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Volumn 63, Issue 1, 2000, Pages 23-34

Reduction of Q(A) in the dark: Another cause of fluorescence F(o) increases by high temperatures in higher plants

Author keywords

Chlororespiration; Pheophytin a; Photosynthesis; Photosystem II; Potato; Tobacco

Indexed keywords


EID: 0034051467     PISSN: 01668595     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1006350706802     Document Type: Article
Times cited : (100)

References (37)
  • 2
    • 0000075484 scopus 로고
    • A highly resolved, oxygen-evolving Photosystem II preparation from spinach thylakoid membranes
    • Berthold DA, Babcock GT and Yocum CF (1981) A highly resolved, oxygen-evolving Photosystem II preparation from spinach thylakoid membranes. FEBS Lett 134: 231-234
    • (1981) FEBS Lett , vol.134 , pp. 231-234
    • Berthold, D.A.1    Babcock, G.T.2    Yocum, C.F.3
  • 3
    • 0021567328 scopus 로고
    • Determination of leaf heat resistance: Comparative investigation of chlorophyll fluorescence changes and tissue necrosis methods
    • Bilger HW, Schreiber U and Lange OL (1984) Determination of leaf heat resistance: Comparative investigation of chlorophyll fluorescence changes and tissue necrosis methods. Oecologia 63: 256-262
    • (1984) Oecologia , vol.63 , pp. 256-262
    • Bilger, H.W.1    Schreiber, U.2    Lange, O.L.3
  • 4
    • 0001851869 scopus 로고
    • Analysis of chlorophyll a fluorescence changes in weak light in heat-treated Amaranthus chloroplasts
    • Bukhov NG, Sabat SC and Mohanty P (1990) Analysis of chlorophyll a fluorescence changes in weak light in heat-treated Amaranthus chloroplasts. Photosynth Res 23: 81-87
    • (1990) Photosynth Res , vol.23 , pp. 81-87
    • Bukhov, N.G.1    Sabat, S.C.2    Mohanty, P.3
  • 6
    • 0024288671 scopus 로고
    • Purification and characterization of a rotenone-insensitive NADH: Q6 oxidoreductase from mitochondria of Saccharomyces cerevisiae
    • de Vries S and Grivell LA (1988) Purification and characterization of a rotenone-insensitive NADH: Q6 oxidoreductase from mitochondria of Saccharomyces cerevisiae. Eur J Biochem 176: 377-384
    • (1988) Eur J Biochem , vol.176 , pp. 377-384
    • De Vries, S.1    Grivell, L.A.2
  • 7
    • 0000108270 scopus 로고
    • Increased heat sensitivity of the photosynthetic apparatus in triazine-resistant biotypes from different plant species
    • Ducruet JM and Lemoine Y (1985) Increased heat sensitivity of the photosynthetic apparatus in triazine-resistant biotypes from different plant species. Plant Cell Physiol 26: 419-429
    • (1985) Plant Cell Physiol , vol.26 , pp. 419-429
    • Ducruet, J.M.1    Lemoine, Y.2
  • 8
    • 0001036383 scopus 로고
    • Respiratory control over photosynthetic electron transport in chloroplasts of higher-plant cells: Evidence of chlororespiration
    • Garab G, Lajko F, Mustardy L and Marton L (1989) Respiratory control over photosynthetic electron transport in chloroplasts of higher-plant cells: Evidence of chlororespiration. Planta 179: 349-358
    • (1989) Planta , vol.179 , pp. 349-358
    • Garab, G.1    Lajko, F.2    Mustardy, L.3    Marton, L.4
  • 9
    • 0000184562 scopus 로고
    • Sixty-three years since Kautsky: Chlorophyll a fluorescence
    • Govindjee (1995) Sixty-three years since Kautsky: Chlorophyll a fluorescence. Aust J Plant Physiol 22: 131-160
    • (1995) Aust J Plant Physiol , vol.22 , pp. 131-160
    • Govindjee1
  • 10
    • 0003050392 scopus 로고
    • Fluorescence properties of chlorophyll b- and chlorophyll c-containing algae
    • Govindjee, Amesz J and Fork DC (eds) Academic Press, New York
    • Govindjee and Satoh K (1986) Fluorescence properties of chlorophyll b- and chlorophyll c-containing algae. In: Govindjee, Amesz J and Fork DC (eds) Light Emission by Plants and Bacteria, pp 497-537. Academic Press, New York
    • (1986) Light Emission by Plants and Bacteria , pp. 497-537
    • Govindjee1    Satoh, K.2
  • 11
    • 0030032608 scopus 로고    scopus 로고
    • Short-term responses of Photosystem I to heat stress
    • Havaux M (1996) Short-term responses of Photosystem I to heat stress. Photosynth Res 47: 85-97
    • (1996) Photosynth Res , vol.47 , pp. 85-97
    • Havaux, M.1
  • 13
    • 34249958267 scopus 로고
    • The use of chlorophyll fluorescence nomenclature in plant stress physiology
    • Kooten O and Snel JFH (1990) The use of chlorophyll fluorescence nomenclature in plant stress physiology. Photosynth Res 25: 147-150
    • (1990) Photosynth Res , vol.25 , pp. 147-150
    • Kooten, O.1    Snel, J.F.H.2
  • 14
    • 12044251905 scopus 로고
    • Chlorophyll fluorescence and photosynthesis: The basics
    • Krause GH and Weis E (1991) Chlorophyll fluorescence and photosynthesis: The basics. Annu Rev Plant Physiol Plant Mol Biol 42: 313-349
    • (1991) Annu Rev Plant Physiol Plant Mol Biol , vol.42 , pp. 313-349
    • Krause, G.H.1    Weis, E.2
  • 15
    • 0029189537 scopus 로고
    • Photoactivation of the electron flow from NADPH to plastoquinone in spinach chloroplasts
    • Mano J, Miyake C, Schreiber U and Asada K (1995) Photoactivation of the electron flow from NADPH to plastoquinone in spinach chloroplasts. Plant Cell Physiol 36: 1589-1598
    • (1995) Plant Cell Physiol , vol.36 , pp. 1589-1598
    • Mano, J.1    Miyake, C.2    Schreiber, U.3    Asada, K.4
  • 16
    • 0028814979 scopus 로고
    • Thylakoid membrane-bound, NADPH-specific pyridine nucleotide dehydrogenase complex mediates cyclic electron transport in the cyanobacterium Synechocystis sp. PCC6803
    • Mi H, Endo T, Ogawa T and Asada K (1995) Thylakoid membrane-bound, NADPH-specific pyridine nucleotide dehydrogenase complex mediates cyclic electron transport in the cyanobacterium Synechocystis sp. PCC6803. Plant Cell Physiol 36: 661-668
    • (1995) Plant Cell Physiol , vol.36 , pp. 661-668
    • Mi, H.1    Endo, T.2    Ogawa, T.3    Asada, K.4
  • 17
    • 4243696506 scopus 로고
    • Donation of electron from NADPH to plastoquinone in thylakoids from higher plants
    • Miyake C, Ogawa K, Schreiber U and Asada K (1994) Donation of electron from NADPH to plastoquinone in thylakoids from higher plants. Plant Cell Physiol 35: s21
    • (1994) Plant Cell Physiol , vol.35
    • Miyake, C.1    Ogawa, K.2    Schreiber, U.3    Asada, K.4
  • 18
    • 0028878630 scopus 로고
    • Ferredoxin-dependent and antimycin A-sensitive reduction of cytochrome b-559 by far-red light in maize thylakoids; participation of a menadiol-reducible cytochrome b-559 in cyclic electron flow
    • Miyake C, Schreiber U and Asada K (1995) Ferredoxin-dependent and antimycin A-sensitive reduction of cytochrome b-559 by far-red light in maize thylakoids; participation of a menadiol-reducible cytochrome b-559 in cyclic electron flow. Plant Cell Physiol 36: 743-748
    • (1995) Plant Cell Physiol , vol.36 , pp. 743-748
    • Miyake, C.1    Schreiber, U.2    Asada, K.3
  • 19
    • 0027479814 scopus 로고
    • Studies on the inhibitory mechanism of iodonium compounds with special reference to neutrophil NADPH oxidase
    • O'Donnell VB, Tew DG, Jones OTG and England PJ (1993) Studies on the inhibitory mechanism of iodonium compounds with special reference to neutrophil NADPH oxidase. Biochem J 290: 41-49
    • (1993) Biochem J , vol.290 , pp. 41-49
    • O'Donnell, V.B.1    Tew, D.G.2    Jones, O.T.G.3    England, P.J.4
  • 20
    • 0028110631 scopus 로고
    • The cyclic electron pathways around Photosystem I in Chlamydomonas reinhardtii as determined in vivo by photoacoustic measurements of energy storage
    • Ravenel J, Peltier G and Havaux M (1994) The cyclic electron pathways around Photosystem I in Chlamydomonas reinhardtii as determined in vivo by photoacoustic measurements of energy storage. Planta 193: 251-259
    • (1994) Planta , vol.193 , pp. 251-259
    • Ravenel, J.1    Peltier, G.2    Havaux, M.3
  • 21
    • 0021049007 scopus 로고
    • NADH and NADPH dehydrogenases from the blue-green alga, Aphanocapsa
    • Sandmann G and Malkin R (1983) NADH and NADPH dehydrogenases from the blue-green alga, Aphanocapsa. Arch Microbiol 136: 49-53
    • (1983) Arch Microbiol , vol.136 , pp. 49-53
    • Sandmann, G.1    Malkin, R.2
  • 22
    • 0000658354 scopus 로고
    • + reductase in Bryopsis chloroplasts
    • + reductase in Bryopsis chloroplasts. Biochim Biophys Acta 638: 327-333
    • (1981) Biochim Biophys Acta , vol.638 , pp. 327-333
    • Satoh, K.1
  • 23
    • 0000112076 scopus 로고
    • Mechanism of photoactivation of electron transport in intact Bryopsis chloroplasts
    • Satoh K (1982) Mechanism of photoactivation of electron transport in intact Bryopsis chloroplasts. Plant Physiol 70: 1004-1008
    • (1982) Plant Physiol , vol.70 , pp. 1004-1008
    • Satoh, K.1
  • 24
    • 0032486451 scopus 로고    scopus 로고
    • The chloroplast Ndh complex mediates the dark reduction of the plastoquinone pool in response to heat stress in tobacco leaves
    • Sazanov LA, Burrows PA and Nixon PJ (1998) The chloroplast Ndh complex mediates the dark reduction of the plastoquinone pool in response to heat stress in tobacco leaves. FEBS Lett 429: 115-118
    • (1998) FEBS Lett , vol.429 , pp. 115-118
    • Sazanov, L.A.1    Burrows, P.A.2    Nixon, P.J.3
  • 25
    • 0017879066 scopus 로고
    • Heat-induced changes of chlorophyll fluorescence in isolated chloroplasts and related heat-damage at the pigment level
    • Schreiber U and Armond PA (1978) Heat-induced changes of chlorophyll fluorescence in isolated chloroplasts and related heat-damage at the pigment level. Biochim Biophys Acta 502: 138-151
    • (1978) Biochim Biophys Acta , vol.502 , pp. 138-151
    • Schreiber, U.1    Armond, P.A.2
  • 26
    • 0001207967 scopus 로고
    • Heat-induced changes of chlorophyll fluorescence in intact leaves correlated with damage of photosynthetic apparatus
    • Schreiber U and Berry JA (1977) Heat-induced changes of chlorophyll fluorescence in intact leaves correlated with damage of photosynthetic apparatus. Planta 136: 233-238
    • (1977) Planta , vol.136 , pp. 233-238
    • Schreiber, U.1    Berry, J.A.2
  • 27
    • 0026008005 scopus 로고
    • The human dioxin-inducible NAD(P)H: Quinone oxidoreductase cDNA-encoded protein expressed in COS-1 cells is identical to diaphorase 4
    • Shaw PM, Reiss A, Adesnik M, Nebert DW, Schembri J and Jaiswal AK (1991) The human dioxin-inducible NAD(P)H: quinone oxidoreductase cDNA-encoded protein expressed in COS-1 cells is identical to diaphorase 4. Eur J Biochem 195: 171-176
    • (1991) Eur J Biochem , vol.195 , pp. 171-176
    • Shaw, P.M.1    Reiss, A.2    Adesnik, M.3    Nebert, D.W.4    Schembri, J.5    Jaiswal, A.K.6
  • 28
    • 0032483030 scopus 로고    scopus 로고
    • Directed disruption of the tobacco ndhB gene impairs cyclic electron flow around Photosystem I
    • Shikanai T, Endo T, Hashimoto T, Yamada Y, Asada K and Yokota A (1998) Directed disruption of the tobacco ndhB gene impairs cyclic electron flow around Photosystem I. Proc Natl Acad Sci USA 95: 9705-9709
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 9705-9709
    • Shikanai, T.1    Endo, T.2    Hashimoto, T.3    Yamada, Y.4    Asada, K.5    Yokota, A.6
  • 29
    • 0018400873 scopus 로고
    • Mitochondrion electron transport inhibitors
    • Singer TP (1979) Mitochondrion electron transport inhibitors. Methods Enzymol 55: 454-462
    • (1979) Methods Enzymol , vol.55 , pp. 454-462
    • Singer, T.P.1
  • 30
    • 77957014322 scopus 로고
    • Application of inhibitors and uncouplers for a study of oxidative phosphorylation
    • Slater EC (1967) Application of inhibitors and uncouplers for a study of oxidative phosphorylation. Methods Enzymol 10: 48-57
    • (1967) Methods Enzymol , vol.10 , pp. 48-57
    • Slater, E.C.1
  • 31
    • 0029914199 scopus 로고    scopus 로고
    • NAD(P)H: (quinone-acceptor) oxidoreductase of tobacco leaves is a flavin mononucleotide-containing flavoenzyme
    • Sparla F, Tedeschi G and Trost P (1996) NAD(P)H: (quinone-acceptor) oxidoreductase of tobacco leaves is a flavin mononucleotide-containing flavoenzyme. Plant Physiol 112: 249-258
    • (1996) Plant Physiol , vol.112 , pp. 249-258
    • Sparla, F.1    Tedeschi, G.2    Trost, P.3
  • 32
    • 0030959675 scopus 로고    scopus 로고
    • Regulation of antenna structure and electron transport in Photosystem II of Pisum sativum under elevated temperature probed by the fast polyphasic chlorophyll a fluorescence transient: OKJIP
    • Srivastava A, Guissé B, Greppin H and Strasser RJ (1997) Regulation of antenna structure and electron transport in Photosystem II of Pisum sativum under elevated temperature probed by the fast polyphasic chlorophyll a fluorescence transient: OKJIP. Biochim Biophys Acta 1320: 95-106
    • (1997) Biochim Biophys Acta , vol.1320 , pp. 95-106
    • Srivastava, A.1    Guissé, B.2    Greppin, H.3    Strasser, R.J.4
  • 33
    • 0001414438 scopus 로고
    • Role of chloroplast ferredoxin in the energy conversion process of photosynthesis
    • Tagawa K, Tsujimoto HY and Arnon DI (1963) Role of chloroplast ferredoxin in the energy conversion process of photosynthesis. Proc Natl Acad Sci USA 49: 567-572
    • (1963) Proc Natl Acad Sci USA , vol.49 , pp. 567-572
    • Tagawa, K.1    Tsujimoto, H.Y.2    Arnon, D.I.3
  • 35
    • 0025007820 scopus 로고
    • Inhibition by capsicin of NADH-quinone oxidore-ductase is correlated with the presence of energy-coupling site 1 in various organisms
    • Yagi T (1990) Inhibition by capsicin of NADH-quinone oxidore-ductase is correlated with the presence of energy-coupling site 1 in various organisms. Arch Biochem Biophys 280: 305-311
    • (1990) Arch Biochem Biophys , vol.280 , pp. 305-311
    • Yagi, T.1
  • 36
    • 0030768015 scopus 로고    scopus 로고
    • o level and reversible inhibition of Photosystem II reaction center by high-temperature treatment in higher plants
    • o level and reversible inhibition of Photosystem II reaction center by high-temperature treatment in higher plants. Photosynth Res 52: 57-64
    • (1997) Photosynth Res , vol.52 , pp. 57-64
    • Yamane, Y.1    Kashino, Y.2    Koike, H.3    Satoh, K.4
  • 37
    • 0031670790 scopus 로고    scopus 로고
    • Effects of high temperatures on the photosynthetic systems in spinach: Oxygen-evolving activities, fluorescence characteristics and the denaturation process
    • Yamane Y, Kashino Y, Koike H and Satoh K (1998) Effects of high temperatures on the photosynthetic systems in spinach: Oxygen-evolving activities, fluorescence characteristics and the denaturation process. Photosynth Res 57: 51-59
    • (1998) Photosynth Res , vol.57 , pp. 51-59
    • Yamane, Y.1    Kashino, Y.2    Koike, H.3    Satoh, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.