849.
    • (1997) Plant Physiol. , vol.114 , pp. 841-849
    • Kanervo, E.1    Tasaka, Y.2    Murata, N.3    Aro, E.-M.4
  • 33
    • 0031403991 scopus 로고    scopus 로고
    • Genetic enhancement of the ability to tolerate photoinhibition by introduction of unsaturated bonds into membrane glycerolipids
    • Gombos Z, Kanervo E, Tsvetkova N, Sakamoto T, Aro E-M, Murata N. Genetic enhancement of the ability to tolerate photoinhibition by introduction of unsaturated bonds into membrane glycerolipids. Plant Physiol. 1997; 115:551-559.
    • (1997) Plant Physiol. , vol.115 , pp. 551-559
    • Gombos, Z.1    Kanervo, E.2    Tsvetkova, N.3    Sakamoto, T.4    Aro, E.-M.5    Murata, N.6
  • 34
    • 0028933939 scopus 로고
    • Low unsaturation level of thylakoid membrane lipids limits turnover of the D1 protein of photosystem II at high irradiance
    • Kanervo E, Aro E-M, Murata N. Low unsaturation level of thylakoid membrane lipids limits turnover of the D1 protein of photosystem II at high irradiance. FEBS Lett. 1995; 364:239-242.
    • (1995) FEBS Lett. , vol.364 , pp. 239-242
    • Kanervo, E.1    Aro, E.-M.2    Murata, N.3
  • 35
    • 0035983676 scopus 로고    scopus 로고
    • Photoinhibition in mutants of Arabidopsis deficient in thylakoid unsaturation
    • Vijayan P, Browse J. Photoinhibition in mutants of Arabidopsis deficient in thylakoid unsaturation. Plant Physiol. 2002; 129:876-885.
    • (2002) Plant Physiol. , vol.129 , pp. 876-885
    • Vijayan, P.1    Browse, J.2
  • 36
  • 37
    • 0036852140 scopus 로고    scopus 로고
    • Salt stress inhibits the repair of photodamaged photosystem II by suppressing the transcription and translation of psbA genes in Synechocystis
    • Allakhverdiev SI, Nishiyama Y, Miyairi S, Yamamoto H, Inagaki N, Kanesaki Y, Murata N. Salt stress inhibits the repair of photodamaged photosystem II by suppressing the transcription and translation of psbA genes in Synechocystis. Plant Physiol. 2002; 130:1443-1453.
    • (2002) Plant Physiol. , vol.130 , pp. 1443-1453
    • Allakhverdiev, S.I.1    Nishiyama, Y.2    Miyairi, S.3    Yamamoto, H.4    Inagaki, N.5    Kanesaki, Y.6    Murata, N.7
  • 38
    • 0029167906 scopus 로고
    • Regulation of D1-protein degradation during photoinhibition of photosystem II in vivo: Phosphorylation of the D1 protein in various plant groups
    • RintamÄki E, Salo R, Lehtonen E, Aro E-M. Regulation of D1-protein degradation during photoinhibition of photosystem II in vivo: phosphorylation of the D1 protein in various plant groups. Planta 1995; 195:379-386.
    • (1995) Planta , vol.195 , pp. 379-386
    • RintamÄki, E.1    Salo, R.2    Lehtonen, E.3    Aro, E.-M.4
  • 39
    • 0028783872 scopus 로고
    • Degradation of the D1- and D2-proteins of photosystem II in higher plant is regulated by reversible phosphorylation
    • Koivuniemi A, Aro E-M, Andersson B. Degradation of the D1- and D2-proteins of photosystem II in higher plant is regulated by reversible phosphorylation. Biochemistry 1995; 34:16022-16029.
    • (1995) Biochemistry , vol.34 , pp. 16022-16029
    • Koivuniemi, A.1    Aro, E.-M.2    Andersson, B.3
  • 40
    • 0030440421 scopus 로고    scopus 로고
    • Phosphorylation of PSII polypeptides inhibits D1 protein-degradation and increases PSII stability
    • Ebbert V, Godde D. Phosphorylation of PSII polypeptides inhibits D1 protein-degradation and increases PSII stability. Photosynth. Res. 1996; 50:257-269.
    • (1996) Photosynth. Res. , vol.50 , pp. 257-269
    • Ebbert, V.1    Godde, D.2
  • 41
    • 0029930771 scopus 로고    scopus 로고
    • Differential D1 dephosphorylation in functional and photodamage photosystem II centers
    • Rintamäki E, Kettunen R, Aro E-M. Differential D1 dephosphorylation in functional and photodamage photosystem II centers. J. Biol. Chem. 1996; 271:14870-14875.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14870-14875
    • Rintamäki, E.1    Kettunen, R.2    Aro, E.-M.3
  • 42
    • 0033081148 scopus 로고    scopus 로고
    • Characterization of damage to the D1 protein of photosystem II under photoinhibitory illumination in non-phosphorylated and phosphorylated thylakoid membranes
    • Mizusawa N, Yamamoto N, Miyao M. Characterization of damage to the D1 protein of photosystem II under photoinhibitory illumination in non-phosphorylated and phosphorylated thylakoid membranes. J. Photochem. Photobiol. 1999; 48:97-103.
    • (1999) J. Photochem. Photobiol. , vol.48 , pp. 97-103
    • Mizusawa, N.1    Yamamoto, N.2    Miyao, M.3
  • 43
    • 0032899433 scopus 로고    scopus 로고
    • Role of phosphorylation in the repair cycle and oligomeric structure of photosystem II
    • Baena-González E, Barbato R, Aro E-M. Role of phosphorylation in the repair cycle and oligomeric structure of photosystem II. Planta 1999; 208:196-204.
    • (1999) Planta , vol.208 , pp. 196-204
    • Baena-González, E.1    Barbato, R.2    Aro, E.-M.3
  • 44
    • 0028822239 scopus 로고
    • Electron transport regulates exchanges of two forms of photosystem II D1 protein in the cyanobacterium Synechococcus
    • Campbell D, Zhou G, Gustafsson P, Öquist G, Clarke AK. Electron transport regulates exchanges of two forms of photosystem II D1 protein in the cyanobacterium Synechococcus. EMBO J. 1995; 14:5457-5466.
    • (1995) EMBO J. , vol.14 , pp. 5457-5466
    • Campbell, D.1    Zhou, G.2    Gustafsson, P.3    Öquist, G.4    Clarke, A.K.5
  • 45
    • 0030087815 scopus 로고    scopus 로고
    • Over-production of the D1:2 protein makes Synechococcus cells more tolerant to photoinhibition of photosystem II
    • Soitamo AJ, Zhou G, Clarke AK, Öquist G, Gustafsson P, Aro E-M. Over-production of the D1:2 protein makes Synechococcus cells more tolerant to photoinhibition of photosystem II. Plant Mol. Biol. 1996; 30:467-478.
    • (1996) Plant Mol. Biol. , vol.30 , pp. 467-478
    • Soitamo, A.J.1    Zhou, G.2    Clarke, A.K.3    Öquist, G.4    Gustafsson, P.5    Aro, E.-M.6
  • 46
    • 0000670645 scopus 로고
    • The cyanobacterium Synechococcus modulates photosystem II function in response to excitation stress through D1 exchange
    • Öquist G, Campbell D, Clarke AK, Gustafsson P. The cyanobacterium Synechococcus modulates photosystem II function in response to excitation stress through D1 exchange. Photosynth. Res. 1995; 46:151-158.
    • (1995) Photosynth. Res. , vol.46 , pp. 151-158
    • Öquist, G.1    Campbell, D.2    Clarke, A.K.3    Gustafsson, P.4
  • 47
    • 0033081176 scopus 로고    scopus 로고
    • The regulatory role of photosystem II photoinactivation and de novo protein synthesis in the degradation and exchange of two forms of the D1 protein in the cyanobacterium Synechococcus PCC 7942
    • Komenda J, Koblízek M, Masojídek J. The regulatory role of photosystem II photoinactivation and de novo protein synthesis in the degradation and exchange of two forms of the D1 protein in the cyanobacterium Synechococcus PCC 7942. J. Photochem. Photobiol. 1999; 48:114-119.
    • (1999) J. Photochem. Photobiol. , vol.48 , pp. 114-119
    • Komenda, J.1    Koblízek, M.2    Masojídek, J.3
  • 48
    • 0030910218 scopus 로고    scopus 로고
    • Synthesis and assembly of the D1 protein into photosystem II: Processing of the C-terminus and identification of the initial assembly partners and complexes during photosystem II repair
    • Van Wijk KJ, Roobol-Boza M, Kettunen R, Andersson B, Aro E-M. Synthesis and assembly of the D1 protein into photosystem II: processing of the C-terminus and identification of the initial assembly partners and complexes during photosystem II repair. Biochemistry 1997; 36:6178-6186.
    • (1997) Biochemistry , vol.36 , pp. 6178-6186
    • Van Wijk, K.J.1    Roobol-Boza, M.2    Kettunen, R.3    Andersson, B.4    Aro, E.-M.5
  • 49
    • 0035544125 scopus 로고    scopus 로고
    • Photosystem II damage and repair cycle in the green alga Dunaliella salina: Involvement of a chloroplast-localized HSP70
    • Yokthongwattana K, Chrost B, Behrman S, Casper-Lindley C, Melis A. Photosystem II damage and repair cycle in the green alga Dunaliella salina: involvement of a chloroplast-localized HSP70. Plant Cell Physiol. 2001; 42:1389-1397.
    • (2001) Plant Cell Physiol. , vol.42 , pp. 1389-1397
    • Yokthongwattana, K.1    Chrost, B.2    Behrman, S.3    Casper-Lindley, C.4    Melis, A.5
  • 50
    • 0033149821 scopus 로고    scopus 로고
    • A chloroplast-targeted heat shock protein 70 (HSP70) contributes to the protection and repair of photosystem II during and after photoinhibition
    • Schroda M, Vallon O, Wollman F-A, Beck CF. A chloroplast-targeted heat shock protein 70 (HSP70) contributes to the protection and repair of photosystem II during and after photoinhibition. Plant Cell 1999; 11:1165-1178.
    • (1999) Plant Cell , vol.11 , pp. 1165-1178
    • Schroda, M.1    Vallon, O.2    Wollman, F.-A.3    Beck, C.F.4
  • 51
    • 0001677316 scopus 로고
    • Phosphorylation and disassembly of the photosystem II core as an early stage of photoinhibition
    • Giardi MT. Phosphorylation and disassembly of the photosystem II core as an early stage of photoinhibition. Planta 1993; 190:107-113.
    • (1993) Planta , vol.190 , pp. 107-113
    • Giardi, M.T.1
  • 52
    • 0023429786 scopus 로고
    • Identification of a primary in vivo degradation product of the rapidly-turning-over 32 kd protein of photosystem II
    • Greenberg BM, Gaba V, Mattoo AK, Edelman M. Identification of a primary in vivo degradation product of the rapidly-turning-over 32 kd protein of photosystem II. EMBO J. 1987; 6:2865-2869.
    • (1987) EMBO J. , vol.6 , pp. 2865-2869
    • Greenberg, B.M.1    Gaba, V.2    Mattoo, A.K.3    Edelman, M.4
  • 53
    • 0025899668 scopus 로고
    • New evidence suggests that the initial photoinduced cleavage of the D1-protein may not occur near the PEST sequence
    • Barbato R, Shipton CA, Giorgio M, Giacometti M, Barber J. New evidence suggests that the initial photoinduced cleavage of the D1-protein may not occur near the PEST sequence. FEBS Lett. 1991; 290:162-166.
    • (1991) FEBS Lett. , vol.290 , pp. 162-166
    • Barbato, R.1    Shipton, C.A.2    Giorgio, M.3    Giacometti, M.4    Barber, J.5
  • 54
    • 0026043886 scopus 로고
    • Photoinduced degradation of the D1 polypeptide in isolated reaction centers of photosystem II: Evidence for an autoproteolytic process triggered by the oxidizing side of the photosystem
    • Shipton CA, Barber J. Photoinduced degradation of the D1 polypeptide in isolated reaction centers of photosystem II: evidence for an autoproteolytic process triggered by the oxidizing side of the photosystem. Proc. Natl. Acad. Sci. USA 1991; 88:6691-6695.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 6691-6695
    • Shipton, C.A.1    Barber, J.2
  • 55
    • 0026597716 scopus 로고
    • Two sites of primary degradation of the D1-protein induced by acceptor or donor side photo-inhibition in photosystem II core complexes
    • De Las Rivas J, Andersson B, Barber J. Two sites of primary degradation of the D1-protein induced by acceptor or donor side photo-inhibition in photosystem II core complexes. FEBS Lett. 1992; 301:246-252.
    • (1992) FEBS Lett. , vol.301 , pp. 246-252
    • De Las Rivas, J.1    Andersson, B.2    Barber, J.3
  • 56
    • 0027325215 scopus 로고
    • Detection of a 10 kDa breakdown product containing the C-terminus of the D1-protein in photoinhibited wheat leaves suggests an acceptor side mechanism
    • Canovas PM, Barber J. Detection of a 10 kDa breakdown product containing the C-terminus of the D1-protein in photoinhibited wheat leaves suggests an acceptor side mechanism. FEBS Lett. 1993; 324:341-344.
    • (1993) FEBS Lett. , vol.324 , pp. 341-344
    • Canovas, P.M.1    Barber, J.2
  • 57
    • 0026628316 scopus 로고
    • Photoinduced degradation of the D1 protein in isolated thylakoids and various photosystem II particles after donor-side inactivations
    • Barbato R, Frizzo A, Friso G, Rigoni F, Giacometti M. Photoinduced degradation of the D1 protein in isolated thylakoids and various photosystem II particles after donor-side inactivations. FEBS Lett. 1992; 304:136-140.
    • (1992) FEBS Lett. , vol.304 , pp. 136-140
    • Barbato, R.1    Frizzo, A.2    Friso, G.3    Rigoni, F.4    Giacometti, M.5
  • 58
    • 0027521566 scopus 로고
    • Evidence for concurrent donor and acceptor side photoinduced degradation of the D1-protein in isolated reaction centers of photosystem II
    • Friso G, Giacometti GM, Barber J, Barbato R. Evidence for concurrent donor and acceptor side photoinduced degradation of the D1-protein in isolated reaction centers of photosystem II. Biochim. Biophys. Acta 1993; 1144:265-270.
    • (1993) Biochim. Biophys. Acta , vol.1144 , pp. 265-270
    • Friso, G.1    Giacometti, G.M.2    Barber, J.3    Barbato, R.4
  • 59
    • 45449121949 scopus 로고
    • Changes in the properties of reaction center II during the initial stages of photoinhibition as revealed by thermoluminescence measurements
    • Ohad I, Koike H, Shoat S, Inoue Y. Changes in the properties of reaction center II during the initial stages of photoinhibition as revealed by thermoluminescence measurements. Biochim. Biophys. Acta 1988; 933:288-298.
    • (1988) Biochim. Biophys. Acta , vol.933 , pp. 288-298
    • Ohad, I.1    Koike, H.2    Shoat, S.3    Inoue, Y.4
  • 60
    • 0032840054 scopus 로고    scopus 로고
    • Light-induced degradation of cytochrome b559 during photoinhibition of the photosystem II reaction center
    • Ortega JM, Roncel M, Losada M. Light-induced degradation of cytochrome b559 during photoinhibition of the photosystem II reaction center. FEBS Lett. 1999; 458:87-92.
    • (1999) FEBS Lett. , vol.458 , pp. 87-92
    • Ortega, J.M.1    Roncel, M.2    Losada, M.3
  • 61
    • 0042473085 scopus 로고    scopus 로고
    • Degradation of the D1 protein of photosystem II under illumination in vivo: Two different pathways involving cleavage or intermolecular cross-linking
    • Mizusawa N, Tomo T, Satoh K, Miyao M. Degradation of the D1 protein of photosystem II under illumination in vivo: two different pathways involving cleavage or intermolecular cross-linking. Biochemistry 2003; 42:10034-10044.
    • (2003) Biochemistry , vol.42 , pp. 10034-10044
    • Mizusawa, N.1    Tomo, T.2    Satoh, K.3    Miyao, M.4
  • 62
    • 1642615623 scopus 로고
    • The role of chloroplastencoded protein biosynthesis on the rate of D1 protein degradation in Dunaliella salina
    • Vasilikiotis C, Melis A. The role of chloroplastencoded protein biosynthesis on the rate of D1 protein degradation in Dunaliella salina. Photosynth. Res. 1995; 147-155.
    • (1995) Photosynth. Res. , pp. 147-155
    • Vasilikiotis, C.1    Melis, A.2
  • 63
    • 0038671972 scopus 로고    scopus 로고
    • Dynamic interaction between the D1 protein, CP43 and OEC33 at the luminal side of photosystem II in spinach chloroplasts: Evidence from light-induced cross-linking of the proteins in the donor-side photoinhibition
    • Henmi T, Yamasaki H, Sakuma S, Tomokawa Y, Tamura N, Shen J-R, Yamamoto Y. Dynamic interaction between the D1 protein, CP43 and OEC33 at the luminal side of photosystem II in spinach chloroplasts:evidence from light-induced cross-linking of the proteins in the donor-side photoinhibition. Plant Cell Physiol. 2003; 44:451-456.
    • (2003) Plant Cell Physiol. , vol.44 , pp. 451-456
    • Henmi, T.1    Yamasaki, H.2    Sakuma, S.3    Tomokawa, Y.4    Tamura, N.5    Shen, J.-R.6    Yamamoto, Y.7
  • 64
    • 0025871297 scopus 로고
    • Light-induced D1 protein degradation is catalyzed by a serine-type protease
    • Virgin I, Salter AH, Ghanotakis DF, Andersson B. Light-induced D1 protein degradation is catalyzed by a serine-type protease. FEBS Lett. 1991; 287:125-128.
    • (1991) FEBS Lett. , vol.287 , pp. 125-128
    • Virgin, I.1    Salter, A.H.2    Ghanotakis, D.F.3    Andersson, B.4
  • 65
    • 0008732737 scopus 로고
    • Degradation of the 32-kilodalton thylakoid-membrane polypeptide of Chlamydomonas reinhardi Y-1
    • Wettern M, Galling G. Degradation of the 32-kilodalton thylakoid-membrane polypeptide of Chlamydomonas reinhardi Y-1. Planta 1985; 166:474-482.
    • (1985) Planta , vol.166 , pp. 474-482
    • Wettern, M.1    Galling, G.2
  • 66
    • 0028578011 scopus 로고
    • Light-dependent degradation of the photosystem II D1 protein is retarded by inhibitors of chloroplast transcription and translation: Possible involvement of a chloroplast-encoded proteinase
    • Gong H. Light-dependent degradation of the photosystem II D1 protein is retarded by inhibitors of chloroplast transcription and translation: possible involvement of a chloroplast-encoded proteinase. Biochim. Biophys. Acta 1994; 1188:422-426.
    • (1994) Biochim. Biophys. Acta , vol.1188 , pp. 422-426
    • Gong, H.1
  • 67
    • 0026695796 scopus 로고
    • On the molecular mechanism of light-induced D1 protein degradation in photosystem II core particles
    • Salter AH, Virgin I, Hagman A, Andersson B. On the molecular mechanism of light-induced D1 protein degradation in photosystem II core particles. Biochemistry 1992; 31:3990-3998.
    • (1992) Biochemistry , vol.31 , pp. 3990-3998
    • Salter, A.H.1    Virgin, I.2    Hagman, A.3    Andersson, B.4
  • 68
    • 0025034263 scopus 로고
    • In vitro studies on light-induced inhibition of photosystem II and D1-protein degradation at low temperature
    • Aro E-M, Hundal T, Carlsberg I, Andersson B. In vitro studies on light-induced inhibition of photosystem II and D1-protein degradation at low temperature. Biochim. Biophys. Acta 1990; 1019:269-275.
    • (1990) Biochim. Biophys. Acta , vol.1019 , pp. 269-275
    • Aro, E.-M.1    Hundal, T.2    Carlsberg, I.3    Andersson, B.4
  • 70
    • 0025071018 scopus 로고
    • Light-induced D1-protein degradation in isolated photosystem II core complexes
    • Virgin I, Ghanotakis DF, Andersson B. Light-induced D1-protein degradation in isolated photosystem II core complexes. FEBS Lett. 1990; 269:45-48.
    • (1990) FEBS Lett. , vol.269 , pp. 45-48
    • Virgin, I.1    Ghanotakis, D.F.2    Andersson, B.3
  • 71
    • 0025834029 scopus 로고
    • The isolated D1/D2/cyt b-559 reaction center complex of photosystem II possesses a serine-type endopeptidase activity
    • Misra AN, Hall SG, Barber J. The isolated D1/D2/cyt b-559 reaction center complex of photosystem II possesses a serine-type endopeptidase activity. Biochim. Biophys. Acta 1991; 1059:239-242.
    • (1991) Biochim. Biophys. Acta , vol.1059 , pp. 239-242
    • Misra, A.N.1    Hall, S.G.2    Barber, J.3
  • 72
    • 0001596491 scopus 로고    scopus 로고
    • A chloroplast DegP2 protease performs the primary cleavage of the photodamage D1 protein in plant photosystem II
    • Haußühl K, Andersson B, Adamska I. A chloroplast DegP2 protease performs the primary cleavage of the photodamage D1 protein in plant photosystem II. EMBO J. 2001; 20:713-722.
    • (2001) EMBO J. , vol.20 , pp. 713-722
    • Haußühl, K.1    Andersson, B.2    Adamska, I.3
  • 73
    • 0034031132 scopus 로고    scopus 로고
    • The thylakoid FtsH protease plays a role in the light-induced turnover of the photosystem II D1 protein
    • Lindahl M, Spetea C, Hundal T, Oppenheim AB, Adam Z, Andersson B. The thylakoid FtsH protease plays a role in the light-induced turnover of the photosystem II D1 protein. Plant Cell 2000; 12:419-431.
    • (2000) Plant Cell , vol.12 , pp. 419-431
    • Lindahl, M.1    Spetea, C.2    Hundal, T.3    Oppenheim, A.B.4    Adam, Z.5    Andersson, B.6
  • 75
    • 0035910656 scopus 로고    scopus 로고
    • Characterization of the stromal protease(s) degrading the cross-linked products of the D1 protein generated by photoinhibition of photosystem II
    • Fernaji A, Abe S, Ishikawa Y, Henmi T, Tomokawa Y, Nishi Y, Tamura N, Yamamoto Y. Characterization of the stromal protease(s) degrading the cross-linked products of the D1 protein generated by photoinhibition of photosystem II. Biochim. Biophys. Acta 2001; 1503:385-395.
    • (2001) Biochim. Biophys. Acta , vol.1503 , pp. 385-395
    • Fernaji, A.1    Abe, S.2    Ishikawa, Y.3    Henmi, T.4    Tomokawa, Y.5    Nishi, Y.6    Tamura, N.7    Yamamoto, Y.8
  • 76
    • 0035083795 scopus 로고    scopus 로고
    • Quality control of photosystem II
    • Yamamoto Y. Quality control of photosystem II. Plant Cell Physiol. 2001; 42:121-128.
    • (2001) Plant Cell Physiol. , vol.42 , pp. 121-128
    • Yamamoto, Y.1
  • 77
    • 0027963598 scopus 로고
    • Involvement of active oxygen species in degradation of the D1 protein under strong illumination in isolated subcomplexes of photosystem II
    • Miyao M. Involvement of active oxygen species in degradation of the D1 protein under strong illumination in isolated subcomplexes of photosystem II. Biochemistry 1994; 33:9722-9730.
    • (1994) Biochemistry , vol.33 , pp. 9722-9730
    • Miyao, M.1
  • 78
    • 0028131199 scopus 로고
    • Singlet oxygen end free radical production during acceptor- and donor-side induced photoinhibition. Studies with spin trapping EPR spectroscopy
    • Hideg E, Spetea C, Vass I. Singlet oxygen end free radical production during acceptor- and donor-side induced photoinhibition. Studies with spin trapping EPR spectroscopy. Biochim. Biophys. Acta 1994; 1186:143-152.
    • (1994) Biochim. Biophys. Acta , vol.1186 , pp. 143-152
    • Hideg, E.1    Spetea, C.2    Vass, I.3
  • 79
    • 0013248642 scopus 로고    scopus 로고
    • Generation and trapping of singlet oxygen during strong illumination of a photosystem II core complex
    • Mishra RK, Mishra NP, Kambourakis S, Orfanopoulos M, Ghanotakis DF. Generation and trapping of singlet oxygen during strong illumination of a photosystem II core complex. Plant Sci. 1996; 115:151-155.
    • (1996) Plant Sci. , vol.115 , pp. 151-155
    • Mishra, R.K.1    Mishra, N.P.2    Kambourakis, S.3    Orfanopoulos, M.4    Ghanotakis, D.F.5
  • 80
    • 0027183423 scopus 로고
    • Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions
    • Stadtmen ER. Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions. Annu. Rev. Biochem. 1993; 62:797-821.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 797-821
    • Stadtmen, E.R.1
  • 81
    • 0002174971 scopus 로고
    • Oxygen activation and oxygen toxicity
    • Eltsner EF. Oxygen activation and oxygen toxicity. Annu. Rev. Plant Physiol. 1982; 33:73-96.
    • (1982) Annu. Rev. Plant Physiol. , vol.33 , pp. 73-96
    • Eltsner, E.F.1
  • 82
    • 84945060319 scopus 로고
    • Free radical scavengers inhibit lightdependent degradation of the 32 kDa photosystem II reaction center protein
    • Sopory SK, Greenberg BM, Mehta RA, Edelman M, Mattoo AK. Free radical scavengers inhibit lightdependent degradation of the 32 kDa photosystem II reaction center protein. Z. Naturforsch. 1989; 45c:412-417.
    • (1989) Z. Naturforsch. , vol.45 C , pp. 412-417
    • Sopory, S.K.1    Greenberg, B.M.2    Mehta, R.A.3    Edelman, M.4    Mattoo, A.K.5
  • 83
    • 0000908246 scopus 로고
    • The effect of oxygen radicals on proteolysis in isolated oat chloroplasts
    • Casano LM, Trippi VS. The effect of oxygen radicals on proteolysis in isolated oat chloroplasts. Plant Cell Physiol. 1992; 33:329-332.
    • (1992) Plant Cell Physiol. , vol.33 , pp. 329-332
    • Casano, L.M.1    Trippi, V.S.2
  • 84
    • 0028232687 scopus 로고
    • Destructive role of singlet oxygen during aerobic illumination of the photosystem II core complex
    • Mishra NP, Francke C, van Gorkom HJ, Ghanotakis DF. Destructive role of singlet oxygen during aerobic illumination of the photosystem II core complex. Biochim. Biophys. Acta 1994; 1186:81-90.
    • (1994) Biochim. Biophys. Acta , vol.1186 , pp. 81-90
    • Mishra, N.P.1    Francke, C.2    van Gorkom, H.J.3    Ghanotakis, D.F.4
  • 85
    • 0027966015 scopus 로고
    • Exposure of a photosystem II complex to chemically generated singlet oxygen result in D1 fragments similar to the ones observed during aerobic photoinhibition
    • Mishra NP, Ghanotakis DF. Exposure of a photosystem II complex to chemically generated singlet oxygen result in D1 fragments similar to the ones observed during aerobic photoinhibition. Biochim. Biophys. Acta 1994; 1187:296-300.
    • (1994) Biochim. Biophys. Acta , vol.1187 , pp. 296-300
    • Mishra, N.P.1    Ghanotakis, D.F.2
  • 86
    • 0033081605 scopus 로고    scopus 로고
    • Singlet oxygen formation detected by near-infrared emission from isolated photosystem II reaction centres: Direct correlation between P680 triplet decay and luminescence rise kinetics and its consequences for photoinhibition
    • Telfer A, Oldham TC, Phillips D, Barber J. Singlet oxygen formation detected by near-infrared emission from isolated photosystem II reaction centres: direct correlation between P680 triplet decay and luminescence rise kinetics and its consequences for photoinhibition. J. Photochem. Photobiol. 1999; 48:89-96.
    • (1999) J. Photochem. Photobiol. , vol.48 , pp. 89-96
    • Telfer, A.1    Oldham, T.C.2    Phillips, D.3    Barber, J.4
  • 87
    • 0034730983 scopus 로고    scopus 로고
    • Do oxidative stress conditions impairing photosynthesis in the light manifest as photoinhibition
    • Hideg E, Kálai T, Hideg K, Vass I. Do oxidative stress conditions impairing photosynthesis in the light manifest as photoinhibition. Philos. Trans. R. Soc. Lond. B 2000; 355:1511-1516.
    • (2000) Philos. Trans. R. Soc. Lond. B , vol.355 , pp. 1511-1516
    • Hideg, E.1    Kálai, T.2    Hideg, K.3    Vass, I.4
  • 88
    • 0036808841 scopus 로고    scopus 로고
    • Detection of singlet oxygen and superoxide with fluorescent sensors in leaves under stress by photoinhibition and UV radiation
    • Hideg E, Barta C, Kálai T, Vass I, Hideg K, Asada K. Detection of singlet oxygen and superoxide with fluorescent sensors in leaves under stress by photoinhibition and UV radiation. Plant Cell Physiol. 2002; 43:1154-1164.
    • (2002) Plant Cell Physiol. , vol.43 , pp. 1154-1164
    • Hideg, E.1    Barta, C.2    Kálai, T.3    Vass, I.4    Hideg, K.5    Asada, K.6
  • 89
    • 5644242010 scopus 로고    scopus 로고
    • Photoinhibition of photosystem II in tobacco plants overexpressing glutathione reductase and poplars overexpressing superoxide dismutase
    • Tyystjärvi E, Riikonen M, Arisi A-CM, Kettunen R, Jouanin L, Foyer CH. Photoinhibition of photosystem II in tobacco plants overexpressing glutathione reductase and poplars overexpressing superoxide dismutase. Physiol. Plant. 1999; 105:409-416.
    • (1999) Physiol. Plant. , vol.105 , pp. 409-416
    • Tyystjärvi, E.1    Riikonen, M.2    Arisi, A.-C.M.3    Kettunen, R.4    Jouanin, L.5    Foyer, C.H.6
  • 90
    • 0037232722 scopus 로고    scopus 로고
    • Study on the photo-generation of superoxide radicals in photosystem II with EPR spin trapping techniques
    • Zhang S, Weng J, Pan J, Tu T, Yao S, Xu C. Study on the photo-generation of superoxide radicals in photosystem II with EPR spin trapping techniques. Photosynth. Res. 2003; 75:41-48.
    • (2003) Photosynth. Res. , vol.75 , pp. 41-48
    • Zhang, S.1    Weng, J.2    Pan, J.3    Tu, T.4    Yao, S.5    Xu, C.6
  • 91
    • 0002112572 scopus 로고
    • Mechanism of photoinactivation in photosynthetic systems. I. The dark reaction in photoinactivation
    • Satoh K. Mechanism of photoinactivation in photosynthetic systems. I. The dark reaction in photoinactivation. Plant Cell Physiol. 1970; 11:15-27.
    • (1970) Plant Cell Physiol. , vol.11 , pp. 15-27
    • Satoh, K.1
  • 92
    • 0002112574 scopus 로고
    • Mechanism of photoinactivation in photosynthetic systems. II. The occurrence of and properties of two different types of photoinactivation
    • Satoh K. Mechanism of photoinactivation in photosynthetic systems. II. The occurrence of and properties of two different types of photoinactivation. Plant Cell Physiol. 1970; 11:29-38.
    • (1970) Plant Cell Physiol. , vol.11 , pp. 29-38
    • Satoh, K.1
  • 93
    • 0000112076 scopus 로고
    • Photoinhibition of reaction centers of photosystem I and II in intact Bryopsis chloroplasts under anaerobic conditions
    • Satoh K, Fork DC. Photoinhibition of reaction centers of photosystem I and II in intact Bryopsis chloroplasts under anaerobic conditions. Plant Physiol. 1982; 70:1004-1008.
    • (1982) Plant Physiol. , vol.70 , pp. 1004-1008
    • Satoh, K.1    Fork, D.C.2
  • 94
    • 0012956285 scopus 로고
    • Mechanism of photoinactivation in photosynthetic systems. III. Site and mode of photoactivation in photosystem I
    • Satoh K. Mechanism of photoinactivation in photosynthetic systems. III. Site and mode of photoactivation in photosystem I. Plant Cell Physiol. 1970; 11:187-197.
    • (1970) Plant Cell Physiol. , vol.11 , pp. 187-197
    • Satoh, K.1
  • 95
    • 0000913268 scopus 로고
    • Photoinactivation sites of photosystem I in isolated chloroplasts
    • Inoue K, Sakurai H, Hiyama T. Photoinactivation sites of photosystem I in isolated chloroplasts. Plant Cell Physiol. 1986; 27:961-968.
    • (1986) Plant Cell Physiol. , vol.27 , pp. 961-968
    • Inoue, K.1    Sakurai, H.2    Hiyama, T.3
  • 96
    • 77957179566 scopus 로고
    • The photoinhibition site of photosystem I in isolated chloroplasts under extremely reducing conditions
    • Inoue K, Fujii T, Yokoyama E, Matsuura K, Hiyama T, Sakurai H. The photoinhibition site of photosystem I in isolated chloroplasts under extremely reducing conditions. Plant Cell Physiol. 1989; 30:65-71.
    • (1989) Plant Cell Physiol. , vol.30 , pp. 65-71
    • Inoue, K.1    Fujii, T.2    Yokoyama, E.3    Matsuura, K.4    Hiyama, T.5    Sakurai, H.6
  • 97
    • 0028025799 scopus 로고
    • The site of photoinhibition in leaves of Cucumis sativus L. at low temperatures is photosystem I, not photosystem II
    • Terashima I, Funayama S, Sonoike K. The site of photoinhibition in leaves of Cucumis sativus L. at low temperatures is photosystem I, not photosystem II. Planta 1994; 193:300-306.
    • (1994) Planta , vol.193 , pp. 300-306
    • Terashima, I.1    Funayama, S.2    Sonoike, K.3
  • 98
    • 0028985765 scopus 로고
    • Destruction of photosystem I iron-sulfur centers in leaves of Cucumis sativus L. by weak illumination at chilling temperatures
    • Sonoike K, Terashima I, Iwaki M, and Itoh S. Destruction of photosystem I iron-sulfur centers in leaves of Cucumis sativus L. by weak illumination at chilling temperatures. FEBS Lett. 1995; 362:235-238.
    • (1995) FEBS Lett. , vol.362 , pp. 235-238
    • Sonoike, K.1    Terashima, I.2    Iwaki, M.3    Itoh, S.4
  • 99
    • 0031992140 scopus 로고    scopus 로고
    • Photosystem I is an early target of photoinhibition in barley illuminated at chilling temperatures
    • Tjus SE, Moller BL, Scheller HS. Photosystem I is an early target of photoinhibition in barley illuminated at chilling temperatures. Plant Physiol. 1998; 116:755-764.
    • (1998) Plant Physiol. , vol.116 , pp. 755-764
    • Tjus, S.E.1    Moller, B.L.2    Scheller, H.S.3
  • 100
    • 0028052392 scopus 로고
    • Mechanism of photosystem-I photoinhibition in leaves of Cucumis sativus L
    • Sonoike K, Terashima I. Mechanism of photosystem-I photoinhibition in leaves of Cucumis sativus L. Planta 1994; 194:287-293.
    • (1994) Planta , vol.194 , pp. 287-293
    • Sonoike, K.1    Terashima, I.2
  • 101
    • 0035029939 scopus 로고    scopus 로고
    • Active oxygen produced during selective excitation of photosystem I is damaging not only to photosystem I but also to photosystem II
    • Tjus SE, Scheller HV, Andersson B, Moller BL. Active oxygen produced during selective excitation of photosystem I is damaging not only to photosystem I but also to photosystem II. Plant Physiol. 2001; 125:2007-2015.
    • (2001) Plant Physiol. , vol.125 , pp. 2007-2015
    • Tjus, S.E.1    Scheller, H.V.2    Andersson, B.3    Moller, B.L.4
  • 102
    • 0032015863 scopus 로고    scopus 로고
    • Various aspects of inhibition of photosynthesis under light/chilling stress: “photoinhibition at chilling temperatures” versus “chilling damage in the light”
    • Sonoike K. Various aspects of inhibition of photosynthesis under light/chilling stress: “photoinhibition at chilling temperatures” versus “chilling damage in the light”. J. Plant Res. 1998; 111:121-129.
    • (1998) J. Plant Res. , vol.111 , pp. 121-129
    • Sonoike, K.1
  • 104
    • 0031113659 scopus 로고    scopus 로고
    • Inactivation and degradation of CuZn-SOD by active oxygen species in wheat chloroplasts exposed to photooxidative stress
    • Casano LM, Gómez LD, Lascano HR, González CA, Trippi VS. Inactivation and degradation of CuZn-SOD by active oxygen species in wheat chloroplasts exposed to photooxidative stress. Plant Cell Physiol. 1997; 38:433-440.
    • (1997) Plant Cell Physiol. , vol.38 , pp. 433-440
    • Casano, L.M.1    Gómez, L.D.2    Lascano, H.R.3    González, C.A.4    Trippi, V.S.5
  • 105
    • 0037639912 scopus 로고    scopus 로고
    • Photoinhibitory light-induced changes in the composition of chlorophyll-protein complexes and photochemical activity in photosystem-I submembrane fractions
    • Rajagopal S, Bukhov NG, Carpentier R. Photoinhibitory light-induced changes in the composition of chlorophyll-protein complexes and photochemical activity in photosystem-I submembrane fractions. Photochem. Photobiol. 2003; 77:284-291.
    • (2003) Photochem. Photobiol. , vol.77 , pp. 284-291
    • Rajagopal, S.1    Bukhov, N.G.2    Carpentier, R.3
  • 106
    • 0029795121 scopus 로고    scopus 로고
    • Photoproduction and detoxification of hydroxyl radicals in chloroplasts and leaves and relation to photoinactivation of photosystem I and photosystem II
    • Jacob B, Heber U. Photoproduction and detoxification of hydroxyl radicals in chloroplasts and leaves and relation to photoinactivation of photosystem I and photosystem II. Plant Cell Physiol. 1996; 37:629-635.
    • (1996) Plant Cell Physiol. , vol.37 , pp. 629-635
    • Jacob, B.1    Heber, U.2
  • 107
    • 0001175088 scopus 로고
    • Degradation of photosystem I reaction center proteins during photoinhibition in vitro
    • Mathis P, ed, Vol II. Dordrecht: Kluwer Academic Publishers
    • Baba K, Itoh S, Hoshina S. Degradation of photosystem I reaction center proteins during photoinhibition in vitro. In: Mathis P, ed. Photosynthesis: From Light to Biosphere, Vol II. Dordrecht: Kluwer Academic Publishers, 1995:179-182.
    • (1995) Photosynthesis: From Light to Biosphere , pp. 179-182
    • Baba, K.1    Itoh, S.2    Hoshina, S.3
  • 108
    • 0000628304 scopus 로고    scopus 로고
    • Degradation of psaB gene product, the reaction center subunit of photosystem I, is caused during photoinhibition of photosystem I: Possible involvement of active oxygen species
    • Sonoike K. Degradation of psaB gene product, the reaction center subunit of photosystem I, is caused during photoinhibition of photosystem I: possible involvement of active oxygen species. Plant Sci. 1996; 115:157-164.
    • (1996) Plant Sci. , vol.115 , pp. 157-164
    • Sonoike, K.1
  • 109
    • 0037253713 scopus 로고    scopus 로고
    • Different kinetics of photoinactivation of photosystem-I mediated electron transport and P700 in isolated thylakoid membranes
    • Velitchkova M, Yruela I, Alfonso M, Alonso PJ, Picorel R. Different kinetics of photoinactivation of photosystem-I mediated electron transport and P700 in isolated thylakoid membranes. J. Photochem. Photobiol. 2003; 69:41-48.
    • (2003) J. Photochem. Photobiol. , vol.69 , pp. 41-48
    • Velitchkova, M.1    Yruela, I.2    Alfonso, M.3    Alonso, P.J.4    Picorel, R.5
  • 110
    • 0030727551 scopus 로고    scopus 로고
    • The mechanism of the degradation of psaB gene product, one of the photosynthetic reaction center subunits of photosystem I, upon photoinhibition
    • Sonoike K, Kamo M, Hihara Y, Hiyama T, Enami T. The mechanism of the degradation of psaB gene product, one of the photosynthetic reaction center subunits of photosystem I, upon photoinhibition. Photosynth. Res. 1997; 53:55-63.
    • (1997) Photosynth. Res. , vol.53 , pp. 55-63
    • Sonoike, K.1    Kamo, M.2    Hihara, Y.3    Hiyama, T.4    Enami, T.5
  • 111
    • 0032713985 scopus 로고    scopus 로고
    • Inhibition of photosystem I and II in chilling-sensitive and chilling-tolerant plants under light and low-temperature stress
    • Barth C, Krause GH. Inhibition of photosystem I and II in chilling-sensitive and chilling-tolerant plants under light and low-temperature stress. Z. Naturforsch. 1999; 54c:645-657.
    • (1999) Z. Naturforsch. , vol.54 C , pp. 645-657
    • Barth, C.1    Krause, G.H.2
  • 112
    • 0035131213 scopus 로고    scopus 로고
    • Response of photosystem I compared with photosystem II to high-light stress in tropical shade and sun leaves
    • Barth C, Krause GH, Winter K. Response of photosystem I compared with photosystem II to high-light stress in tropical shade and sun leaves. Plant Cell Environ. 2001; 24:163-176.
    • (2001) Plant Cell Environ. , vol.24 , pp. 163-176
    • Barth, C.1    Krause, G.H.2    Winter, K.3
  • 113
    • 0000968916 scopus 로고    scopus 로고
    • Photoinhibition of photosystem I: Its physiological significance in the chilling sensitivity of plants
    • Sonoike K. Photoinhibition of photosystem I: its physiological significance in the chilling sensitivity of plants. Plant Cell Physiol. 1996; 37:239-247.
    • (1996) Plant Cell Physiol. , vol.37 , pp. 239-247
    • Sonoike, K.1
  • 114
    • 0036938632 scopus 로고    scopus 로고
    • Irreversible damage to photosystem I by chilling in the light: Cause of the degradation of chlorophyll after returning to normal growth temperature
    • Kudoh H, Sonoike K. Irreversible damage to photosystem I by chilling in the light: cause of the degradation of chlorophyll after returning to normal growth temperature. Planta 2002; 215:541-548.
    • (2002) Planta , vol.215 , pp. 541-548
    • Kudoh, H.1    Sonoike, K.2
  • 115
    • 0032876021 scopus 로고    scopus 로고
    • Photoinhibition of photosystem I damaged both reaction centre proteins PSI-A and PSI-B and acceptor-side located small photosystem I polypeptides
    • Tjus SE, Moller BL, Scheller HV. Photoinhibition of photosystem I damaged both reaction centre proteins PSI-A and PSI-B and acceptor-side located small photosystem I polypeptides. Photosynth. Res. 1999; 60:75-86.
    • (1999) Photosynth. Res. , vol.60 , pp. 75-86
    • Tjus, S.E.1    Moller, B.L.2    Scheller, H.V.3
  • 116
    • 17744370527 scopus 로고    scopus 로고
    • Photoinhibition of photosystem I in field-grown barley (Hordeum vulgare L.): Induction, recovery and acclimation
    • Teicher HB, Moller BL, Scheller HV. Photoinhibition of photosystem I in field-grown barley (Hordeum vulgare L.): induction, recovery and acclimation. Photosynth. Res. 2000; 64:53-61.
    • (2000) Photosynth. Res. , vol.64 , pp. 53-61
    • Teicher, H.B.1    Moller, B.L.2    Scheller, H.V.3
  • 117
    • 0036650608 scopus 로고    scopus 로고
    • Changes in the structure of chlorophyll-protein complexes and excitation energy during photoinhibitory treatments of isolated photosystem I submembrane particles
    • Rajagopal S, Bukhov NG, Carpentier R. Changes in the structure of chlorophyll-protein complexes and excitation energy during photoinhibitory treatments of isolated photosystem I submembrane particles. J. Photochem. Photobiol. 2002; 62:194-200.
    • (2002) J. Photochem. Photobiol. , vol.62 , pp. 194-200
    • Rajagopal, S.1    Bukhov, N.G.2    Carpentier, R.3
  • 118
    • 0039050324 scopus 로고
    • Interaction of dephenylpicrylhydrazyl with chloroplast lipids and the antioxidant function of tocopherol and carotenoids in photosynthetic membranes
    • Merzlyak MH, Kovrighnikh VA, Reshetnikova IV, Gusev MV. Interaction of dephenylpicrylhydrazyl with chloroplast lipids and the antioxidant function of tocopherol and carotenoids in photosynthetic membranes. Photobiochem. Photobiophys. 1986; 11:49-55.
    • (1986) Photobiochem. Photobiophys. , vol.11 , pp. 49-55
    • Merzlyak, M.H.1    Kovrighnikh, V.A.2    Reshetnikova, I.V.3    Gusev, M.V.4
  • 119
    • 85013306081 scopus 로고
    • Chloroplast protection in greening leaves
    • Gillam DJ, Dodge AD. Chloroplast protection in greening leaves. Physiol. Plant. 1985; 65:393-396.
    • (1985) Physiol. Plant. , vol.65 , pp. 393-396
    • Gillam, D.J.1    Dodge, A.D.2
  • 120
    • 1042265239 scopus 로고
    • Studies on chlorophyll photooxidation enhanced by benzonitriles in vivo and in vitro
    • Szigeti Z, Vagujfalvi D. Studies on chlorophyll photooxidation enhanced by benzonitriles in vivo and in vitro. Photobiochem. Photobiophys. 1984; 7:103-109.
    • (1984) Photobiochem. Photobiophys. , vol.7 , pp. 103-109
    • Szigeti, Z.1    Vagujfalvi, D.2
  • 121
    • 0007437362 scopus 로고
    • Suppression of carotenoid photobleaching by kaempferol in isolated chloroplasts
    • Takahama U. Suppression of carotenoid photobleaching by kaempferol in isolated chloroplasts. Plant Cell Physiol. 1982; 23:859-864.
    • (1982) Plant Cell Physiol. , vol.23 , pp. 859-864
    • Takahama, U.1
  • 122
    • 0342490288 scopus 로고
    • Inhibition of chloroplast photo-oxidation by flavonoids and mechanisms of the antioxidative action
    • Wagner GR, Youngman RJ, Elstner EF. Inhibition of chloroplast photo-oxidation by flavonoids and mechanisms of the antioxidative action. J. Photochem. Photobiol. B 1988; 1:451-460.
    • (1988) J. Photochem. Photobiol. B , vol.1 , pp. 451-460
    • Wagner, G.R.1    Youngman, R.J.2    Elstner, E.F.3
  • 123
    • 0000484231 scopus 로고
    • Non-photosynthetic functions of carotenoids
    • Krinsky NI. Non-photosynthetic functions of carotenoids. Philos. Trans. R. Soc. Lond. B 1978; 284:581-590.
    • (1978) Philos. Trans. R. Soc. Lond. B , vol.284 , pp. 581-590
    • Krinsky, N.I.1
  • 124
    • 84995097941 scopus 로고
    • Protection of chlorophyll-a by carotenoids from photodynamic decomposition
    • Koka P, Song P-S. Protection of chlorophyll-a by carotenoids from photodynamic decomposition. Photochem. Photobiol. 1978; 28:509-515.
    • (1978) Photochem. Photobiol. , vol.28 , pp. 509-515
    • Koka, P.1    Song, P.-S.2
  • 125
    • 0014667937 scopus 로고
    • Photobleaching of carotenoids related to the electron transport in chloroplasts
    • Yamashita K, Konishi K, Itoh M, Shibata K. Photobleaching of carotenoids related to the electron transport in chloroplasts. Biochim. Biophys. Acta 1969; 172:511-524.
    • (1969) Biochim. Biophys. Acta , vol.172 , pp. 511-524
    • Yamashita, K.1    Konishi, K.2    Itoh, M.3    Shibata, K.4
  • 126
    • 0018816688 scopus 로고
    • Chlorophyll photobleaching and ethane production in dichlorophenyldimethylurea-(DCMU) or paraquat-treated Euglena gracilis cell
    • Elstner EF, Osswald W. Chlorophyll photobleaching and ethane production in dichlorophenyldimethylurea-(DCMU) or paraquat-treated Euglena gracilis cell. Z. Naturforsch. 1980; 35c:129-135.
    • (1980) Z. Naturforsch. , vol.35 C , pp. 129-135
    • Elstner, E.F.1    Osswald, W.2
  • 127
    • 0345077807 scopus 로고
    • DCMU-induced fluorescence changes and photodestruction of pigments associated with an inhibition of photosystem I cyclic electron flow
    • Ridley SM, Horton P. DCMU-induced fluorescence changes and photodestruction of pigments associated with an inhibition of photosystem I cyclic electron flow. Z. Naturforch. 1984; 39c:351-353.
    • (1984) Z. Naturforch. , vol.39 C , pp. 351-353
    • Ridley, S.M.1    Horton, P.2
  • 128
    • 0001025833 scopus 로고    scopus 로고
    • Photoinhibition of photosystem I electron transfer activity in isolated photosystem I preparations with different chlorophyll contents
    • Baba K, Itoh S, Hastings G, Hoshina S. Photoinhibition of photosystem I electron transfer activity in isolated photosystem I preparations with different chlorophyll contents. Photosynth. Res. 1996; 47:121-130.
    • (1996) Photosynth. Res. , vol.47 , pp. 121-130
    • Baba, K.1    Itoh, S.2    Hastings, G.3    Hoshina, S.4
  • 129
    • 0034309797 scopus 로고    scopus 로고
    • Degradation of the photosystem I complex during photoinhibition
    • Hui Y, Jie W, Carpentier R. Degradation of the photosystem I complex during photoinhibition. Photochem. Photobiol. 2000; 72:508-512.
    • (2000) Photochem. Photobiol. , vol.72 , pp. 508-512
    • Hui, Y.1    Jie, W.2    Carpentier, R.3
  • 130
    • 10844274872 scopus 로고
    • Absorption spectra and relative photostability of the different forms of chlorophyll in Chlorella
    • Brown JS, French CS. Absorption spectra and relative photostability of the different forms of chlorophyll in Chlorella. Plant Physiol. 1959; 34:305-309.
    • (1959) Plant Physiol. , vol.34 , pp. 305-309
    • Brown, J.S.1    French, C.S.2
  • 131
    • 0014432812 scopus 로고
    • Relative stability of chlorophyll complexes in vivo
    • Thomas JB, Nijhuis HH. Relative stability of chlorophyll complexes in vivo. Biochim. Biophys. Acta 1968; 153:868-877.
    • (1968) Biochim. Biophys. Acta , vol.153 , pp. 868-877
    • Thomas, J.B.1    Nijhuis, H.H.2
  • 132
    • 1042288331 scopus 로고
    • Photobleaching and dark-bleaching in Euglena gracilis chloroplast fragments
    • Thomas JB, Bollen MHM, Klijn WJ. Photobleaching and dark-bleaching in Euglena gracilis chloroplast fragments. Acta Bot. Neerl. 1976; 25:361-369.
    • (1976) Acta Bot. Neerl. , vol.25 , pp. 361-369
    • Thomas, J.B.1    Bollen, M.H.M.2    Klijn, W.J.3
  • 133
    • 24844451937 scopus 로고
    • Absorption spectra of spinach quantasomes and bleaching of pigments
    • Sauer K, Calvin M. Absorption spectra of spinach quantasomes and bleaching of pigments. Biochim. Biophys. Acta 1962; 64:324-336.
    • (1962) Biochim. Biophys. Acta , vol.64 , pp. 324-336
    • Sauer, K.1    Calvin, M.2
  • 134
    • 0000436715 scopus 로고
    • Chlorophyll photobleaching in pigment-protein complexes
    • Carpentier R, Leblanc RM, Bellemare G. Chlorophyll photobleaching in pigment-protein complexes. Z. Naturforsch. 1986; 41c:284-290.
    • (1986) Z. Naturforsch. , vol.41 C , pp. 284-290
    • Carpentier, R.1    Leblanc, R.M.2    Bellemare, G.3
  • 135
    • 0001520389 scopus 로고
    • Chlorophyll a in unilamellar vesicles made with chloroplast lipids. Absorbance and photobleaching
    • Carpentier R, Dijkmans H, Leblanc RM, Aghion J. Chlorophyll a in unilamellar vesicles made with chloroplast lipids. Absorbance and photobleaching. Photobiochem. Photobiophys. 1983; 5:245-252.
    • (1983) Photobiochem. Photobiophys. , vol.5 , pp. 245-252
    • Carpentier, R.1    Dijkmans, H.2    Leblanc, R.M.3    Aghion, J.4
  • 136
    • 0032535215 scopus 로고    scopus 로고
    • A thermal broadening study of the antenna chlorophylls in PSI-200
    • Croce R, Zucchelli G, Galaschi FM, Jennings RC. A thermal broadening study of the antenna chlorophylls in PSI-200. Biochemistry 1998; 37:17355-17360.
    • (1998) Biochemistry , vol.37 , pp. 17355-17360
    • Croce, R.1    Zucchelli, G.2    Galaschi, F.M.3    Jennings, R.C.4
  • 137
    • 0031788230 scopus 로고    scopus 로고
    • Chlorina and viridis mutants of barley (Hordeum vulgare L.) allow assignment of long-wavelength chlorophyll forms to individual Lhca proteins of photosystem I in vivo
    • Knoetzel J, Bossmann B, Grimme H. Chlorina and viridis mutants of barley (Hordeum vulgare L.) allow assignment of long-wavelength chlorophyll forms to individual Lhca proteins of photosystem I in vivo. FEBS Lett. 1998; 436:339-342.
    • (1998) FEBS Lett. , vol.436 , pp. 339-342
    • Knoetzel, J.1    Bossmann, B.2    Grimme, H.3
  • 138
    • 85024793623 scopus 로고
    • Sequential extraction of chlorophyll a antenna of photosystem I
    • Oquist G, Samuelson G. Sequential extraction of chlorophyll a antenna of photosystem I. Physiol. Plant. 1980; 50:63-70.
    • (1980) Physiol. Plant. , vol.50 , pp. 63-70
    • Oquist, G.1    Samuelson, G.2
  • 139
    • 0000904285 scopus 로고
    • Long-wavelength absorbing antenna pigments and heterogeneous bands concentrate excitons and increases absorption cross-section
    • Trissl HW. Long-wavelength absorbing antenna pigments and heterogeneous bands concentrate excitons and increases absorption cross-section. Photosynth. Res. 1993; 35:247-263.
    • (1993) Photosynth. Res. , vol.35 , pp. 247-263
    • Trissl, H.W.1
  • 140
    • 37849016515 scopus 로고
    • Spectroscopic analysis of chlorophyll photobleaching in spinach thylakoids, grana and light-harvesting chlorophyll a/b protein complex
    • Zucchelli G, Galarschi FM, Jennings RC. Spectroscopic analysis of chlorophyll photobleaching in spinach thylakoids, grana and light-harvesting chlorophyll a/b protein complex. J. Photochem. Photobiol. B 1988; 2:483-490.
    • (1988) J. Photochem. Photobiol. B , vol.2 , pp. 483-490
    • Zucchelli, G.1    Galarschi, F.M.2    Jennings, R.C.3
  • 141
    • 0028150312 scopus 로고
    • Homogeneous photobleaching of chlorophyll holochromes in a photosystem I reaction center complex
    • Purcell M, Carpentier R. Homogeneous photobleaching of chlorophyll holochromes in a photosystem I reaction center complex. Photochem. Photobiol. 1994; 59:215-218.
    • (1994) Photochem. Photobiol. , vol.59 , pp. 215-218
    • Purcell, M.1    Carpentier, R.2
  • 142
    • 4243463569 scopus 로고
    • The influence of reducing the chlorophyll concentration by photobleaching on energy transfer to artificial traps within photosystem II antenna system
    • Jennings RC, Zucchelli G, Garlaschi FM. The influence of reducing the chlorophyll concentration by photobleaching on energy transfer to artificial traps within photosystem II antenna system. Biochim. Biophys. Acta 1989; 975:29-33.
    • (1989) Biochim. Biophys. Acta , vol.975 , pp. 29-33
    • Jennings, R.C.1    Zucchelli, G.2    Garlaschi, F.M.3
  • 143
    • 0029895603 scopus 로고    scopus 로고
    • Excited state equilibration in the photosystem I-light-harvesting I complex: P700 is almost isoenergetic with its antenna
    • Croce R, Zucchelli G, Garlaschi FM, Bassi R, Jennings RC. Excited state equilibration in the photosystem I-light-harvesting I complex: P700 is almost isoenergetic with its antenna. Biochemistry 1996; 35:8572-8579.
    • (1996) Biochemistry , vol.35 , pp. 8572-8579
    • Croce, R.1    Zucchelli, G.2    Garlaschi, F.M.3    Bassi, R.4    Jennings, R.C.5
  • 144
    • 0024280216 scopus 로고
    • Cytochrome b-559 may function to protect photosystem II from photoinhibition
    • Thompson LK, Brudvig GW. Cytochrome b-559 may function to protect photosystem II from photoinhibition. Biochemistry 1988; 27:6653-6658.
    • (1988) Biochemistry , vol.27 , pp. 6653-6658
    • Thompson, L.K.1    Brudvig, G.W.2
  • 145
    • 0030899689 scopus 로고    scopus 로고
    • Evidence for the involvement of cyclic electron transport in the protection of photosystem II against photoinhibition: Influence of a new phenolic compound
    • Allkhverdiev SI, Klimov VV, Carpentier R. Evidence for the involvement of cyclic electron transport in the protection of photosystem II against photoinhibition:influence of a new phenolic compound. Biochemistry 1997; 36:4149-4154.
    • (1997) Biochemistry , vol.36 , pp. 4149-4154
    • Allkhverdiev, S.I.1    Klimov, V.V.2    Carpentier, R.3
  • 146
    • 0027489759 scopus 로고
    • A functional model for the role of cytochrome b-559 in the protection against donor and acceptor side photoinhibition
    • Barber J, De Las Rivas J. A functional model for the role of cytochrome b-559 in the protection against donor and acceptor side photoinhibition. Proc. Natl. Acad. Sci. USA 1993; 90:10942-10956.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10942-10956
    • Barber, J.1    De Las Rivas, J.2
  • 147
    • 0001593103 scopus 로고
    • Cytochrome b-559 and proton conductance in oxygenic photosynthesis
    • Arnon DI, Tang GM-S. Cytochrome b-559 and proton conductance in oxygenic photosynthesis. Proc. Natl. Acad. Sci. USA 1988; 85:9524-9528.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 9524-9528
    • Arnon, D.I.1    Tang, G.M.-S.2
  • 148
    • 0026614703 scopus 로고
    • Photooxidation of cytochrome b559 in oxygen-evolving photosystem II
    • Buser CA, Diner BA, Brudvig GW. Photooxidation of cytochrome b559 in oxygen-evolving photosystem II. Biochemistry 1992; 31:11449-11459.
    • (1992) Biochemistry , vol.31 , pp. 11449-11459
    • Buser, C.A.1    Diner, B.A.2    Brudvig, G.W.3
  • 150
    • 0026722305 scopus 로고
    • Redox state of a one-electron component controls the rate of photoinhibition of photosystem II
    • Nedbal L, Samson G, Whitmarsh J. Redox state of a one-electron component controls the rate of photoinhibition of photosystem II. Proc. Natl. Acad. Sci. USA 1992; 89:7929-7933.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7929-7933
    • Nedbal, L.1    Samson, G.2    Whitmarsh, J.3
  • 152
    • 0027470096 scopus 로고
    • Possible photoacoustic detection of cyclic electron transport around photosystem II in photoinhibited thylakoid preparations
    • Lapointe L, Huner NPA, Leblanc RM, Carpentier R. Possible photoacoustic detection of cyclic electron transport around photosystem II in photoinhibited thylakoid preparations. Biochim. Biophys. Acta 1993; 1142:43-48.
    • (1993) Biochim. Biophys. Acta , vol.1142 , pp. 43-48
    • Lapointe, L.1    Huner, N.P.A.2    Leblanc, R.M.3    Carpentier, R.4
  • 154
    • 0000993550 scopus 로고
    • Photoinduced quenching of chlorophyll fluorescence in intact chloroplasts and algae
    • Krause GH, Vernotte C, Briantais J-M. Photoinduced quenching of chlorophyll fluorescence in intact chloroplasts and algae. Biochim. Biophys. Acta 1982; 679:116-124.
    • (1982) Biochim. Biophys. Acta , vol.679 , pp. 116-124
    • Krause, G.H.1    Vernotte, C.2    Briantais, J.-M.3
  • 155
    • 0018787380 scopus 로고
    • A quantitative study of the slow decline of chlorophyll a fluorescence in isolated chloroplast
    • Briantais J-M, Vernotte C, Picaud M, Krause GH. A quantitative study of the slow decline of chlorophyll a fluorescence in isolated chloroplast. Biochim. Biophys. Acta 1979; 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
  • 156
    • 45949114703 scopus 로고
    • Quantum efficiency of photosystem II in relation to energy-dependent quenching of chlorophyll fluorescence
    • Weiss E, Berry JA. Quantum efficiency of photosystem II in relation to energy-dependent quenching of chlorophyll fluorescence. Biochim. Biophys. Acta 1987; 894:198-208.
    • (1987) Biochim. Biophys. Acta , vol.894 , pp. 198-208
    • Weiss, E.1    Berry, J.A.2
  • 157
    • 0000191606 scopus 로고
    • 2 dependent electron flow, membrane energization and the mechanism of nonphotochemical quenching of chlorophyll fluorescence
    • 2 dependent electron flow, membrane energization and the mechanism of nonphotochemical quenching of chlorophyll fluorescence. Photosynth. Res. 1990; 25:279-293.
    • (1990) Photosynth. Res. , vol.25 , pp. 279-293
    • Schreiber, U.1    Neubauer, C.2
  • 158
    • 0002091376 scopus 로고
    • pH-dependence of oxygen evolution and reduction kinetics of photooxidized chlorophyll a II (P680) in photosystem II particles from Synechococcus sp
    • Schlodder E, Meyer B. pH-dependence of oxygen evolution and reduction kinetics of photooxidized chlorophyll a II (P680) in photosystem II particles from Synechococcus sp. Biochim. Biophys. Acta 1987; 890:23-31.
    • (1987) Biochim. Biophys. Acta , vol.890 , pp. 23-31
    • Schlodder, E.1    Meyer, B.2
  • 159
    • 0001634709 scopus 로고
    • 2-evolution in higher plant photosystem II by a simple low pH treatment
    • 2-evolution in higher plant photosystem II by a simple low pH treatment. FEBS Lett. 1988; 227:147-152.
    • (1988) FEBS Lett. , vol.227 , pp. 147-152
    • Ono, T.1    Inoue, I.2
  • 160
    • 0000746842 scopus 로고
    • The role of calcium in the pHdependent control of photosystem II
    • Kreiger A, Weiss E. The role of calcium in the pHdependent control of photosystem II. Photosynth. Res. 1993; 37:117-130.
    • (1993) Photosynth. Res. , vol.37 , pp. 117-130
    • Kreiger, A.1    Weiss, E.2
  • 161
    • 0026757544 scopus 로고
    • Energy-dependent quenching of chlorophyll-a-fluorescence: Effect of pH on stationary fluorescence and picosecond-relaxation kinetics in thylakoid membranes and photosystem II preparations
    • Kreiger A, MoyaI, Weiss E. Energy-dependent quenching of chlorophyll-a-fluorescence: effect of pH on stationary fluorescence and picosecond-relaxation kinetics in thylakoid membranes and photosystem II preparations. Biochim. Biophys. Acta 1992; 1102:167-176.
    • (1992) Biochim. Biophys. Acta , vol.1102 , pp. 167-176
    • Kreiger, A.1    Moya, I.2    Weiss, E.3
  • 163
    • 85023704649 scopus 로고
    • The relationship between quantum yield of photosynthetic electron transport and quenching of chlorophyll fluorescence
    • Genty B, Briantais J-M, Baker NR. The relationship between quantum yield of photosynthetic electron transport and quenching of chlorophyll fluorescence. Biochim. Biophys. Acta 1989; 990:87-92.
    • (1989) Biochim. Biophys. Acta , vol.990 , pp. 87-92
    • Genty, B.1    Briantais, J.-M.2    Baker, N.R.3
  • 164
    • 0026072865 scopus 로고
    • Control of light harvesting function of chloroplast membranes by aggregation of the LHCII chlorophyll-protein complex
    • Horton P, Ruban AV, Rees D, Pascal AA, Noctor G, Young AJ. Control of light harvesting function of chloroplast membranes by aggregation of the LHCII chlorophyll-protein complex. FEBS Lett. 1991; 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
  • 165
    • 0000642171 scopus 로고
    • Photoinhibition and zeaxanthin formation in intact leaves. A possible role of the xanthophyll cycle in the dissipation of excess light energy
    • Demming B, Winter K, Kruger A, Czygan FC. Photoinhibition and zeaxanthin formation in intact leaves. A possible role of the xanthophyll cycle in the dissipation of excess light energy. Plant Physiol. 1987; 84:218-224.
    • (1987) Plant Physiol. , vol.84 , pp. 218-224
    • Demming, B.1    Winter, K.2    Kruger, A.3    Czygan, F.C.4
  • 166
    • 0030095112 scopus 로고    scopus 로고
    • In vivo functions of carotenoids in higher plants
    • Demming-Adams B, Gilmore AM, Adams III WW. In vivo functions of carotenoids in higher plants. FASEB J. 1996; 10:403-412.
    • (1996) FASEB J. , vol.10 , pp. 403-412
    • Demming-Adams, B.1    Gilmore, A.M.2    Adams, W.W.3
  • 167
    • 0030995292 scopus 로고    scopus 로고
    • Mechanistic aspects of xanthophyll cycle-dependent photoprotection in higher plant chloroplasts and leaves
    • Gilmore AM. Mechanistic aspects of xanthophyll cycle-dependent photoprotection in higher plant chloroplasts and leaves. Physiol. Plant. 1997; 99:197-209.
    • (1997) Physiol. Plant. , vol.99 , pp. 197-209
    • Gilmore, A.M.1
  • 169
    • 0027945970 scopus 로고
    • The role of light-harvesting complex II in excess excitation energy dissipation: An in vivo fluorescence study on the origin of high-energy quenching
    • Lokstein H, Härtel H, Hoffmann P, Woitke P, Renger G. The role of light-harvesting complex II in excess excitation energy dissipation: an in vivo fluorescence study on the origin of high-energy quenching. J. Photochem. Photobiol. B 1994; 26:175-184.
    • (1994) J. Photochem. Photobiol. B , vol.26 , pp. 175-184
    • Lokstein, H.1    Härtel, H.2    Hoffmann, P.3    Woitke, P.4    Renger, G.5
  • 170
    • 0028150061 scopus 로고
    • Relationship among violaxanthin deepoxidation, thylakoid membrane conformation, and nonphotochemical chlorophyll fluorescence quenching in leaves of cotton
    • Bilger W, Björkman O. Relationship among violaxanthin deepoxidation, thylakoid membrane conformation, and nonphotochemical chlorophyll fluorescence quenching in leaves of cotton. Planta 1994; 193:238-246.
    • (1994) Planta , vol.193 , pp. 238-246
    • Bilger, W.1    Björkman, O.2
  • 171
    • 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, Hazlett TL, Debrunner PG, Govindjee. 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. 1996; 48:171-187.
    • (1996) Photosynth. Res. , vol.48 , pp. 171-187
    • Gilmore, A.1    Hazlett, T.L.2    Debrunner, P.G.3    Govindjee4
  • 172
    • 0030062555 scopus 로고    scopus 로고
    • Kinetics studies on the xanthophyll cycle in barley leaves. Influence of antenna size and relations to nonphotochemical chlorophyll fluorescence quenching
    • Härtel H, Lokstein H, Grimm B, Rank B. Kinetics studies on the xanthophyll cycle in barley leaves. Influence of antenna size and relations to nonphotochemical chlorophyll fluorescence quenching. Plant Physiol. 1996; 110:471-482.
    • (1996) Plant Physiol , vol.110 , pp. 471-482
    • Härtel, H.1    Lokstein, H.2    Grimm, B.3    Rank, B.4
  • 173
    • 2642704242 scopus 로고    scopus 로고
    • The xanthophyll cycle of Mantoniella squamata converts violaxanthin into anteraxanthin but not to zeaxanthin: Consequences for the mechanism of enhanced non-photochemical energy dissipation
    • Goss R, Böhme K, Wilhelm C. The xanthophyll cycle of Mantoniella squamata converts violaxanthin into anteraxanthin but not to zeaxanthin: consequences for the mechanism of enhanced non-photochemical energy dissipation. Planta 1998; 205:613-621.
    • (1998) Planta , vol.205 , pp. 613-621
    • Goss, R.1    Böhme, K.2    Wilhelm, C.3
  • 174
    • 0030060496 scopus 로고    scopus 로고
    • Violaxanthin deepoxidase. Purification of a 43-kilodalton luminal protein from lettuce by lipid-affinity precipitation with monogalactodyldiacylglyceride
    • Rockholm DC, Yamamoto HY. Violaxanthin deepoxidase. Purification of a 43-kilodalton luminal protein from lettuce by lipid-affinity precipitation with monogalactodyldiacylglyceride. Plant Physiol. 1996; 110:697-703.
    • (1996) Plant Physiol. , vol.110 , pp. 697-703
    • Rockholm, D.C.1    Yamamoto, H.Y.2
  • 175
    • 0030011229 scopus 로고    scopus 로고
    • Molecular cloning of violaxanthin de-epoxidase from romaine lettuce and expression in Escherichia coli
    • Bugos RC, Yamamoto HY. Molecular cloning of violaxanthin de-epoxidase from romaine lettuce and expression in Escherichia coli. Proc. Natl. Acad. Sci. USA 1996; 93:6320-6325.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6320-6325
    • Bugos, R.C.1    Yamamoto, H.Y.2
  • 176
    • 0031588952 scopus 로고    scopus 로고
    • Purification and properties of violaxanthin de-epoxidase from spinach
    • Havir EA, Tausta SL, Peterson RB. Purification and properties of violaxanthin de-epoxidase from spinach. Plant Sci. 1997; 123:57-66.
    • (1997) Plant Sci. , vol.123 , pp. 57-66
    • Havir, E.A.1    Tausta, S.L.2    Peterson, R.B.3
  • 177
    • 0032546960 scopus 로고    scopus 로고
    • Xanthophyll cycle enzymes are members of the lipocalin family, the first identified from plants
    • Bugos RC, Hieber AD, Yamamoto HY. Xanthophyll cycle enzymes are members of the lipocalin family, the first identified from plants. J. Biol. Chem. 1998; 273:15321-15324.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15321-15324
    • Bugos, R.C.1    Hieber, A.D.2    Yamamoto, H.Y.3
  • 178
    • 0029842720 scopus 로고    scopus 로고
    • Xanthophyll biosynhthesis: Cloning, expression, functional reconstitution, and regulation of b-cyclohexenyl carotenoids epoxidase from pepper (Capsicum annuum)
    • Bouvier F, d’Harlingue A, Hugueney P, Marin E, Marion-Poll A, Camara B. Xanthophyll biosynhthesis:cloning, expression, functional reconstitution, and regulation of b-cyclohexenyl carotenoids epoxidase from pepper (Capsicum annuum). J. Biol. Chem. 1996; 271:28861-28867.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28861-28867
    • Bouvier, F.1    d’Harlingue, A.2    Hugueney, P.3    Marin, E.4    Marion-Poll, A.5    Camara, B.6
  • 179
    • 0028004703 scopus 로고
    • Localization of the xanthophyllcycle enzyme violaxanthin de-epoxidase within the thylakoid lumen and abolition of its mobility by a (lightdependent) pH increase
    • Hager A, Holocher K. Localization of the xanthophyllcycle enzyme violaxanthin de-epoxidase within the thylakoid lumen and abolition of its mobility by a (lightdependent) pH increase. Planta 1994; 192:581-589.
    • (1994) Planta , vol.192 , pp. 581-589
    • Hager, A.1    Holocher, K.2
  • 180
    • 0342618438 scopus 로고    scopus 로고
    • Cis-trans-isomerisation of violaxanthin in LHCII: Violaxanthin isomerization cycle within the violaxanthin cycle
    • Gruszecki WI, Matula M, Ko-chi N, Koyama Y, Krupa Z. Cis-trans-isomerisation of violaxanthin in LHCII: violaxanthin isomerization cycle within the violaxanthin cycle. Biochim. Biophys. Acta 1997; 1319:267-274.
    • (1997) Biochim. Biophys. Acta , vol.1319 , pp. 267-274
    • Gruszecki, W.I.1    Matula, M.2    Ko-Chi, N.3    Koyama, Y.4    Krupa, Z.5
  • 181
    • 0032949556 scopus 로고    scopus 로고
    • Substrate specificity and functional aspects of violaxanthin-deepoxidase, an enzyme of the xanthophyll cycle
    • Grotz B, Molnár P, Stransky H, Hager A. Substrate specificity and functional aspects of violaxanthin-deepoxidase, an enzyme of the xanthophyll cycle. J. Plant Physiol. 1999; 154:437-446.
    • (1999) J. Plant Physiol. , vol.154 , pp. 437-446
    • Grotz, B.1    Molnár, P.2    Stransky, H.3    Hager, A.4
  • 182
    • 0027227672 scopus 로고
    • LHCII, the major light-harvesting pigment-protein complex is a zeaxanthin epoxidase
    • Gruszecki WI, Krupa Z. LHCII, the major light-harvesting pigment-protein complex is a zeaxanthin epoxidase. Biochim. Biophys. Acta 1993; 1144:97-101.
    • (1993) Biochim. Biophys. Acta , vol.1144 , pp. 97-101
    • Gruszecki, W.I.1    Krupa, Z.2
  • 183
    • 0038772441 scopus 로고    scopus 로고
    • The xanthophyll cycle of higher plants: Influence of antenna size and membrane organization
    • Färber A, Jahns P. The xanthophyll cycle of higher plants: influence of antenna size and membrane organization. Biochim. Biophys. Acta 1998; 1363:47-58.
    • (1998) Biochim. Biophys. Acta , vol.1363 , pp. 47-58
    • Färber, A.1    Jahns, P.2
  • 184
    • 0345034814 scopus 로고    scopus 로고
    • Suppression of zeaxanthin epoxidation by chloroplast phosphatase inhibitors in rice leaves
    • Xu CC, Jeon YA, Hwang HJ, Lee C-H. Suppression of zeaxanthin epoxidation by chloroplast phosphatase inhibitors in rice leaves. Plant Sci. 1999; 146:27-34.
    • (1999) Plant Sci. , vol.146 , pp. 27-34
    • Xu, C.C.1    Jeon, Y.A.2    Hwang, H.J.3    Lee, C.-H.4
  • 186
    • 0027966114 scopus 로고
    • Epoxidation of zeaxanthin and antheraxanthin reverses nonphotochemical quenching of photosystem II chlorophyll a fluorescence in the presence of trans-thylakoid DpH
    • Gilmore AM, Mohanty N, Yamamoto HY. Epoxidation of zeaxanthin and antheraxanthin reverses nonphotochemical quenching of photosystem II chlorophyll a fluorescence in the presence of trans-thylakoid DpH. FEBS Lett. 1994; 350:271-274.
    • (1994) FEBS Lett. , vol.350 , pp. 271-274
    • Gilmore, A.M.1    Mohanty, N.2    Yamamoto, H.Y.3
  • 187
    • 0028321177 scopus 로고
    • Enhancement by artificial electron acceptors of thylakoid lumen acidification and zeaxanthin formation
    • Büch K, Stransky H, Bigus H-J, Hager A. Enhancement by artificial electron acceptors of thylakoid lumen acidification and zeaxanthin formation. J. Plant Physiol. 1994; 144:641-648.
    • (1994) J. Plant Physiol. , vol.144 , pp. 641-648
    • Büch, K.1    Stransky, H.2    Bigus, H.-J.3    Hager, A.4
  • 188
    • 0032578572 scopus 로고    scopus 로고
    • Quantitative analysis of the effects of intrathylakoid pH and xanthophyll cycle pigments on chlorophyll a fluorescence lifetime distributions and intensity in thylakoids
    • Gilmore AM, Shinkarev VP, Hazlett TL, Govindjee. Quantitative analysis of the effects of intrathylakoid pH and xanthophyll cycle pigments on chlorophyll a fluorescence lifetime distributions and intensity in thylakoids. Biochemistry 1998; 37:13582-13593.
    • (1998) Biochemistry , vol.37 , pp. 13582-13593
    • Gilmore, A.M.1    Shinkarev, V.P.2    Hazlett, T.L.3    Govindjee4
  • 191
    • 0032573152 scopus 로고    scopus 로고
    • Altered xanthophyll compositions adversely affect chlorophyll accumulation and nonphotochemical quenching in Arabidopsis mutants
    • Pogson BJ, Niyogi KK, Björkman O, DellaPenna D. Altered xanthophyll compositions adversely affect chlorophyll accumulation and nonphotochemical quenching in Arabidopsis mutants. Proc. Natl. Acad. Sci. USA 1998; 95:13324-13329.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 13324-13329
    • Pogson, B.J.1    Niyogi, K.K.2    Björkman, O.3    DellaPenna, D.4
  • 192
    • 0037821740 scopus 로고    scopus 로고
    • Thermodynamic investigation into the mechanism of the chlorophyll fluorescence quenching in isolated photosystem II light-harvesting complexes
    • Wentworth M, Ruban AV, Horton P. Thermodynamic investigation into the mechanism of the chlorophyll fluorescence quenching in isolated photosystem II light-harvesting complexes. J. Biol. Chem. 2003; 278:21845-21850.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21845-21850
    • Wentworth, M.1    Ruban, A.V.2    Horton, P.3
  • 193
    • 0030484808 scopus 로고    scopus 로고
    • Picosecond time-resolved study on the nature of high-energy-state quenching in isolated pea thylakoids. Different localization of zeaxanthin dependent and independent quenching mechanisms
    • Wagner B, Goss R, Richter M, Wild A, Holzwarth AR. Picosecond time-resolved study on the nature of high-energy-state quenching in isolated pea thylakoids. Different localization of zeaxanthin dependent and independent quenching mechanisms. J. Photochem. Photobiol. 1996; 36:339-350.
    • (1996) J. Photochem. Photobiol. , vol.36 , pp. 339-350
    • Wagner, B.1    Goss, R.2    Richter, M.3    Wild, A.4    Holzwarth, A.R.5
  • 194
    • 11944264144 scopus 로고
    • Inhibition of zeaxanthin formation and of rapid changes in radiationless energy dissipation by dithiothreitol in spinach leaves and chloroplasts
    • Demming-Adams B, Adams III WW, Heber U, Neimanis S, Winter K, Kruger A, Czygan F-C, Bilger W, Björkman O. Inhibition of zeaxanthin formation and of rapid changes in radiationless energy dissipation by dithiothreitol in spinach leaves and chloroplasts. Plant Physiol. 1990; 92:293-301.
    • (1990) Plant Physiol. , vol.92 , pp. 293-301
    • Demming-Adams, B.1    Adams, W.W.2    Heber, U.3    Neimanis, S.4    Winter, K.5    Kruger, A.6    Czygan, F.-C.7    Bilger, W.8    Björkman, O.9
  • 195
    • 34249960486 scopus 로고
    • Role of xanthophyll cycle in photoprotection elucidated by measurements of lightinduced absorbance, fluorescence and photosynthesis in leaves of Hedera canariensis
    • Bilger W, Björkman O. Role of xanthophyll cycle in photoprotection elucidated by measurements of lightinduced absorbance, fluorescence and photosynthesis in leaves of Hedera canariensis. Photosynth. Res. 1990; 25:173-185.
    • (1990) Photosynth. Res. , vol.25 , pp. 173-185
    • Bilger, W.1    Björkman, O.2
  • 196
    • 0008243561 scopus 로고
    • Zeaxanthin formation and energy-dependent fluorescence quenching in pea chloroplasts under artificially mediated linear cyclic electron transport
    • Gilmore AM, Yamamoto HY. Zeaxanthin formation and energy-dependent fluorescence quenching in pea chloroplasts under artificially mediated linear cyclic electron transport. Plant Physiol. 1991; 96:635-643.
    • (1991) Plant Physiol. , vol.96 , pp. 635-643
    • Gilmore, A.M.1    Yamamoto, H.Y.2
  • 197
    • 0028155413 scopus 로고
    • Light-harvesting chlorophyll a-b complex requirement for regulation of photosystem II photochemistry by non-photochemical quenching
    • Briantais J-M. Light-harvesting chlorophyll a-b complex requirement for regulation of photosystem II photochemistry by non-photochemical quenching. Photosynth. Res. 1994; 40:287-294.
    • (1994) Photosynth. Res. , vol.40 , pp. 287-294
    • Briantais, J.-M.1
  • 198
    • 0029240265 scopus 로고
    • Analysis of the pigment stoichiometry of pigment-protein complexes from barley (Hordeum vulgare). The xanthophyll cycle intermediates occurs mainly in the light-harvesting complexes of photosystem I and photosystem II
    • Lee AL, Thornber JP. Analysis of the pigment stoichiometry of pigment-protein complexes from barley (Hordeum vulgare). The xanthophyll cycle intermediates occurs mainly in the light-harvesting complexes of photosystem I and photosystem II. Plant Physiol. 1995; 107:565-574.
    • (1995) Plant Physiol. , vol.107 , pp. 565-574
    • Lee, A.L.1    Thornber, J.P.2
  • 200
    • 0037069468 scopus 로고    scopus 로고
    • PsbS-dependent enhancement of feedback de-excitation protects photosystem II from photoinhibition
    • Li X-P, Müller-Moulé P, Gilmore AM, Niyogi KK. PsbS-dependent enhancement of feedback de-excitation protects photosystem II from photoinhibition. Proc. Natl. Acad. Sci. 2002; 99:15222-15227.
    • (2002) Proc. Natl. Acad. Sci. , vol.99 , pp. 15222-15227
    • Li, X.-P.1    Müller-Moulé, P.2    Gilmore, A.M.3    Niyogi, K.K.4
  • 201
    • 0038482125 scopus 로고    scopus 로고
    • Xanthophyll binding sites of the CP29 (Lhcb4) subunit of higher plant photosystem II investigated by domain swapping and mutation analysis
    • Gastaldelli M, Canino G, Croce R, Bassi R. Xanthophyll binding sites of the CP29 (Lhcb4) subunit of higher plant photosystem II investigated by domain swapping and mutation analysis. J. Biol. Chem. 2003; 278:19190-19198.
    • (2003) J. Biol. Chem. , vol.278 , pp. 19190-19198
    • Gastaldelli, M.1    Canino, G.2    Croce, R.3    Bassi, R.4
  • 202
    • 0030060007 scopus 로고    scopus 로고
    • Kinetic correlation of recovery from photoinhibition and zeaxanthin epoxidation
    • Jahns P, Miehe B. Kinetic correlation of recovery from photoinhibition and zeaxanthin epoxidation. Planta 1996; 198:202-210.
    • (1996) Planta , vol.198 , pp. 202-210
    • Jahns, P.1    Miehe, B.2
  • 203
    • 0035519581 scopus 로고    scopus 로고
    • Involvement of zeaxanthin and of Cbr protein in the repair of photosystem II from photoinhibition in the green alga Dunaliella salina
    • Jin E, Polle JEW, Melis A. Involvement of zeaxanthin and of Cbr protein in the repair of photosystem II from photoinhibition in the green alga Dunaliella salina. Biochim. Biophys. Acta 2001; 1506:244-259.
    • (2001) Biochim. Biophys. Acta , vol.1506 , pp. 244-259
    • Jin, E.1    Polle, J.E.W.2    Melis, A.3
  • 204
    • 0037648904 scopus 로고    scopus 로고
    • Role of the reversible xanthophyll cycle in the photosystem II damage and repair cycle in Dunaliella salina
    • Jin E, Yokthongwattana K, Polle JEW, Melis A. Role of the reversible xanthophyll cycle in the photosystem II damage and repair cycle in Dunaliella salina. Plant Physiol. 2003; 132:352-364.
    • (2003) Plant Physiol. , vol.132 , pp. 352-364
    • Jin, E.1    Yokthongwattana, K.2    Polle, J.E.W.3    Melis, A.4
  • 205
    • 0027974954 scopus 로고
    • Xanthophyll cycle and thermal energy dissipation in photosystem II: Relationship between zeaxanthin formation, energy-dependent fluorescence quenching and photoinhibition
    • Thiele A, Krause GH. Xanthophyll cycle and thermal energy dissipation in photosystem II: relationship between zeaxanthin formation, energy-dependent fluorescence quenching and photoinhibition. J. Plant Physiol. 1994; 144:324-332.
    • (1994) J. Plant Physiol. , vol.144 , pp. 324-332
    • Thiele, A.1    Krause, G.H.2
  • 206
    • 0032766859 scopus 로고    scopus 로고
    • The role of ascorbate in the protection of thylakoids against photoinactivation
    • Forti G, Barbagallo RP, Inversini B. The role of ascorbate in the protection of thylakoids against photoinactivation. Photosynth. Res. 1999; 59:215-222.
    • (1999) Photosynth. Res. , vol.59 , pp. 215-222
    • Forti, G.1    Barbagallo, R.P.2    Inversini, B.3
  • 207
    • 0001515234 scopus 로고
    • Regulation of thermal dissipation of absorbed light energy in chloroplasts indicated by energy-dependent fluorescence quenching
    • Krause GH, Laasch H, Weis E. Regulation of thermal dissipation of absorbed light energy in chloroplasts indicated by energy-dependent fluorescence quenching. Plant Physiol. Biochem. 1988; 26:445-452.
    • (1988) Plant Physiol. Biochem. , vol.26 , pp. 445-452
    • Krause, G.H.1    Laasch, H.2    Weis, E.3
  • 208
    • 0000349004 scopus 로고
    • A study of the regulation and function of energy-dependent quenching in pea chloroplasts
    • Oxborough K, Horton P. A study of the regulation and function of energy-dependent quenching in pea chloroplasts. Biochim. Biophys. Acta 1988; 934:135-143.
    • (1988) Biochim. Biophys. Acta , vol.934 , pp. 135-143
    • Oxborough, K.1    Horton, P.2
  • 209
    • 0001722176 scopus 로고
    • pH dependent chlorophyll fluorescence quenching indicating a mechanism of protection against photoinhibition of chloroplasts
    • Krause GH, Behrend U. pH dependent chlorophyll fluorescence quenching indicating a mechanism of protection against photoinhibition of chloroplasts. FEBS Lett. 1986; 200:298-302.
    • (1986) FEBS Lett. , vol.200 , pp. 298-302
    • Krause, G.H.1    Behrend, U.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.