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Volumn 53, Issue 2-3, 1997, Pages 197-204

Ascorbate in thylakoid lumen as an endogenous electron donor to Photosystem II: Protection of thylakoids from photoinhibition and regeneration of ascorbate in stroma by dehydroascorbate reductase

Author keywords

Donor side induced photoinhibition; Electron spin resonance; Monodehydroascorbate radical; Monodehyroascorbate reductase

Indexed keywords


EID: 0030730520     PISSN: 01668595     EISSN: None     Source Type: Journal    
DOI: 10.1023/a:1005832022204     Document Type: Article
Times cited : (57)

References (40)
  • 1
    • 0000774546 scopus 로고
    • Light-dependent reduction of dehydroascorbate and uptake of exogeneous ascorbate by spinach chloroplasts
    • Anderson JW, Foyer C and Walker D (1983) Light-dependent reduction of dehydroascorbate and uptake of exogeneous ascorbate by spinach chloroplasts. Planta 158: 442-450
    • (1983) Planta , vol.158 , pp. 442-450
    • Anderson, J.W.1    Foyer, C.2    Walker, D.3
  • 2
    • 0029109619 scopus 로고
    • Decrease in activity of glutathione reductase enhances paraquat sensitivity in transgenic Nicotiana tabacum
    • Aono M, Saji H, Fujiyama K, Sugita M, Kondo N and Tanaka K (1995a) Decrease in activity of glutathione reductase enhances paraquat sensitivity in transgenic Nicotiana tabacum. Plant Physiol 107: 645-648
    • (1995) Plant Physiol , vol.107 , pp. 645-648
    • Aono, M.1    Saji, H.2    Fujiyama, K.3    Sugita, M.4    Kondo, N.5    Tanaka, K.6
  • 3
    • 0029582869 scopus 로고
    • Paraquat tolerance of transgenic Nicotiana tabacum with enhanced activities of glutathione reductase and Superoxide dismutase
    • Aono M, Saji H, Sakamoto A, Tanaka K, Kondo N and Tanaka K (1995b) Paraquat tolerance of transgenic Nicotiana tabacum with enhanced activities of glutathione reductase and Superoxide dismutase. Plant Cell Physiol 36: 1687-1691
    • (1995) Plant Cell Physiol , vol.36 , pp. 1687-1691
    • Aono, M.1    Saji, H.2    Sakamoto, A.3    Tanaka, K.4    Kondo, N.5    Tanaka, K.6
  • 4
    • 0027199986 scopus 로고
    • Photoinhibition of Photosystem II. Inactivation, protein damage and turnover
    • Aro E-M, Virgin I and Andersson B (1993) Photoinhibition of Photosystem II. Inactivation, protein damage and turnover. Biochim Biophys Acta 1143: 113-134
    • (1993) Biochim Biophys Acta , vol.1143 , pp. 113-134
    • Aro, E.-M.1    Virgin, I.2    Andersson, B.3
  • 5
    • 84983392009 scopus 로고
    • Ascorbate peroxidase - A hydrogen peroxide scavenging enzyme in plants
    • Asada K (1992) Ascorbate peroxidase - a hydrogen peroxide scavenging enzyme in plants. Physiol Plant 85: 235-241
    • (1992) Physiol Plant , vol.85 , pp. 235-241
    • Asada, K.1
  • 6
    • 0002844238 scopus 로고
    • Production and action of active oxygen species in photosynthetic tissues
    • Foyer CH and Mullineaux PM (eds) CRC Press, Boca Raton, FL
    • Asada K (1994) Production and action of active oxygen species in photosynthetic tissues. In: Foyer CH and Mullineaux PM (eds) Causes of Photooxidative Stress and Amelioration of Defense Systems in Plants, pp 77-104. CRC Press, Boca Raton, FL
    • (1994) Causes of Photooxidative Stress and Amelioration of Defense Systems in Plants , pp. 77-104
    • Asada, K.1
  • 7
    • 0001307047 scopus 로고
    • Mechanism of disproportionation of ascorbate radicals
    • Bielski BHJ, Allen AO and Schwarz HA (1981) Mechanism of disproportionation of ascorbate radicals. J Am Chem Soc 103: 3516-3518
    • (1981) J Am Chem Soc , vol.103 , pp. 3516-3518
    • Bielski, B.H.J.1    Allen, A.O.2    Schwarz, H.A.3
  • 8
    • 0025748045 scopus 로고
    • Photoinhibition of hydroxylamine-extracted Photosystem II membranes: Identification of the sites of photodamage
    • Blubaugh DJ, Atamian M, Babcock GT, Golbeck JH and Cheniae GM (1991) Photoinhibition of hydroxylamine-extracted Photosystem II membranes: Identification of the sites of photodamage. Biochemistry 30: 7586-7597
    • (1991) Biochemistry , vol.30 , pp. 7586-7597
    • Blubaugh, D.J.1    Atamian, M.2    Babcock, G.T.3    Golbeck, J.H.4    Cheniae, G.M.5
  • 9
    • 34249758236 scopus 로고
    • Regulation of violaxanthin de-epoxidase activity by pH and ascorbate concentration
    • Bratt CE, Arvidsson P-O, Carlsson M and Åkerlund H-E(1995) Regulation of violaxanthin de-epoxidase activity by pH and ascorbate concentration. Photosynth Res 45: 169-175
    • (1995) Photosynth Res , vol.45 , pp. 169-175
    • Bratt, C.E.1    Arvidsson, P.-O.2    Carlsson, M.3    Åkerlund, H.-E.4
  • 10
    • 0026496536 scopus 로고
    • Photoinhibition of hydroxylamine-extracted Photosystem II membranes: Studies of the mechanism
    • Chen G-X, Kazimir J. and Cheniae G M (1992) Photoinhibition of hydroxylamine-extracted Photosystem II membranes: Studies of the mechanism. Biochemistry 31: 11072-11083
    • (1992) Biochemistry , vol.31 , pp. 11072-11083
    • Chen, G.-X.1    Kazimir, J.2    Cheniae, G.M.3
  • 11
    • 0028938833 scopus 로고
    • Superoxide contributes to the rapid inactivation of specific secondary donors of the Photosystem II reaction center duing photodamage of manganese-depleted Photosystem II membranes
    • Chen G-X, Blubaugh DJ, Homann JH, Golbeck JH and Cheniae GM (1995) Superoxide contributes to the rapid inactivation of specific secondary donors of the Photosystem II reaction center duing photodamage of manganese-depleted Photosystem II membranes. Biochemistry 34: 2317-2332.
    • (1995) Biochemistry , vol.34 , pp. 2317-2332
    • Chen, G.-X.1    Blubaugh, D.J.2    Homann, J.H.3    Golbeck, J.H.4    Cheniae, G.M.5
  • 12
    • 0025187594 scopus 로고
    • Carotenoids and photoprotection in plants: A role for the xanthophyll zeaxanthin
    • Demmig-Adams, B (1990) Carotenoids and photoprotection in plants: A role for the xanthophyll zeaxanthin. Biochim Biophys Acta 1020: 1-24
    • (1990) Biochim Biophys Acta , vol.1020 , pp. 1-24
    • Demmig-Adams, B.1
  • 13
    • 0030062410 scopus 로고    scopus 로고
    • Xanthophyll cycle and light stress in nature: Uniform response to excess direct sunlight among plant species
    • Demmig-Adams B and Adams W W III (1996) Xanthophyll cycle and light stress in nature: Uniform response to excess direct sunlight among plant species. Planta 198: 460-470
    • (1996) Planta , vol.198 , pp. 460-470
    • Demmig-Adams, B.1    Adams III, W.W.2
  • 14
    • 0001839795 scopus 로고
    • Two sites of photoinhibition of the electron transfer in oxygen evolving and Tris-treated PS II membrane fragments from spinach
    • Eckert H-J, Geiken B, Bernarding J, Napiwotzky A, Eichler H-J and Renger G. (1991) Two sites of photoinhibition of the electron transfer in oxygen evolving and Tris-treated PS II membrane fragments from spinach. Photosynth Res 27: 97-108
    • (1991) Photosynth Res , vol.27 , pp. 97-108
    • Eckert, H.-J.1    Geiken, B.2    Bernarding, J.3    Napiwotzky, A.4    Eichler, H.-J.5    Renger, G.6
  • 15
    • 0000489441 scopus 로고
    • Purification and properties of dehydroascorbate reductase from spinach leaves
    • Foyer CH and Halliwell B (1977) Purification and properties of dehydroascorbate reductase from spinach leaves. Phytochemistry 16: 1347-1350
    • (1977) Phytochemistry , vol.16 , pp. 1347-1350
    • Foyer, C.H.1    Halliwell, B.2
  • 16
    • 0028934243 scopus 로고
    • Formation and decay of monodehydroascorbate radicals in illuminated thylakoids as determined by ESR spectroscopy
    • Grace S, Pace R and Wydrzynski T (1995) Formation and decay of monodehydroascorbate radicals in illuminated thylakoids as determined by ESR spectroscopy. Biochim Biophyis Acta 1229: 155-165
    • (1995) Biochim Biophyis Acta , vol.1229 , pp. 155-165
    • Grace, S.1    Pace, R.2    Wydrzynski, T.3
  • 17
    • 0030425635 scopus 로고    scopus 로고
    • Monodehydroascorbate radical detected by electron paramagnetic resonance spectrometry is a sensitve probe of oxidative stress in intact leaves
    • Heber U, Miyake C, Mano J, Ohno C. and Asada K (1996) Monodehydroascorbate radical detected by electron paramagnetic resonance spectrometry is a sensitve probe of oxidative stress in intact leaves. Plant Cell Physiol 37: 1066-1072
    • (1996) Plant Cell Physiol , vol.37 , pp. 1066-1072
    • Heber, U.1    Miyake, C.2    Mano, J.3    Ohno, C.4    Asada, K.5
  • 18
    • 0015904985 scopus 로고
    • Alkalization of the chloroplast stroma caused by light-dependent proton flux into the thylakoid space
    • Heldt HW, Werden K, Milovancev M and Geller G (1973) Alkalization of the chloroplast stroma caused by light-dependent proton flux into the thylakoid space. Biochim Biophys Acta 314: 224-241
    • (1973) Biochim Biophys Acta , vol.314 , pp. 224-241
    • Heldt, H.W.1    Werden, K.2    Milovancev, M.3    Geller, G.4
  • 19
    • 0002458223 scopus 로고
    • Purification of dehydroascorbate reductase from spinach and its characterization as a thiol enzyme
    • Hossain MA, and Asada K (1984) Purification of dehydroascorbate reductase from spinach and its characterization as a thiol enzyme. Plant Cell Physiol 25: 85-92
    • (1984) Plant Cell Physiol , vol.25 , pp. 85-92
    • Hossain, M.A.1    Asada, K.2
  • 20
    • 0000918942 scopus 로고
    • Monodehydroascorbate reductase in spinach chloroplasts and its participation in regeneration of ascorbate for scavenging hydrogen peroxide
    • Hossain MA, Nakano Y and Asada K (1984) Monodehydroascorbate reductase in spinach chloroplasts and its participation in regeneration of ascorbate for scavenging hydrogen peroxide. Plant Cell Physiol 25: 385-395
    • (1984) Plant Cell Physiol , vol.25 , pp. 385-395
    • Hossain, M.A.1    Nakano, Y.2    Asada, K.3
  • 21
    • 0014143081 scopus 로고
    • Ascorbate-supported NADP photoreduction by heated Euglena chloroplasts
    • Katoh S and San Pietro A (1967) Ascorbate-supported NADP photoreduction by heated Euglena chloroplasts. Arch Biochem Biophys 122: 144-152
    • (1967) Arch Biochem Biophys , vol.122 , pp. 144-152
    • Katoh, S.1    San Pietro, A.2
  • 22
    • 0030994762 scopus 로고    scopus 로고
    • Purification and characterization of dehydroascrobate reductase from rice
    • Kato Y, Urano J, Maki Y and Ushimaru T (1997) Purification and characterization of dehydroascrobate reductase from rice. Plant Cell Physiol 38: 173-178
    • (1997) Plant Cell Physiol , vol.38 , pp. 173-178
    • Kato, Y.1    Urano, J.2    Maki, Y.3    Ushimaru, T.4
  • 23
    • 0002179049 scopus 로고
    • Photoinactivation of the reactivation capacity of Photosystem II in pea subchloroplast particles after a complete removal of manganese
    • Klimov VV, Shafiev MA and Allakhverdiev SI (1990) Photoinactivation of the reactivation capacity of Photosystem II in pea subchloroplast particles after a complete removal of manganese. Photosynth Res 23: 59-65
    • (1990) Photosynth Res , vol.23 , pp. 59-65
    • Klimov, V.V.1    Shafiev, M.A.2    Allakhverdiev, S.I.3
  • 24
    • 0028825699 scopus 로고
    • A direct demonstration of the catalytic action of monodehydroascorbate reductase by pulse radiolysis
    • Kobayashi K, Tagawa S, Sano S and Asada K (1995) A direct demonstration of the catalytic action of monodehydroascorbate reductase by pulse radiolysis. J Biol Chem 270: 27551-27554
    • (1995) J Biol Chem , vol.270 , pp. 27551-27554
    • Kobayashi, K.1    Tagawa, S.2    Sano, S.3    Asada, K.4
  • 25
    • 77957181306 scopus 로고
    • Thylakoid-bound ascorbate peroxidase in spinach chloroplasts and photoreduction of its primary oxidation product monodehydroascorbate radicals in thylakoids
    • Miyake C and Asada K (1992) Thylakoid-bound ascorbate peroxidase in spinach chloroplasts and photoreduction of its primary oxidation product monodehydroascorbate radicals in thylakoids. Plant Cell Physiol 33: 541-553
    • (1992) Plant Cell Physiol , vol.33 , pp. 541-553
    • Miyake, C.1    Asada, K.2
  • 26
    • 0028155106 scopus 로고
    • Ferredoxin-dependent photoreduction of the monodehydroascorbate radicals in spinach thylakoids
    • Miyake C and Asada K (1994) Ferredoxin-dependent photoreduction of the monodehydroascorbate radicals in spinach thylakoids. Plant Cell Physiol 35: 539-549
    • (1994) Plant Cell Physiol , vol.35 , pp. 539-549
    • Miyake, C.1    Asada, K.2
  • 27
    • 0006802141 scopus 로고    scopus 로고
    • A new assay of ascorbate peroxidase using the coupled system with monodehydroascorbate radical reductase
    • Oblinger C, Burner U, Ebermann R, Penel C and Greppin H (eds) University of Agriculture, Vienna and University of Geneva
    • Miyake C, Sano S and Asada K (1996) A new assay of ascorbate peroxidase using the coupled system with monodehydroascorbate radical reductase. In: Oblinger C, Burner U, Ebermann R, Penel C and Greppin H (eds) Plant Peroxidases Biochemistry and Physiology, pp 386-389. University of Agriculture, Vienna and University of Geneva
    • (1996) Plant Peroxidases Biochemistry and Physiology , pp. 386-389
    • Miyake, C.1    Sano, S.2    Asada, K.3
  • 28
    • 0000629113 scopus 로고
    • Mehler-peroxidase reaction mediates zeaxanthin formation and zeacanthin-related fluorescence quenching in intact chloroplasts
    • Neubauer C and Yamamoto HY (1992) Mehler-peroxidase reaction mediates zeaxanthin formation and zeacanthin-related fluorescence quenching in intact chloroplasts. Plant Physiol 99: 1354-1361
    • (1992) Plant Physiol , vol.99 , pp. 1354-1361
    • Neubauer, C.1    Yamamoto, H.Y.2
  • 30
    • 0019318635 scopus 로고
    • Cyclic photophosphorylation reactions catalyzed by ferredoxin, methyl viologen and anthraquinone sulfonate. Use of photochemical reactions to optimize redox poising
    • Robinson HH and Yocum CF (1980) Cyclic photophosphorylation reactions catalyzed by ferredoxin, methyl viologen and anthraquinone sulfonate. Use of photochemical reactions to optimize redox poising. Biochim Biophys Acta 590: 97-106
    • (1980) Biochim Biophys Acta , vol.590 , pp. 97-106
    • Robinson, H.H.1    Yocum, C.F.2
  • 31
    • 0029089221 scopus 로고
    • Molecular characterization of monodehydroascorbate radical reductase from cucumber highly expressed in Escherichia coli
    • Sano S, Miyake C, Mikami B and Asada K (1995) Molecular characterization of monodehydroascorbate radical reductase from cucumber highly expressed in Escherichia coli. J Biol Chem 270: 21354-31361
    • (1995) J Biol Chem , vol.270 , pp. 21354-31361
    • Sano, S.1    Miyake, C.2    Mikami, B.3    Asada, K.4
  • 32
    • 0000191606 scopus 로고
    • 2-dependent electron flow, membrane energization and the mechanism of non-photochemical quenching of chlorophyll fluorescence
    • 2-dependent electron flow, membrane energization and the mechanism of non-photochemical quenching of chlorophyll fluorescence. Photosynth Res 25: 279-293
    • (1990) Photosynth Res , vol.25 , pp. 279-293
    • Schreiber, U.1    Neubauer, C.2
  • 33
    • 0028136613 scopus 로고
    • A novel dehydroascorbate reductase from spinach chloroplasts homologous to plant trypsin inhibitor
    • Trümper S, Follmann H and Häberlein I (1994) A novel dehydroascorbate reductase from spinach chloroplasts homologous to plant trypsin inhibitor. FEBS Lett 352: 159-162
    • (1994) FEBS Lett , vol.352 , pp. 159-162
    • Trümper, S.1    Follmann, H.2    Häberlein, I.3
  • 34
    • 0030015611 scopus 로고    scopus 로고
    • UV-B-induced inhibition of Photosystem II electron transport studied by EPR and chlorophyll fluorescence. Impairment of donor and acceptor side components
    • Vass I, Sass L, Spetea C, Bakou A Ghanotakis DF and Petrouleas V (1996) UV-B-induced inhibition of Photosystem II electron transport studied by EPR and chlorophyll fluorescence. Impairment of donor and acceptor side components. Biochemistry 35: 8964-8973
    • (1996) Biochemistry , vol.35 , pp. 8964-8973
    • Vass, I.1    Sass, L.2    Spetea, C.3    Bakou, A.4    Ghanotakis, D.F.5    Petrouleas, V.6
  • 36
    • 0008126240 scopus 로고
    • Effect of cold treatments on the binding stability of Photosystem II extrinsic proteins and an associated increase in susceptibility to photoinhibition
    • Wang W-Q, Chapman DJ and Barber J (1992) Effect of cold treatments on the binding stability of Photosystem II extrinsic proteins and an associated increase in susceptibility to photoinhibition. Plant Physiol 99: 21-25
    • (1992) Plant Physiol , vol.99 , pp. 21-25
    • Wang, W.-Q.1    Chapman, D.J.2    Barber, J.3
  • 37
    • 0000021893 scopus 로고
    • Physiological significance of the ascorbate regenerating system for the high-light tolerance of chloroplasts
    • Mathis P (ed) Kluwer Academic Publishers, Dordrecht, the Netherlands
    • Yamasaki H, Heshiki R, Yamasu T, Sakihama Y and Ikehara N (1995) Physiological significance of the ascorbate regenerating system for the high-light tolerance of chloroplasts. In: Mathis P (ed) Photosynthesis: From Light to Biosphere, Vol IV, pp 291-294. Kluwer Academic Publishers, Dordrecht, the Netherlands
    • (1995) Photosynthesis: from Light to Biosphere , vol.4 , pp. 291-294
    • Yamasaki, H.1    Heshiki, R.2    Yamasu, T.3    Sakihama, Y.4    Ikehara, N.5
  • 38
    • 0014373433 scopus 로고
    • Photoreduction and photophosphorylation with Tris-washed chloroplasts
    • Yamashita T and Butler WL (1968) Photoreduction and photophosphorylation with Tris-washed chloroplasts. Plant Physiol 43: 1978-1986
    • (1968) Plant Physiol , vol.43 , pp. 1978-1986
    • Yamashita, T.1    Butler, W.L.2
  • 39
    • 0014570319 scopus 로고
    • Photooxidation by Photosystem H of Tris-washed chloroplasts
    • Yamashita T and Butler W (1969) Photooxidation by Photosystem H of Tris-washed chloroplasts. Plant Physiol 44: 1342-1346
    • (1969) Plant Physiol , vol.44 , pp. 1342-1346
    • Yamashita, T.1    Butler, W.2
  • 40
    • 0019320131 scopus 로고
    • Photosystem II oxidation of charged electron donors. Surface charge effects
    • Yerkes CT and Babcock GT (1980) Photosystem II oxidation of charged electron donors. Surface charge effects. Biochim Biophys Acta 590: 360-372
    • (1980) Biochim Biophys Acta , vol.590 , pp. 360-372
    • Yerkes, C.T.1    Babcock, G.T.2


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