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Volumn 1608, Issue 1, 2004, Pages 63-73

Formation of radicals from singlet oxygen produced during photoinhibition of isolated light-harvesting proteins of photosystem II

Author keywords

ESR; Light harvesting complex; Photoinhibition; Protein degradation; Reactive oxygen species; Singlet oxygen

Indexed keywords

APOPROTEIN; CHLOROPHYLL; HYDROGEN PEROXIDE; RADICAL; SINGLET OXYGEN;

EID: 1642533553     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2003.10.009     Document Type: Article
Times cited : (92)

References (52)
  • 1
    • 0028058268 scopus 로고
    • The light-harvesting chlorophyll a/b-binding proteins
    • Jansson S. The light-harvesting chlorophyll a/b-binding proteins. Biochim. Biophys. Acta. 1184:1994;1-19.
    • (1994) Biochim. Biophys. Acta , vol.1184 , pp. 1-19
    • Jansson, S.1
  • 2
    • 0000575132 scopus 로고    scopus 로고
    • Induction of acclimative proteolysis of the light-harvesting chlorophyll a/b protein of photosystem II in response to elevated light intensities
    • Yang D.H., Webster J., Adam Z., Lindahl M., Andersson B. Induction of acclimative proteolysis of the light-harvesting chlorophyll a/b protein of photosystem II in response to elevated light intensities. Plant Physiol. 118:1998;827-834.
    • (1998) Plant Physiol. , vol.118 , pp. 827-834
    • Yang, D.H.1    Webster, J.2    Adam, Z.3    Lindahl, M.4    Andersson, B.5
  • 3
    • 0037015995 scopus 로고    scopus 로고
    • Involvement of active oxygen species in degradation of light-harvesting proteins under light stresses
    • Zolla L., Rinalducci S. Involvement of active oxygen species in degradation of light-harvesting proteins under light stresses. Biochemistry. 41:2002;14391-14402.
    • (2002) Biochemistry , vol.41 , pp. 14391-14402
    • Zolla, L.1    Rinalducci, S.2
  • 4
    • 0024082182 scopus 로고
    • The dynamic photosynthetic membrane and regulation of solar energy conversion
    • Anderson J.M., Andersson B. The dynamic photosynthetic membrane and regulation of solar energy conversion. Trends Biochem. Sci. 13:1988;351-355.
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 351-355
    • Anderson, J.M.1    Andersson, B.2
  • 5
    • 0025797479 scopus 로고
    • Dynamics of photosynthetic membrane composition and function
    • Melis A. Dynamics of photosynthetic membrane composition and function. Biochim. Biophys. Acta. 1058:1991;87-106.
    • (1991) Biochim. Biophys. Acta , vol.1058 , pp. 87-106
    • Melis, A.1
  • 6
    • 0001696041 scopus 로고    scopus 로고
    • Excitation energy transfer: Functional and dynamic aspects of Lhc (cab) proteins
    • Melis A. Excitation energy transfer: functional and dynamic aspects of Lhc (cab) proteins. Adv. Photosynth. 4:1996;523-538.
    • (1996) Adv. Photosynth. , vol.4 , pp. 523-538
    • Melis, A.1
  • 7
    • 0346823891 scopus 로고    scopus 로고
    • Dynamics of light-harvesting protein stoichiometry adjustment by light quality in chloroplasts
    • S.G. Pandalay. Trivandrum: Transworld Research Network
    • Zolla L., Rinalducci S., Timperio A.M. Dynamics of light-harvesting protein stoichiometry adjustment by light quality in chloroplasts. Pandalay S.G. Recent Research Developments in Bioenergetics. 2000;9-32 Transworld Research Network, Trivandrum.
    • (2000) Recent Research Developments in Bioenergetics , pp. 9-32
    • Zolla, L.1    Rinalducci, S.2    Timperio, A.M.3
  • 8
    • 0030870674 scopus 로고    scopus 로고
    • Novel aspects chlorophyll a/b-binding proteins
    • Bassi R., Sandonà D., Croce R. Novel aspects chlorophyll a/b-binding proteins. Physiol. Plant. 100:1997;769-779.
    • (1997) Physiol. Plant. , vol.100 , pp. 769-779
    • Bassi, R.1    Sandonà, D.2    Croce, R.3
  • 9
    • 0030767058 scopus 로고    scopus 로고
    • Proteolytic activities and proteases of plant chloroplasts
    • Andersson B., Aro E.-M. Proteolytic activities and proteases of plant chloroplasts. Physiol. Plant. 100:1997;780-793.
    • (1997) Physiol. Plant , vol.100 , pp. 780-793
    • Andersson, B.1    Aro, E.-M.2
  • 10
    • 0001848758 scopus 로고
    • Regulation of photosynthetic light energy capture, conversion, and dissipation in leaves of higher plants
    • E.D. Schulze, & M. Caldwell. New York: Springer
    • Björkman O., Demmig-Adams B. Regulation of photosynthetic light energy capture, conversion, and dissipation in leaves of higher plants. Schulze E.D., Caldwell M. Ecological Studies. 1994;17-47 Springer, New York.
    • (1994) Ecological Studies , pp. 17-47
    • Björkman, O.1    Demmig-Adams, B.2
  • 11
    • 0003050958 scopus 로고
    • Photoinhibition of photosynthesis induced by visible light
    • Powles S.B. Photoinhibition of photosynthesis induced by visible light. Annu. Rev. Plant Physiol. 35:1984;15-44.
    • (1984) Annu. Rev. Plant Physiol. , vol.35 , pp. 15-44
    • Powles, S.B.1
  • 12
    • 0000226607 scopus 로고
    • Dynamics of photosystem II: Mechanism of photoinhibition and recovery processes
    • J. Barber. Amsterdam: Elsevier
    • Prasil O., Adir N., Ohad I. Dynamics of photosystem II: mechanism of photoinhibition and recovery processes. Barber J. The Photosystems: Structure, Function and Molecular Biology. 1992;295-348 Elsevier, Amsterdam.
    • (1992) The Photosystems: Structure, Function and Molecular Biology , pp. 295-348
    • Prasil, O.1    Adir, N.2    Ohad, I.3
  • 13
    • 0028801517 scopus 로고
    • Thylakoid-bound proteolytic activity vs. LHCII apoprotein in bean
    • Anastassiou R., Argyroudi-Akoyunoglou J.H. Thylakoid-bound proteolytic activity vs. LHCII apoprotein in bean. Photosynth. Res. 43:1995;241-250.
    • (1995) Photosynth. Res. , vol.43 , pp. 241-250
    • Anastassiou, R.1    Argyroudi-Akoyunoglou, J.H.2
  • 14
    • 0011088692 scopus 로고    scopus 로고
    • Implications of a developmental-stage-dependent thylakoid-bound protease in the stabilization of the light-harvesting pigment-protein complex serving photosystem II during thylakoid biogenesis in Red Kidney Bean
    • Tziveleka L.-A., Argyroudi-Akoyunoglou J.H. Implications of a developmental-stage-dependent thylakoid-bound protease in the stabilization of the light-harvesting pigment-protein complex serving photosystem II during thylakoid biogenesis in Red Kidney Bean. Plant Physiol. 117:1998;961-970.
    • (1998) Plant Physiol. , vol.117 , pp. 961-970
    • Tziveleka, L.-A.1    Argyroudi-Akoyunoglou, J.H.2
  • 15
    • 0037015689 scopus 로고    scopus 로고
    • Proteolytic activity against the light-harvesting complex and the D1/D2 core proteins of Photosystem II in close association to the light-harvesting complex II trimer
    • Georgakopoulos J.H., Sokolenko A., Arkas M., Sofou G., Herrmann R.G., Argyroudi-Akoyunoglou J.H. Proteolytic activity against the light-harvesting complex and the D1/D2 core proteins of Photosystem II in close association to the light-harvesting complex II trimer. Biochim. Biophys. Acta. 1556:2002;53-64.
    • (2002) Biochim. Biophys. Acta , vol.1556 , pp. 53-64
    • Georgakopoulos, J.H.1    Sokolenko, A.2    Arkas, M.3    Sofou, G.4    Herrmann, R.G.5    Argyroudi-Akoyunoglou, J.H.6
  • 16
    • 0029034534 scopus 로고
    • Regulatory proteolysis of the major light-harvesting chlorophyll a/b protein of photosystem II by light-induced membrane associated enzymic system
    • Lindahl M., Yang D.-H., Andersson B. Regulatory proteolysis of the major light-harvesting chlorophyll a/b protein of photosystem II by light-induced membrane associated enzymic system. Eur. J. Biochem. 213:1995;503-509.
    • (1995) Eur. J. Biochem. , vol.213 , pp. 503-509
    • Lindahl, M.1    Yang, D.-H.2    Andersson, B.3
  • 17
    • 0035823557 scopus 로고    scopus 로고
    • Identification and characterization of SppA, a novel light-inducible chloroplast protease complex associated with thylakoid membranes
    • Lensch M., Herrmann R.G., Sokolenko A. Identification and characterization of SppA, a novel light-inducible chloroplast protease complex associated with thylakoid membranes. J. Biol. Chem. 276:2001;33645-33651.
    • (2001) J. Biol. Chem. , vol.276 , pp. 33645-33651
    • Lensch, M.1    Herrmann, R.G.2    Sokolenko, A.3
  • 18
    • 0026251573 scopus 로고
    • Definition of type I and type II photosinsetized oxidation
    • Foote C.S. Definition of type I and type II photosinsetized oxidation. Photochem. Photobiol. 54:1991;659.
    • (1991) Photochem. Photobiol. , vol.54 , pp. 659
    • Foote, C.S.1
  • 19
    • 84995066572 scopus 로고
    • Carotenoid triplet state and chlorophyll fluorescence quenching in chloroplasts and subchloroplast particles
    • Mathis P., Butler W.L., Satoh K. Carotenoid triplet state and chlorophyll fluorescence quenching in chloroplasts and subchloroplast particles. Photochem. Photobiol. 30:1979;603-614.
    • (1979) Photochem. Photobiol. , vol.30 , pp. 603-614
    • Mathis, P.1    Butler, W.L.2    Satoh, K.3
  • 20
    • 0028791993 scopus 로고
    • Chlorophyll a and carotenoid triplet states in light-harvesting complex II of higher plants
    • Peterman E.J.G., Dukker F.M., van Grondelle R., van Amerongen H. Chlorophyll a and carotenoid triplet states in light-harvesting complex II of higher plants. Biophys. J. 69:1995;2670-2678.
    • (1995) Biophys. J. , vol.69 , pp. 2670-2678
    • Peterman, E.J.G.1    Dukker, F.M.2    Van Grondelle, R.3    Van Amerongen, H.4
  • 21
    • 0032512418 scopus 로고    scopus 로고
    • The influence of aggregation on triplet formation in light-harvesting chlorophyll a/b pigment-protein complex II of green plants
    • Barzda V., Peterman E.J., van Grondelle R., van Amerongen H. The influence of aggregation on triplet formation in light-harvesting chlorophyll a/b pigment-protein complex II of green plants. Biochemistry. 37:1998;546-551.
    • (1998) Biochemistry , vol.37 , pp. 546-551
    • Barzda, V.1    Peterman, E.J.2    Van Grondelle, R.3    Van Amerongen, H.4
  • 22
    • 0001806046 scopus 로고
    • FDMR of carotenoid and chlorophyll triplets in light-harvesting complex LHCII of spinach
    • Carbonera D., Giacometti G., Agostini G. FDMR of carotenoid and chlorophyll triplets in light-harvesting complex LHCII of spinach. Appl. Magn. Reson. 3:1992;859-872.
    • (1992) Appl. Magn. Reson. , vol.3 , pp. 859-872
    • Carbonera, D.1    Giacometti, G.2    Agostini, G.3
  • 23
  • 24
    • 0028819374 scopus 로고
    • Triplet and fluorescing states of the CP47 antenna complex of photosystem II studied as a function of temperature
    • Groot M.-L., Peterman E.J.G., van Stokkum I.H.M., Dekker J.P., van Grondelle R. Triplet and fluorescing states of the CP47 antenna complex of photosystem II studied as a function of temperature. Biophys. J. 68:1995;281-290.
    • (1995) Biophys. J. , vol.68 , pp. 281-290
    • Groot, M.-L.1    Peterman, E.J.G.2    Van Stokkum, I.H.M.3    Dekker, J.P.4    Van Grondelle, R.5
  • 25
    • 0033427070 scopus 로고    scopus 로고
    • Isolation and characterization of chloroplast Photosystem II antenna of spinach by reversed-phase liquid chromatography
    • Zolla L., Timperio A.M., Testi M.G., Bianchetti M., Bassi R., Manera F., Corradini D. Isolation and characterization of chloroplast Photosystem II antenna of spinach by reversed-phase liquid chromatography. Photosynth. Res. 61:1999;281-290.
    • (1999) Photosynth. Res. , vol.61 , pp. 281-290
    • Zolla, L.1    Timperio, A.M.2    Testi, M.G.3    Bianchetti, M.4    Bassi, R.5    Manera, F.6    Corradini, D.7
  • 26
    • 0030819559 scopus 로고    scopus 로고
    • Rapid resolution by reversed-phase high-performance liquid chromatography of the thylakoid membrane proteins of the photosystem II light-harvesting complex
    • Zolla L., Bianchetti M., Timperio A.M., Corradini D. Rapid resolution by reversed-phase high-performance liquid chromatography of the thylakoid membrane proteins of the photosystem II light-harvesting complex. J. Chromatogr., A. 779:1997;131-138.
    • (1997) J. Chromatogr., a , vol.779 , pp. 131-138
    • Zolla, L.1    Bianchetti, M.2    Timperio, A.M.3    Corradini, D.4
  • 27
    • 0002204357 scopus 로고
    • Photosensitized oxidation and singlet oxygen: Consequences in biological systems
    • W.A. Prior. New York: Academic Press
    • Foote C.S. Photosensitized oxidation and singlet oxygen: consequences in biological systems. Prior W.A. Free Radicals in Biology. 1976;85-133 Academic Press, New York.
    • (1976) Free Radicals in Biology , pp. 85-133
    • Foote, C.S.1
  • 28
    • 0025836735 scopus 로고
    • Production of singlet oxygen-derived hydroxyl radical adducts during merocyanine-540-mediated photosensitization: Analysis by ESR-spin trapping and HPLC with electrochemical detection
    • Feix J.B., Kalyanaraman B. Production of singlet oxygen-derived hydroxyl radical adducts during merocyanine-540-mediated photosensitization: analysis by ESR-spin trapping and HPLC with electrochemical detection. Arch. Biochem. Biophys. 291:1991;43-51.
    • (1991) Arch. Biochem. Biophys. , vol.291 , pp. 43-51
    • Feix, J.B.1    Kalyanaraman, B.2
  • 29
    • 0024394741 scopus 로고
    • Polyamines as radical scavengers and protectants against ozone damage
    • Bors W., Langebartels C., Michel C., Sandermann H. Jr. Polyamines as radical scavengers and protectants against ozone damage. Phytochemistry. 28:1989;1589-1595.
    • (1989) Phytochemistry , vol.28 , pp. 1589-1595
    • Bors, W.1    Langebartels, C.2    Michel, C.3    Sandermann, H.Jr.4
  • 30
    • 84989674924 scopus 로고
    • A spin trapping study of the photochemistry of 5,5-dimethyl-1-pyrroline N-oxide (DMPO)
    • Chignell C.F., Motten A.G., Sik R.H., Parker C.E., Reszka K. A spin trapping study of the photochemistry of 5,5-dimethyl-1-pyrroline N-oxide (DMPO). Photochem. Photobiol. 59:1994;5-11.
    • (1994) Photochem. Photobiol. , vol.59 , pp. 5-11
    • Chignell, C.F.1    Motten, A.G.2    Sik, R.H.3    Parker, C.E.4    Reszka, K.5
  • 31
    • 84995104913 scopus 로고
    • On the production of nitroxide radicals by singlet oxygen reaction: An EPR study
    • Lion Y., Gandin E., van de Vorst A. On the production of nitroxide radicals by singlet oxygen reaction: an EPR study. Photochem. Photobiol. 31:1980;305-309.
    • (1980) Photochem. Photobiol. , vol.31 , pp. 305-309
    • Lion, Y.1    Gandin, E.2    Van De Vorst, A.3
  • 32
    • 0023505008 scopus 로고
    • Spin trapping: ESR parameters of spin adducts
    • Buettner G.R. Spin trapping: ESR parameters of spin adducts. Free Radic. Biol. Med. 3:1987;259-303.
    • (1987) Free Radic. Biol. Med. , vol.3 , pp. 259-303
    • Buettner, G.R.1
  • 33
    • 0036591861 scopus 로고    scopus 로고
    • Beta-scission of side-chain alkoxyl radicals on peptides and proteins results in the loss of side-chains as aldehydes and ketones
    • Headlam H.A., Davies M.J. Beta-scission of side-chain alkoxyl radicals on peptides and proteins results in the loss of side-chains as aldehydes and ketones. Free Radic. Biol. Med. 32:2002;1171-1184.
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 1171-1184
    • Headlam, H.A.1    Davies, M.J.2
  • 34
    • 0030004986 scopus 로고    scopus 로고
    • N-[5-Nitro-2-furfurylidene]-3-amino-2-oxazolidinone activation by the human intestinal cell line Caco-2 monitored through noninvasive electron spin resonance spectroscopy
    • Rossi L., De Angelis I., Pedersen J.Z., Marchese E., Stammati A., Rotilio G., Zucco F. N-[5-Nitro-2-furfurylidene]-3-amino-2-oxazolidinone activation by the human intestinal cell line Caco-2 monitored through noninvasive electron spin resonance spectroscopy. Mol. Pharmacol. 49:1996;547-555.
    • (1996) Mol. Pharmacol. , vol.49 , pp. 547-555
    • Rossi, L.1    De Angelis, I.2    Pedersen, J.Z.3    Marchese, E.4    Stammati, A.5    Rotilio, G.6    Zucco, F.7
  • 35
    • 0028131199 scopus 로고
    • Singlet oxygen and free radical production during acceptor- and donor-side-induced photoinhibition. Studies with spin trapping EPR spectroscopy
    • Hideg É., Spetea C., Vass I. Singlet oxygen and free radical production during acceptor- and donor-side-induced photoinhibition. Studies with spin trapping EPR spectroscopy. Biochim. Biophys. Acta. 1186:1994;143-152.
    • (1994) Biochim. Biophys. Acta , vol.1186 , pp. 143-152
    • Hideg, É.1    Spetea, C.2    Vass, I.3
  • 36
    • 0026653397 scopus 로고
    • Relationship between photosensitizing activities and chemical structure of hypocrellin a and B
    • Wang N., Zhang Z. Relationship between photosensitizing activities and chemical structure of hypocrellin A and B. J. Photochem. Photobiol., B. 14:1992;207-217.
    • (1992) J. Photochem. Photobiol., B , vol.14 , pp. 207-217
    • Wang, N.1    Zhang, Z.2
  • 37
    • 0022991969 scopus 로고
    • Photosensitization by antitumor agents. 3: Spectroscopic evidence for superoxide and hydroxyl radical production by anthrapyrazole-sensitized oxidation of NADH
    • Reszka K., Kolodziejczyk P., Lown J.W. Photosensitization by antitumor agents. 3: Spectroscopic evidence for superoxide and hydroxyl radical production by anthrapyrazole-sensitized oxidation of NADH. J. Free Radic. Biol. Med. 2:1986;267-274.
    • (1986) J. Free Radic. Biol. Med. , vol.2 , pp. 267-274
    • Reszka, K.1    Kolodziejczyk, P.2    Lown, J.W.3
  • 38
    • 0032950791 scopus 로고    scopus 로고
    • Electron spin resonance studies on photosensitized formation of hydroxyl radical by C-phycocyanin from Spirulina platensis
    • Zhang S.P., Xie J., Zhang J.P., Zhao J.Q., Jiang L.J. Electron spin resonance studies on photosensitized formation of hydroxyl radical by C-phycocyanin from Spirulina platensis. Biochim. Biophys. Acta. 1426:1999;205-211.
    • (1999) Biochim. Biophys. Acta , vol.1426 , pp. 205-211
    • Zhang, S.P.1    Xie, J.2    Zhang, J.P.3    Zhao, J.Q.4    Jiang, L.J.5
  • 39
    • 0029197108 scopus 로고
    • Singlet oxygen is not produced in photosystem I under photoinhibitory conditions
    • Hideg É., Vass I. Singlet oxygen is not produced in photosystem I under photoinhibitory conditions. Photochem. Photobiol. 62:1995;949-952.
    • (1995) Photochem. Photobiol. , vol.62 , pp. 949-952
    • Hideg, É.1    Vass, I.2
  • 40
    • 0034493939 scopus 로고    scopus 로고
    • Photosensitized formation of singlet oxygen by phycobiliproteins in neutral aqueous solutions
    • Zhang S.P., Zhao J.Q., Jiang L.J. Photosensitized formation of singlet oxygen by phycobiliproteins in neutral aqueous solutions. Free Radic. Res. 33:2000;489-496.
    • (2000) Free Radic. Res. , vol.33 , pp. 489-496
    • Zhang, S.P.1    Zhao, J.Q.2    Jiang, L.J.3
  • 41
    • 0026597716 scopus 로고
    • Two sites of primary degradation of the D1-protein induced by acceptor or donor side photoinhibition 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 photoinhibition in photosystem II core complexes. FEBS Lett. 301:1992;246-252.
    • (1992) FEBS Lett. , vol.301 , pp. 246-252
    • De Las Rivas, J.1    Andersson, B.2    Barber, J.3
  • 42
    • 0025965385 scopus 로고
    • Fast oxygen-independent degradation of the D1 reaction center protein in photosystem II
    • Jegerschoeld C., Styring S. Fast oxygen-independent degradation of the D1 reaction center protein in photosystem II. FEBS Lett. 280:1991;87-90.
    • (1991) FEBS Lett. , vol.280 , pp. 87-90
    • Jegerschoeld, C.1    Styring, S.2
  • 43
    • 0034698478 scopus 로고    scopus 로고
    • Resolution and identification of the protein components of the photosystem II antenna system of higher plants by reversed-phase liquid chromatography with electrospray mass-spectrometric detection
    • Corradini D., Huber C.G., Timperio A.M., Zolla L. Resolution and identification of the protein components of the photosystem II antenna system of higher plants by reversed-phase liquid chromatography with electrospray mass-spectrometric detection. J. Chromatogr., A. 886:2000;111-121.
    • (2000) J. Chromatogr., a , vol.886 , pp. 111-121
    • Corradini, D.1    Huber, C.G.2    Timperio, A.M.3    Zolla, L.4
  • 45
    • 0001502848 scopus 로고    scopus 로고
    • Kinetic analysis of the light-induced fluorescence quenching in light-harvesting chlorophyll a/b pigment-protein complex of photosystem II
    • Barzda V., Jennings R.C., Zucchelli G., Garab G. Kinetic analysis of the light-induced fluorescence quenching in light-harvesting chlorophyll a/b pigment-protein complex of photosystem II. Photochem. Photobiol. 70:1999;751-759.
    • (1999) Photochem. Photobiol. , vol.70 , pp. 751-759
    • Barzda, V.1    Jennings, R.C.2    Zucchelli, G.3    Garab, G.4
  • 48
    • 0034616379 scopus 로고    scopus 로고
    • Chlorophyll fluorescence quenching in isolated light harvesting complexes induced by zeaxanthin
    • Wentworth M., Ruban A.V., Horton P. Chlorophyll fluorescence quenching in isolated light harvesting complexes induced by zeaxanthin. FEBS Lett. 471:2000;71-74.
    • (2000) FEBS Lett. , vol.471 , pp. 71-74
    • Wentworth, M.1    Ruban, A.V.2    Horton, P.3
  • 49
    • 0035928839 scopus 로고    scopus 로고
    • Kinetic analysis of nonphotochemical quenching of chlorophyll fluorescence. 2. Isolated light-harvesting complexes
    • Wentworth M., Ruban A.V., Horton P. Kinetic analysis of nonphotochemical quenching of chlorophyll fluorescence. 2. Isolated light-harvesting complexes. Biochemistry. 40:2001;9902-9908.
    • (2001) Biochemistry , vol.40 , pp. 9902-9908
    • Wentworth, M.1    Ruban, A.V.2    Horton, P.3
  • 50
    • 0036808841 scopus 로고    scopus 로고
    • Detection of singlet oxygen and superoxide with fluorescent sensors in leaves under stress by photoinhibition or UV radiation
    • Hideg É., Barta C., Kalai T., Vass I., Hideg K., Asada K. Detection of singlet oxygen and superoxide with fluorescent sensors in leaves under stress by photoinhibition or UV radiation. Plant Cell Physiol. 43:2002;1154-1164.
    • (2002) Plant Cell Physiol. , vol.43 , pp. 1154-1164
    • Hideg, É.1    Barta, C.2    Kalai, T.3    Vass, I.4    Hideg, K.5    Asada, K.6
  • 51
    • 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. 72:2000;508-512.
    • (2000) Photochem. Photobiol. , vol.72 , pp. 508-512
    • Hui, Y.1    Jie, W.2    Carpentier, R.3
  • 52
    • 0036122145 scopus 로고    scopus 로고
    • Functional studies of the Synechocystis phycobilisome organization by high performance liquid chromatography on line with a mass spectrometer
    • Zolla L., Bianchetti M., Rinalducci S. Functional studies of the Synechocystis phycobilisome organization by high performance liquid chromatography on line with a mass spectrometer. Eur. J. Biochem. 269:2002;1534-1542.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1534-1542
    • Zolla, L.1    Bianchetti, M.2    Rinalducci, S.3


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