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Volumn 153, Issue 2, 2000, Pages 145-154

Antioxidant responses of cucumber (Cucumis sativus) to photoinhibition and oxidative stress induced by norflurazon under high and low PPFDs

Author keywords

Antioxidant enzymes; Cucumber (Cucumis sativus); Non photochemical quenching; Norflurazon; Oxidative stress; Xanthophylls

Indexed keywords

ANTIOXIDANT; CAROTENOID; CHLOROPHYLL; GLUTATHIONE REDUCTASE; NORFLURAZON; PEROXIDASE; SUPEROXIDE DISMUTASE; ZEAXANTHIN;

EID: 0343963213     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-9452(99)00259-9     Document Type: Article
Times cited : (75)

References (43)
  • 1
    • 0002946269 scopus 로고
    • Photosystem II: Molecular organisation, function, and acclimation
    • Andersson B., Styring S. Photosystem II: molecular organisation, function, and acclimation. Curr. Top Bioenerg. 16:1991;1-81.
    • (1991) Curr. Top Bioenerg. , vol.16 , pp. 1-81
    • Andersson, B.1    Styring, S.2
  • 2
    • 0027199986 scopus 로고
    • Photoinhibition of photosystem II. Inactivation, protein damage and turnover
    • Aro E.M., Virgin I., Andersson B. Photoinhibition of photosystem II. Inactivation, protein damage and turnover. Biochim. Biophys. Acta. 1143:1993;113-134.
    • (1993) Biochim. Biophys. Acta , vol.1143 , pp. 113-134
    • Aro, E.M.1    Virgin, I.2    Andersson, B.3
  • 3
    • 0002844238 scopus 로고
    • Production and action of active oxygen species in photosynthetic tissues
    • C.H. Foyer, & P.M. Mullineaux. Boca Raton, FL: CRC Press
    • Asada K. Production and action of active oxygen species in photosynthetic tissues. Foyer C.H., Mullineaux P.M. Causes of Photooxidative Stress and Amelioration of Defence Systems in Plants. 1994;77-104 CRC Press, Boca Raton, FL.
    • (1994) Causes of Photooxidative Stress and Amelioration of Defence Systems in Plants , pp. 77-104
    • Asada, K.1
  • 4
    • 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
  • 5
    • 77957179566 scopus 로고
    • The photoinhibition site of photosystem I in isolated chloroplasts under extremely reducing conditions
    • Inoue K., Fujii Y., Yokoyama E., Matsuura K., Hiyama K., Sakurai H. The photoinhibition site of photosystem I in isolated chloroplasts under extremely reducing conditions. Plant Cell Physiol. 30:1989;65-71.
    • (1989) Plant Cell Physiol. , vol.30 , pp. 65-71
    • Inoue, K.1    Fujii, Y.2    Yokoyama, E.3    Matsuura, K.4    Hiyama, K.5    Sakurai, H.6
  • 6
    • 0027717584 scopus 로고
    • Loss of the trans-thylakoid proton gradient is an early event during photoinhibitory illumination of chloroplast preparations
    • Tjus S.E., Andersson B. Loss of the trans-thylakoid proton gradient is an early event during photoinhibitory illumination of chloroplast preparations. Biochim. Biophys. Acta. 1183:1993;315-322.
    • (1993) Biochim. Biophys. Acta , vol.1183 , pp. 315-322
    • Tjus, S.E.1    Andersson, B.2
  • 9
    • 0002368978 scopus 로고
    • Linear models relating xanthophylls and lumen acidity to non-photochemical fluorescence quenching. Evidence that antheraxanthin explains zeaxanthin-independent quenching
    • Gilmore A.M., Yamamoto H.Y. Linear models relating xanthophylls and lumen acidity to non-photochemical fluorescence quenching. Evidence that antheraxanthin explains zeaxanthin-independent quenching. Photosynth. Res. 35:1993;67-78.
    • (1993) Photosynth. Res. , vol.35 , pp. 67-78
    • Gilmore, A.M.1    Yamamoto, H.Y.2
  • 10
    • 45949114703 scopus 로고
    • Quantum efficiency of photosystem II in relation to energy-dependent quenching of chlorophyll fluorescence
    • Weis E., Berry J.A. Quantum efficiency of photosystem II in relation to energy-dependent quenching of chlorophyll fluorescence. Biochim. Biophys. Acta. 894:1987;198-208.
    • (1987) Biochim. Biophys. Acta , vol.894 , pp. 198-208
    • Weis, E.1    Berry, J.A.2
  • 11
    • 0002298265 scopus 로고
    • Chlorophyll fluorescence as a non-intrusive indicator for rapid assessment of in vivo photosynthesis
    • E.D. Schulze, & M.M. Caldwell. Berlin: Springer-Verlag
    • Schreiber U., Bilger W., Neubauer C. Chlorophyll fluorescence as a non-intrusive indicator for rapid assessment of in vivo photosynthesis. Schulze E.D., Caldwell M.M. Ecology of Photosynthesis. 1994;49-70 Springer-Verlag, Berlin.
    • (1994) Ecology of Photosynthesis , pp. 49-70
    • Schreiber, U.1    Bilger, W.2    Neubauer, C.3
  • 12
    • 34249960486 scopus 로고
    • Role of the xanthophyll cycle in photoprotection elucidated by measurements of light-induced absorbance changes, fluorescence and photosynthesis in leaves of Hedera canariensis
    • Bilger W., Björkman O. Role of the xanthophyll cycle in photoprotection elucidated by measurements of light-induced absorbance changes, fluorescence and photosynthesis in leaves of Hedera canariensis. Photosynth. Res. 25:1990;173-185.
    • (1990) Photosynth. Res. , vol.25 , pp. 173-185
    • Bilger, W.1    Björkman, O.2
  • 13
    • 0342608761 scopus 로고    scopus 로고
    • Mehler reaction: Friend or foe in photosynthesis?
    • Polle A. Mehler reaction: friend or foe in photosynthesis? Botanica Acta. 109:1996;84-89.
    • (1996) Botanica Acta , vol.109 , pp. 84-89
    • Polle, A.1
  • 14
    • 0003121376 scopus 로고
    • The presence of glutathione and glutathione reductase in chloroplasts: A proposed role in ascorbic acid metabolism
    • Foyer C.H., Halliwell B. The presence of glutathione and glutathione reductase in chloroplasts: a proposed role in ascorbic acid metabolism. Planta. 133:1976;21-25.
    • (1976) Planta , vol.133 , pp. 21-25
    • Foyer, C.H.1    Halliwell, B.2
  • 16
    • 0029169262 scopus 로고
    • Factors affecting the enhancement of oxidative stress tolerance in transgenic tobacco overexpressing maganese superoxide dismutase in the chloroplasts
    • Slooten L., Capiau K., Van Camp W., Van Montagu M., Sybesma C., Inzé D. Factors affecting the enhancement of oxidative stress tolerance in transgenic tobacco overexpressing maganese superoxide dismutase in the chloroplasts. Plant Physiol. 107:1995;737-750.
    • (1995) Plant Physiol. , vol.107 , pp. 737-750
    • Slooten, L.1    Capiau, K.2    Van Camp, W.3    Van Montagu, M.4    Sybesma, C.5    Inzé, D.6
  • 17
    • 0030452648 scopus 로고    scopus 로고
    • Enhancement of oxidative stress tolerance in transgenic tobacco plants overproducing Fe-superoxide dismutase in chloroplasts
    • Van Camp W., Capiau K., Van Montagu M., Inzé D., Slooten L. Enhancement of oxidative stress tolerance in transgenic tobacco plants overproducing Fe-superoxide dismutase in chloroplasts. Plant Physiol. 112:1996;1703-1714.
    • (1996) Plant Physiol. , vol.112 , pp. 1703-1714
    • Van Camp, W.1    Capiau, K.2    Van Montagu, M.3    Inzé, D.4    Slooten, L.5
  • 18
    • 0001263618 scopus 로고
    • Overproduction of petunia copper/zinc superoxide dismutase does not confer ozone tolerance in transgenic tobacco
    • Pitcher L.H., Brennan E., Hurley A., Dunsmuir P., Tepperman J.M., Zilinskas B.A. Overproduction of petunia copper/zinc superoxide dismutase does not confer ozone tolerance in transgenic tobacco. Plant Physiol. 97:1991;452-455.
    • (1991) Plant Physiol. , vol.97 , pp. 452-455
    • Pitcher, L.H.1    Brennan, E.2    Hurley, A.3    Dunsmuir, P.4    Tepperman, J.M.5    Zilinskas, B.A.6
  • 19
    • 0030856013 scopus 로고    scopus 로고
    • Over-expression of chloroplast-targeted Mn superoxide dismutase in cotton (Gossypium hirsutum L., cv. (Coker 312) does not alter the reduction of photosynthesis after short exposures to low temperature and high light intensity
    • Payton P., Allen R.D., Trolinder N., Holiday A.S. Over-expression of chloroplast-targeted Mn superoxide dismutase in cotton (Gossypium hirsutum L., cv. (Coker 312) does not alter the reduction of photosynthesis after short exposures to low temperature and high light intensity. Photosynth. Res. 52:1997;233-244.
    • (1997) Photosynth. Res. , vol.52 , pp. 233-244
    • Payton, P.1    Allen, R.D.2    Trolinder, N.3    Holiday, A.S.4
  • 22
    • 84986938772 scopus 로고
    • Mechanism of paraquat tolerance in perennial ryegrass. II. Role of superoxide dismutase, catalase, and peroxidase
    • Harper D.B., Harvey B.M.R. Mechanism of paraquat tolerance in perennial ryegrass. II. Role of superoxide dismutase, catalase, and peroxidase. Plant Cell Environ. 1:1978;211-215.
    • (1978) Plant Cell Environ. , vol.1 , pp. 211-215
    • Harper, D.B.1    Harvey, B.M.R.2
  • 23
    • 0030478735 scopus 로고    scopus 로고
    • Alterations in the antioxidative system of suspension-cultured soybean cells (Glycine max) induced by oxidative stress
    • Knörzer O.C., Durner J., Böger P. Alterations in the antioxidative system of suspension-cultured soybean cells (Glycine max) induced by oxidative stress. Physiol. Plant. 97:1996;388-396.
    • (1996) Physiol. Plant , vol.97 , pp. 388-396
    • Knörzer, O.C.1    Durner, J.2    Böger, P.3
  • 24
    • 0001882412 scopus 로고
    • Inhibition of carotenoid biosynthesis
    • A. Young, & G. Britton. London: Chapman and Hall
    • Bramley P.M. Inhibition of carotenoid biosynthesis. Young A., Britton G. Carotenoids in Photosynthesis. 1993;127-159 Chapman and Hall, London.
    • (1993) Carotenoids in Photosynthesis , pp. 127-159
    • Bramley, P.M.1
  • 25
    • 34250126784 scopus 로고
    • Continuous recording of photochemical and non-photochemical chlorophyll fluorescence quenching with a new type of modulation fluorometer
    • Schreiber U., Schliwa U., Bilger W. Continuous recording of photochemical and non-photochemical chlorophyll fluorescence quenching with a new type of modulation fluorometer. Photosynth. Res. 10:1986;51-62.
    • (1986) Photosynth. Res. , vol.10 , pp. 51-62
    • Schreiber, U.1    Schliwa, U.2    Bilger, W.3
  • 26
    • 85023704649 scopus 로고
    • The relationship between the quantum yield of photosynthetic electron transport and quenching of chlorophyll fluorescence
    • Genty B., Briantais J.M., Baker N. The relationship between the quantum yield of photosynthetic electron transport and quenching of chlorophyll fluorescence. Biochim. Biophys. Acta. 990:1989;87-92.
    • (1989) Biochim. Biophys. Acta , vol.990 , pp. 87-92
    • Genty, B.1    Briantais, J.M.2    Baker, N.3
  • 27
    • 0026692945 scopus 로고
    • Truncation of the COOH-terminal domain of the psbE gene product in Synechocystis sp. PCC 6803: Requirements for Photosystem II assembly and function
    • Tae G.S., Cramer W.A. Truncation of the COOH-terminal domain of the psbE gene product in Synechocystis sp. PCC 6803: requirements for Photosystem II assembly and function. Biochemistry. 31:1992;4066-4074.
    • (1992) Biochemistry , vol.31 , pp. 4066-4074
    • Tae, G.S.1    Cramer, W.A.2
  • 28
    • 0030858110 scopus 로고    scopus 로고
    • Influence of photosynthetic photon flux densities before and during long-term chilling on xanthophyll cycle and chlorophyll fluorescence quenching in leaves of tomato (Lycopersicon hirsutum)
    • Jung S., Steffen K.L. Influence of photosynthetic photon flux densities before and during long-term chilling on xanthophyll cycle and chlorophyll fluorescence quenching in leaves of tomato (Lycopersicon hirsutum). Physiol. Plant. 100:1997;958-966.
    • (1997) Physiol. Plant , vol.100 , pp. 958-966
    • Jung, S.1    Steffen, K.L.2
  • 29
    • 0019944971 scopus 로고
    • Comparative biochemistry of oxygen toxicity in lactic acid-forming aquatic fungi
    • Natvig D.O. Comparative biochemistry of oxygen toxicity in lactic acid-forming aquatic fungi. Arch. Microbiol. 132:1982;107-114.
    • (1982) Arch. Microbiol. , vol.132 , pp. 107-114
    • Natvig, D.O.1
  • 30
    • 0000931998 scopus 로고
    • Role of peroxidase in the development of water-impermeable seed coats in Sida spinosa L
    • Egley G.H., Paul R.N. Jr, Vaughn K.C., Duke S.O. Role of peroxidase in the development of water-impermeable seed coats in Sida spinosa L. Planta. 157:1983;224-232.
    • (1983) Planta , vol.157 , pp. 224-232
    • Egley, G.H.1    Paul R.N., Jr.2    Vaughn, K.C.3    Duke, S.O.4
  • 31
    • 11944254277 scopus 로고
    • Superoxide dismutase, catalase and alpha tocopherol content of stored potato tubers
    • Spychalla J.P., Desborough S.L. Superoxide dismutase, catalase and alpha tocopherol content of stored potato tubers. Plant Physiol. 94:1990;1214-1218.
    • (1990) Plant Physiol. , vol.94 , pp. 1214-1218
    • Spychalla, J.P.1    Desborough, S.L.2
  • 32
    • 33745314723 scopus 로고
    • Ascorbate peroxidase in tea leaves: Occurrence of two isozymes and the differences in their enzymatic and molecular properties
    • Chen G.X., Asada K. Ascorbate peroxidase in tea leaves: occurrence of two isozymes and the differences in their enzymatic and molecular properties. Plant Cell Physiol. 30:1989;987-998.
    • (1989) Plant Cell Physiol. , vol.30 , pp. 987-998
    • Chen, G.X.1    Asada, K.2
  • 33
    • 0030023240 scopus 로고    scopus 로고
    • Ultraviolet-B- And ozone-induced biochemical changes in antioxidant enzymes of Arabodopsis thaliana
    • Rao M.V., Paliyath G., Ormrod D.P. Ultraviolet-B- and ozone-induced biochemical changes in antioxidant enzymes of Arabodopsis thaliana. Plant Physiol. 110:1996;125-136.
    • (1996) Plant Physiol. , vol.110 , pp. 125-136
    • Rao, M.V.1    Paliyath, G.2    Ormrod, D.P.3
  • 34
    • 0015152970 scopus 로고
    • An improved procedure for using ferricyanide for detecting catalase isozymes
    • Woodbury W., Spencer A.K., Stahman M.A. An improved procedure for using ferricyanide for detecting catalase isozymes. Anal. Biochem. 44:1971;301-305.
    • (1971) Anal. Biochem. , vol.44 , pp. 301-305
    • Woodbury, W.1    Spencer, A.K.2    Stahman, M.A.3
  • 35
    • 0027135026 scopus 로고
    • Hydrogen peroxide and lignification
    • Olson P.D., Varner J.E. Hydrogen peroxide and lignification. Plant J. 4:1993;887-892.
    • (1993) Plant J. , vol.4 , pp. 887-892
    • Olson, P.D.1    Varner, J.E.2
  • 37
    • 0030498562 scopus 로고    scopus 로고
    • Using chlorophyll fluorescence to assess the fraction of absorbed light allocated to thermal dissipation of excess excitation
    • Demmig-Adams B., Adams W.W. III, Barker D.H., Logan B.A., Bowling D.R., Verhoeven A.S. Using chlorophyll fluorescence to assess the fraction of absorbed light allocated to thermal dissipation of excess excitation. Physiol. Plant. 98:1996;253-264.
    • (1996) Physiol. Plant , vol.98 , pp. 253-264
    • Demmig-Adams, B.1    Adams W.W. III2    Barker, D.H.3    Logan, B.A.4    Bowling, D.R.5    Verhoeven, A.S.6
  • 38
    • 0030788044 scopus 로고    scopus 로고
    • Cadmium and zinc induction of lipid peroxidation and effects on antioxidant enzyme activities in bean (Phaseolus vulgaris L.)
    • Chaoui A., Mazhoudi S., Ghorbal M.H., Ferjani E.E. Cadmium and zinc induction of lipid peroxidation and effects on antioxidant enzyme activities in bean (Phaseolus vulgaris L.). Plant Sci. 127:1997;139-147.
    • (1997) Plant Sci. , vol.127 , pp. 139-147
    • Chaoui, A.1    Mazhoudi, S.2    Ghorbal, M.H.3    Ferjani, E.E.4
  • 39
    • 84981674366 scopus 로고
    • Photoinactivation of catalase at low temperature and its relevance to photosynthetic and peroxide metabolism in leaves
    • Volk J., Feierabend J. Photoinactivation of catalase at low temperature and its relevance to photosynthetic and peroxide metabolism in leaves. Plant Cell Environ. 12:1989;701-712.
    • (1989) Plant Cell Environ. , vol.12 , pp. 701-712
    • Volk, J.1    Feierabend, J.2
  • 40
    • 0001459645 scopus 로고
    • Changes in the activities of antioxidant enzymes during exposure of intact wheat leaves to strong visible light at different temperatures in the presence of different protein synthesis inhibitors
    • Mishra N.P., Mishra R.K., Singhal G.S. Changes in the activities of antioxidant enzymes during exposure of intact wheat leaves to strong visible light at different temperatures in the presence of different protein synthesis inhibitors. Plant Physiol. 102:1993;867-880.
    • (1993) Plant Physiol. , vol.102 , pp. 867-880
    • Mishra, N.P.1    Mishra, R.K.2    Singhal, G.S.3
  • 41
    • 0000686970 scopus 로고
    • Light-dependent reduction of dehydroascorbate by ruptured pea chloroplasts
    • Jablonski P.P., Anderson J.W. Light-dependent reduction of dehydroascorbate by ruptured pea chloroplasts. Plant Physiol. 67:1981;1239-1244.
    • (1981) Plant Physiol. , vol.67 , pp. 1239-1244
    • Jablonski, P.P.1    Anderson, J.W.2
  • 42
    • 0031111135 scopus 로고    scopus 로고
    • Differential expression of CuZn- And Fe-superoxide dismutase genes of tobacco during development, oxidative stress, and hormonal treatments
    • Kurepa J., Hérouart D., Montagu M.V., Inzé D. Differential expression of CuZn- and Fe-superoxide dismutase genes of tobacco during development, oxidative stress, and hormonal treatments. Plant Cell Physiol. 38:1997;463-470.
    • (1997) Plant Cell Physiol. , vol.38 , pp. 463-470
    • Kurepa, J.1    Hérouart, D.2    Montagu, M.V.3    Inzé, D.4
  • 43
    • 0001045008 scopus 로고    scopus 로고
    • A cyanobacterium lacking iron superoxide dismutase is sensitized to oxidative stress induced with methyl viologen but is not sensitized to oxidative stress induced with norflurazon
    • Thomas D.J., Avenson T.J., Thomas J.B., Herbert S.K. A cyanobacterium lacking iron superoxide dismutase is sensitized to oxidative stress induced with methyl viologen but is not sensitized to oxidative stress induced with norflurazon. Plant Physiol. 116:1998;1593-1602.
    • (1998) Plant Physiol. , vol.116 , pp. 1593-1602
    • Thomas, D.J.1    Avenson, T.J.2    Thomas, J.B.3    Herbert, S.K.4


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