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Volumn 44, Issue 9, 2005, Pages 3123-3133

Investigations on the reaction pattern of photosystem II in leaves from Arabidopsis thaliana by time-resolved fluorometric analysis

Author keywords

[No Author keywords available]

Indexed keywords

AMINES; BIOCHEMISTRY; CHLOROPHYLL; FLUORESCENCE; GENES; LIPIDS; OXIDATION; PHOTOCHEMICAL REACTIONS; QUENCHING; REACTION KINETICS; TIME DOMAIN ANALYSIS;

EID: 14644426562     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0484668     Document Type: Article
Times cited : (40)

References (77)
  • 1
    • 14644397253 scopus 로고    scopus 로고
    • Investigations on the reaction pattern of photosystem II in leaves from Arabidopsis thaliana wild type plants and mutants with genetically modified lipid content
    • Steffen, R., Kelly, A. A., Huyer, J., Dörmann, P., and Renger, G. (2005) Investigations on the reaction pattern of photosystem II in leaves from Arabidopsis thaliana wild type plants and mutants with genetically modified lipid content, Biochemistry 44, 3134-3142.
    • (2005) Biochemistry , vol.44 , pp. 3134-3142
    • Steffen, R.1    Kelly, A.A.2    Huyer, J.3    Dörmann, P.4    Renger, G.5
  • 2
    • 0026530174 scopus 로고
    • Oxygen activation and the conservation of energy in cell respiration
    • Babcock, G. T., and Wikström, M. (1992) Oxygen activation and the conservation of energy in cell respiration, Nature 356, 301-306.
    • (1992) Nature , vol.356 , pp. 301-306
    • Babcock, G.T.1    Wikström, M.2
  • 3
    • 0000514256 scopus 로고
    • The role of acyl lipids in reconstitution of lipid-depleted light-harvesting complex II from cold-hardened and nonhardened rye
    • Krupa, Z., Williams, J. P., Mobashoher, U. K., and Humer, N. P. A. (1992) The role of acyl lipids in reconstitution of lipid-depleted light-harvesting complex II from cold-hardened and nonhardened rye, Plant Physiol. 100, 931-938.
    • (1992) Plant Physiol. , vol.100 , pp. 931-938
    • Krupa, Z.1    Williams, J.P.2    Mobashoher, U.K.3    Humer, N.P.A.4
  • 4
    • 0027452052 scopus 로고
    • Lipid-protein interactions in crystals of plant light-harvesting complex
    • Nussberger, S., Dörr, K., Wang, D. N., and Kuhlbrandt, W. (1993) Lipid-protein interactions in crystals of plant light-harvesting complex, J. Mol. Biol. 234, 347-356.
    • (1993) J. Mol. Biol. , vol.234 , pp. 347-356
    • Nussberger, S.1    Dörr, K.2    Wang, D.N.3    Kuhlbrandt, W.4
  • 5
    • 0028796714 scopus 로고
    • Chlorophyll a/b binding proteins
    • Paulsen, H. (1995) Chlorophyll a/b binding proteins., Photochem. Photobiol. 62, 367-382.
    • (1995) Photochem. Photobiol. , vol.62 , pp. 367-382
    • Paulsen, H.1
  • 6
    • 2942700872 scopus 로고    scopus 로고
    • Violaxanthin de-epoxidase, the xanthophyll cycle enzyme, requires lipid inverted hexagonal structures for its activity
    • Latowski, D., Akerlund, H. E., and Strzalka, K. (2004) Violaxanthin de-epoxidase, the xanthophyll cycle enzyme, requires lipid inverted hexagonal structures for its activity, Biochemistry 43, 4417-4420.
    • (2004) Biochemistry , vol.43 , pp. 4417-4420
    • Latowski, D.1    Akerlund, H.E.2    Strzalka, K.3
  • 8
    • 0001410324 scopus 로고
    • The effect of thylakoid lipids on an oxygen-evolving Photosystem II preparation
    • Gounaris, K., Whitford, D., and Barber, J. (1983) The effect of thylakoid lipids on an oxygen-evolving Photosystem II preparation, FEBS Lett. 163, 230-234.
    • (1983) FEBS Lett. , vol.163 , pp. 230-234
    • Gounaris, K.1    Whitford, D.2    Barber, J.3
  • 9
    • 0000703251 scopus 로고    scopus 로고
    • Reconstitution of photosynthetic structures and activities with lipids
    • Siegenthaler, P.-A., and Murata, N., Eds. Kluwer Academic Publishers, Dordrecht
    • Tremolieres, A., and Siegenthaler, P.-A. (1998) Reconstitution of photosynthetic structures and activities with lipids, in Lipids in Photosynthesis: Structure, Function and Genetics (Siegenthaler, P.-A., and Murata, N., Eds.) pp 175-189, Kluwer Academic Publishers, Dordrecht.
    • (1998) Lipids in Photosynthesis: Structure, Function and Genetics , pp. 175-189
    • Tremolieres, A.1    Siegenthaler, P.-A.2
  • 10
    • 14644404533 scopus 로고
    • Effects of BSA, fatty acids and lipase treatment on PS II
    • Murata, N., Ed. Kluwer, Dordrecht
    • Schröder, W. P., Messinger, J., Tremolieres, A., and Renger, G. (1992) Effects of BSA, fatty acids and lipase treatment on PS II, in Research in Photosynthesis (Murata, N., Ed.) pp 159-162, Kluwer, Dordrecht.
    • (1992) Research in Photosynthesis , pp. 159-162
    • Schröder, W.P.1    Messinger, J.2    Tremolieres, A.3    Renger, G.4
  • 11
    • 0038082185 scopus 로고    scopus 로고
    • Involvment of sulfoquinovosyl diacylglycerol in the structural integrity and heat-tolerance of photosystem II
    • Sato. N., Aoki, M., Marau, Y., Sonoike, K., Minoda, A., and Tsuzuki, M. (2003) Involvment of sulfoquinovosyl diacylglycerol in the structural integrity and heat-tolerance of photosystem II, Planta 217, 245-251.
    • (2003) Planta , vol.217 , pp. 245-251
    • Sato, N.1    Aoki, M.2    Marau, Y.3    Sonoike, K.4    Minoda, A.5    Tsuzuki, M.6
  • 12
    • 0030852458 scopus 로고    scopus 로고
    • Modification of the water oxidizing complex in leaves of the dgd1 mutant of Arabidopsis thaliana deficient in the galactolipid digalactosyldiacylglycerol
    • Reifarth, F., Christen, G., Seeliger, A. G., Dörmann, P., Benning, C., and Renger, G. (1997) Modification of the water oxidizing complex in leaves of the dgd1 mutant of Arabidopsis thaliana deficient in the galactolipid digalactosyldiacylglycerol, Biochemistry 36, 11769-11776.
    • (1997) Biochemistry , vol.36 , pp. 11769-11776
    • Reifarth, F.1    Christen, G.2    Seeliger, A.G.3    Dörmann, P.4    Benning, C.5    Renger, G.6
  • 14
    • 0037117493 scopus 로고    scopus 로고
    • Arabidopsis disrupted in SQD2 encoding sulfolipid synthase is impaired in phosphatelimited growth
    • Yu, B., Xu, C., and Benning, C. (2002) Arabidopsis disrupted in SQD2 encoding sulfolipid synthase is impaired in phosphatelimited growth, Proc. Natl. Acad. Sci. U.S.A. 99, 5732-5737.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 5732-5737
    • Yu, B.1    Xu, C.2    Benning, C.3
  • 15
    • 0036091099 scopus 로고    scopus 로고
    • Role of sulfoquinovosyl diacylglycerol for the maintenance of photosystem II in Chlamydomonas reinhardtii
    • Minoda, A., Sato, N., Nozaki, H., Okada, K., Takahashi, H., Sonoike, K., and Tsuzuki, M. (2002) Role of sulfoquinovosyl diacylglycerol for the maintenance of photosystem II in Chlamydomonas reinhardtii, Eur. J. Biochem. 269, 2353-2358.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2353-2358
    • Minoda, A.1    Sato, N.2    Nozaki, H.3    Okada, K.4    Takahashi, H.5    Sonoike, K.6    Tsuzuki, M.7
  • 16
    • 1342301479 scopus 로고    scopus 로고
    • Differing involvement of sulfoquinovosyl diacylglycerol in photosystem II in two species of unicellular cyanobacteria
    • Aoki, M., Sato, N., Meguro, A., and Tsuzuki, M. (2004) Differing involvement of sulfoquinovosyl diacylglycerol in photosystem II in two species of unicellular cyanobacteria, Eur. J. Biochem. 271, 685-693.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 685-693
    • Aoki, M.1    Sato, N.2    Meguro, A.3    Tsuzuki, M.4
  • 17
    • 0000937802 scopus 로고
    • Practical applications of fluorometric methods to algae and higher plants
    • Govindjee, Amesz, J., and Fork, D. C., Eds. Academic Press, New York
    • Renger, G., and Schreiber, U. (1986) Practical applications of fluorometric methods to algae and higher plants, in Light Emission by Plants and Bacteria (Govindjee, Amesz, J., and Fork, D. C., Eds.) pp 587-619, Academic Press, New York.
    • (1986) Light Emission by Plants and Bacteria , pp. 587-619
    • Renger, G.1    Schreiber, U.2
  • 19
    • 0002572645 scopus 로고
    • Chlorophyll Fluorescence: An Intrinsic Probe of Photosynthesis
    • Govindjee, Ed. Academic Press, New York
    • Papageorgiou, G. (1975) Chlorophyll Fluorescence: An Intrinsic Probe of Photosynthesis, in Bioenergetics of Photosynthesis (Govindjee, Ed.) pp 319-371, Academic Press, New York.
    • (1975) Bioenergetics of Photosynthesis , pp. 319-371
    • Papageorgiou, G.1
  • 20
    • 0001782991 scopus 로고
    • Chlorophyll a Fluorescence of Higher Plants: Chloroplasts and Leaves
    • Govindjee, Amez, J., and Fork, D. C., Eds. Academic Press, New York
    • Briantais, J. M., Vernotte, C., Krause, G. H., and Weiss, E. (1986) Chlorophyll a Fluorescence of Higher Plants: Chloroplasts and Leaves, in Light Emission by Plants and Bacteria (Govindjee, Amez, J., and Fork, D. C., Eds.) pp 539-583, Academic Press, New York.
    • (1986) Light Emission by Plants and Bacteria , pp. 539-583
    • Briantais, J.M.1    Vernotte, C.2    Krause, G.H.3    Weiss, E.4
  • 21
    • 0024852650 scopus 로고
    • Applications of ultrafast laser spectroscopy for the study of biological systems
    • Holzwarth, A.-R. (1989) Applications of ultrafast laser spectroscopy for the study of biological systems, Q. Rev. Biophys. 22, 239-326.
    • (1989) Q. Rev. Biophys. , vol.22 , pp. 239-326
    • Holzwarth, A.-R.1
  • 22
    • 34250963831 scopus 로고
    • Neue Versuche zur Kohlenstoffassimilation
    • Kautsky, H., and Hirsch, A. (1931) Neue Versuche zur Kohlenstoffassimilation, Naturwissenschaften 19, 964.
    • (1931) Naturwissenschaften , vol.19 , pp. 964
    • Kautsky, H.1    Hirsch, A.2
  • 23
    • 0019879148 scopus 로고
    • Analysis of the slow phases of the in vivo chlorophyll fluorescence induction curve. Changes in the redox state of photosystem II electron acceptors and fluorescence emission from photosystems I and II
    • Bradbury, M., and Baker, N. R. (1981) Analysis of the slow phases of the in vivo chlorophyll fluorescence induction curve. Changes in the redox state of photosystem II electron acceptors and fluorescence emission from photosystems I and II, Biochim. Biophys. Acta 635, 542-551.
    • (1981) Biochim. Biophys. Acta , vol.635 , pp. 542-551
    • Bradbury, M.1    Baker, N.R.2
  • 24
    • 0030592717 scopus 로고    scopus 로고
    • Two fundamentally different types of variable chlorophyll fluorescence in vivo
    • Schreiber, U., and Krieger, A. (1996) Two fundamentally different types of variable chlorophyll fluorescence in vivo, FEES Lett. 397, 131-135.
    • (1996) FEES Lett. , vol.397 , pp. 131-135
    • Schreiber, U.1    Krieger, A.2
  • 25
    • 0032955812 scopus 로고    scopus 로고
    • Theories for kinetics and yields of fluorescence and photochemistry: How, if at all, can different models of antenna organization be distinguished experimentally?
    • Bernhardt, K., and Trissl, H. W. (1999) Theories for kinetics and yields of fluorescence and photochemistry: how, if at all, can different models of antenna organization be distinguished experimentally?, Biochim. Biophys. Acta 1409, 125-142.
    • (1999) Biochim. Biophys. Acta , vol.1409 , pp. 125-142
    • Bernhardt, K.1    Trissl, H.W.2
  • 26
    • 0032493414 scopus 로고    scopus 로고
    • Chlorophyll a flurescence induction in higher plants: Modelling and numerical simulation
    • Stirbet, A., Govindjee, Strasser, B. J., and Strasser, R. J. (1998) Chlorophyll a flurescence induction in higher plants: Modelling and numerical simulation, J. Theor. Biol. 193, 131 -151.
    • (1998) J. Theor. Biol. , vol.193 , pp. 131-151
    • Stirbet, A.1    Govindjee2    Strasser, B.J.3    Strasser, R.J.4
  • 27
    • 0032914373 scopus 로고    scopus 로고
    • Chlorophyll a fluorescence induction
    • Lazar, D. (1999) Chlorophyll a fluorescence induction, Biochim. Biophys. Acta 1412, 1-28.
    • (1999) Biochim. Biophys. Acta , vol.1412 , pp. 1-28
    • Lazar, D.1
  • 28
    • 0028155190 scopus 로고
    • Molecular mechanisms and quantitative models of variable Photosystem II fluorescence
    • Dau, H. (1994) Molecular mechanisms and quantitative models of variable Photosystem II fluorescence, Photochem. Photobiol. 60, 1-23.
    • (1994) Photochem. Photobiol. , vol.60 , pp. 1-23
    • Dau, H.1
  • 29
    • 0015354390 scopus 로고
    • Light-induced fluorescence changes in Chlorella, and the primary photoreactions for the production of oxygen
    • Mauzerall, D. (1972) Light-induced fluorescence changes in Chlorella, and the primary photoreactions for the production of oxygen, Proc. Natl. Acad. Sci. U.S.A. 69, 1358-1362.
    • (1972) Proc. Natl. Acad. Sci. U.S.A. , vol.69 , pp. 1358-1362
    • Mauzerall, D.1
  • 30
    • 0015899271 scopus 로고
    • Rapid fluorescence changes observed in chloroplasts: Their relationship to the O2 evolving system
    • Zankel, K. L. (1973) Rapid fluorescence changes observed in chloroplasts: their relationship to the O2 evolving system, Biochim. Biophys. Acta 325, 138-148.
    • (1973) Biochim. Biophys. Acta , vol.325 , pp. 138-148
    • Zankel, K.L.1
  • 31
    • 0016397189 scopus 로고
    • Fluorescence yield kinetics in the microsecond-range in Chlorella pyrenoidosa and spinach chloroplasts in the presence of hydroxylamine
    • den Haan, G. A., Duysens, L. N. M., and Egberts, D. J. (1974) Fluorescence yield kinetics in the microsecond-range in Chlorella pyrenoidosa and spinach chloroplasts in the presence of hydroxylamine, Biochim. Biophys. Acta 368, 409-421.
    • (1974) Biochim. Biophys. Acta , vol.368 , pp. 409-421
    • Den Haan, G.A.1    Duysens, L.N.M.2    Egberts, D.J.3
  • 32
    • 0002939355 scopus 로고
    • Rapid reactions of photosystem 2 as studied by the kinetics of the fluorescence and luminescence of chlorophyll a in Chlorella pyrenoidosa
    • Avron, M., Ed. Elsevier, Amsterdam
    • Duysens, L. N. M., den Haan, G. A., and van Best, J. A. (1975) Rapid reactions of photosystem 2 as studied by the kinetics of the fluorescence and luminescence of chlorophyll a in Chlorella pyrenoidosa, in Proceedings of the Third International Congress on Photosynthesis (Avron, M., Ed.) pp 1 -12, Elsevier, Amsterdam.
    • (1975) Proceedings of the Third International Congress on Photosynthesis , pp. 1-12
    • Duysens, L.N.M.1    Den Haan, G.A.2    Van Best, J.A.3
  • 33
    • 0017619690 scopus 로고
    • Flash induced fluorescence kinetics in chloroplasts in the 20-100s time range in the presence of 3(3,4 dichlorophenyl)-1,1-dimethylurea-Effects of Hydroxylamine
    • Joliot, A. (1976) Flash induced fluorescence kinetics in chloroplasts in the 20-100s time range in the presence of 3(3,4 dichlorophenyl)-1,1- dimethylurea-Effects of Hydroxylamine. Biochim. Biophys. Acta 460, 142-151.
    • (1976) Biochim. Biophys. Acta , vol.460 , pp. 142-151
    • Joliot, A.1
  • 34
    • 0017372625 scopus 로고
    • The rise in chlorophyll a fluorescence yield and decay in delayed light emission in triswashed chloroplasts in the 6-100 microseconds time range after an excitation flash
    • Jursinic, P., and Govindjee. (1977) The rise in chlorophyll a fluorescence yield and decay in delayed light emission in triswashed chloroplasts in the 6-100 microseconds time range after an excitation flash, Biochim. Biophys. Acta 461, 253-267.
    • (1977) Biochim. Biophys. Acta , vol.461 , pp. 253-267
    • Jursinic, P.1    Govindjee2
  • 35
    • 0019320156 scopus 로고
    • Binary oscillations in the rate of reoxidation of the primary acceptor of photosystem II
    • Bowes, J. M., and Crofts, A. R. (1980) Binary oscillations in the rate of reoxidation of the primary acceptor of photosystem II, Biochim. Biophys. Acta 590, 373-384.
    • (1980) Biochim. Biophys. Acta , vol.590 , pp. 373-384
    • Bowes, J.M.1    Crofts, A.R.2
  • 36
    • 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
  • 37
    • 0002556618 scopus 로고    scopus 로고
    • Control of photosynthesis and measurement of photosynthetic reactions in intact plants
    • Baker, N., Ed. Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Kramer, D. M., and Crofts, A. R. (1996) Control of photosynthesis and measurement of photosynthetic reactions in intact plants, in Photosynthesis and the environment. Advances in Photosynthesis (Baker, N., Ed.) pp 25-66, Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1996) Photosynthesis and the Environment. Advances in Photosynthesis , pp. 25-66
    • Kramer, D.M.1    Crofts, A.R.2
  • 38
    • 0030974332 scopus 로고    scopus 로고
    • +asterisk inside a circle sign reduction in PS II preparations and green plants
    • +asterisk inside a circle sign reduction in PS II preparations and green plants, Photosynth. Res. 51, 231-242.
    • (1997) Photosynth. Res. , vol.51 , pp. 231-242
    • Reifarth, F.1    Christen, G.2    Renger, G.3
  • 39
    • 0035830426 scopus 로고    scopus 로고
    • Time-resolved monitoring of flash-induced changes of fluorescence quantum yield and decay of delayed light emission in oxygen-evolving photosynthetic organisms
    • Steifen, R., Christen, G., and Renger, G. (2001) Time-resolved monitoring of flash-induced changes of fluorescence quantum yield and decay of delayed light emission in oxygen-evolving photosynthetic organisms, Biochemistry 40, 173-180.
    • (2001) Biochemistry , vol.40 , pp. 173-180
    • Steifen, R.1    Christen, G.2    Renger, G.3
  • 40
    • 84982358134 scopus 로고
    • A revised medium for rapid growth and bioassays with tobacco tissue cultures
    • Murashige, T., and Skoog, F. (1962) A revised medium for rapid growth and bioassays with tobacco tissue cultures, Physiol. Plant. 15, 473-497.
    • (1962) Physiol. Plant. , vol.15 , pp. 473-497
    • Murashige, T.1    Skoog, F.2
  • 42
    • 0000075484 scopus 로고
    • A highly resolved, oxygen-evolving photosystem II preparation from spinach thylakoid membranes: EPR and electron-transport properties
    • Berthold, D. A., Babcock, G. T., and Yocum, C. A. (1981) A highly resolved, oxygen-evolving photosystem II preparation from spinach thylakoid membranes: EPR and electron-transport properties, FEBS Lett. 134, 231-234.
    • (1981) FEBS Lett. , vol.134 , pp. 231-234
    • Berthold, D.A.1    Babcock, G.T.2    Yocum, C.A.3
  • 43
    • 0037559587 scopus 로고
    • Effect of trypsin on PS-II particles. Correlation between Hill-activity, Mn-abundance and peptide pattern
    • Völker, M., Ono, T., Inoue, Y., and Renger, G. (1985) Effect of trypsin on PS-II particles. Correlation between Hill-activity, Mn-abundance and peptide pattern, Biochim. Biophys. Acta 806, 25-34.
    • (1985) Biochim. Biophys. Acta , vol.806 , pp. 25-34
    • Völker, M.1    Ono, T.2    Inoue, Y.3    Renger, G.4
  • 45
    • 4244113299 scopus 로고
    • A 160-Kilodalton Photosystem-I Reaction-Center Complex. Low-Temperature Fluorescence Spectroscopy
    • Ikegami, I., and Ke, B. (1984) A 160-Kilodalton Photosystem-I Reaction-Center Complex. Low-Temperature Fluorescence Spectroscopy, Biochim. Biophys. Acta 764, 80-85.
    • (1984) Biochim. Biophys. Acta , vol.764 , pp. 80-85
    • Ikegami, I.1    Ke, B.2
  • 46
    • 0011839929 scopus 로고
    • Photosynthesis
    • Hoppe, W., Lohmann, W., Markl, H., and Ziegler, H., Eds. Springer, Berlin
    • Renger, G. (1983) Photosynthesis, in Biophysics (Hoppe, W., Lohmann, W., Markl, H., and Ziegler, H., Eds.) pp 515-542, Springer, Berlin.
    • (1983) Biophysics , pp. 515-542
    • Renger, G.1
  • 47
    • 78651153734 scopus 로고
    • Kinetic Study of the Photochemical Reaction Liberating Oxygen during Photosynthesis
    • Joliot, A., and Joliot, P. (1964) Kinetic Study of the Photochemical Reaction Liberating Oxygen During Photosynthesis, C. R. Hebd. Seances Acad. Sci. 258, 4622-4625.
    • (1964) C. R. Hebd. Seances Acad. Sci. , vol.258 , pp. 4622-4625
    • Joliot, A.1    Joliot, P.2
  • 48
    • 0002441056 scopus 로고
    • Quantitative analysis of fluorescence induction curves in isolated chloroplasts
    • Renger, G., and Schulze, A. (1985) Quantitative analysis of fluorescence induction curves in isolated chloroplasts, Photobiochem. Photobiophys. 9, 79-87.
    • (1985) Photobiochem. Photobiophys. , vol.9 , pp. 79-87
    • Renger, G.1    Schulze, A.2
  • 50
    • 0039530612 scopus 로고    scopus 로고
    • Rate of carotenoid triplet formation in solubilized light-harvesting complex II (LHCII) from spinach
    • Schödel, R., Irrgang, K. D., Voigt, J., and Renger, G. (1998) Rate of carotenoid triplet formation in solubilized light-harvesting complex II (LHCII) from spinach, Biophys. J. 75, 3143-3153.
    • (1998) Biophys. J. , vol.75 , pp. 3143-3153
    • Schödel, R.1    Irrgang, K.D.2    Voigt, J.3    Renger, G.4
  • 51
    • 0017746823 scopus 로고
    • Reduciton of Pheophytin in the primary light reaction of Photosystem II
    • Klimov, V. V., Klevanik, A. V., Shuvalov, V. A., and Krasnovsky, A. A. (1977) Reduciton of Pheophytin in the primary light reaction of Photosystem II, FEBS Lett. 82, 183-186.
    • (1977) FEBS Lett. , vol.82 , pp. 183-186
    • Klimov, V.V.1    Klevanik, A.V.2    Shuvalov, V.A.3    Krasnovsky, A.A.4
  • 52
    • 0001240706 scopus 로고
    • On the mechanism of fluorescence quenching by photoaccumulating of the pheophytin anion radical in photosystem II
    • Renger, G., and Kayed, A. (1987) On the mechanism of fluorescence quenching by photoaccumulating of the pheophytin anion radical in photosystem II, Biochim. Biophys. Acta 894, 261-269.
    • (1987) Biochim. Biophys. Acta , vol.894 , pp. 261-269
    • Renger, G.1    Kayed, A.2
  • 53
    • 46149142812 scopus 로고
    • Primary-charge separation and excitation of chlorophyll a in photosystem II particles from spinach as studies by picosecond absorbance-difference spectroscopy
    • Nuijs, A. M., van Gorkom, H. J., Plijter, J. J., and Duysens, L. M. N. (1986) Primary-charge separation and excitation of chlorophyll a in photosystem II particles from spinach as studies by picosecond absorbance-difference spectroscopy, Biochim. Biophys. Acta 848, 167-172.
    • (1986) Biochim. Biophys. Acta , vol.848 , pp. 167-172
    • Nuijs, A.M.1    Van Gorkom, H.J.2    Plijter, J.J.3    Duysens, L.M.N.4
  • 54
    • 0024294057 scopus 로고
    • Analysis of the electron transfer from Pheo- To QA in PS II membrane fragments from spinach by time resolved 325 nm absorption changes in the picosecond domain
    • Eckert, H. J., Wiese, N., Bernarding, J., Eichler, H. J., and Renger, G. (1988) Analysis of the electron transfer from Pheo- to QA in PS II membrane fragments from spinach by time resolved 325 nm absorption changes in the picosecond domain, FEBS Lett. 240, 153-158.
    • (1988) FEBS Lett. , vol.240 , pp. 153-158
    • Eckert, H.J.1    Wiese, N.2    Bernarding, J.3    Eichler, H.J.4    Renger, G.5
  • 57
    • 84980148406 scopus 로고
    • Delayed Fluorescence and some properties of the chlorophyll triplets
    • Parker, C. A., and Joyce, T. A. (1967) Delayed Fluorescence and some properties of the chlorophyll triplets, Photochem. Photobiol. 6, 395-406.
    • (1967) Photochem. Photobiol. , vol.6 , pp. 395-406
    • Parker, C.A.1    Joyce, T.A.2
  • 59
    • 0030901810 scopus 로고    scopus 로고
    • Quenching of chlorophyll a fluorescence in the aggregates of LHCII: Steady state fluorescence and picosecond relaxation kinetics
    • Vasil'ev, S., Irrgang, K. D., Schrotter, T., Bergmann, A., Eichler, H. J., and Renger, G. (1997) Quenching of chlorophyll a fluorescence in the aggregates of LHCII: steady state fluorescence and picosecond relaxation kinetics, Biochemistry 36, 7503-7512.
    • (1997) Biochemistry , vol.36 , pp. 7503-7512
    • Vasil'ev, S.1    Irrgang, K.D.2    Schrotter, T.3    Bergmann, A.4    Eichler, H.J.5    Renger, G.6
  • 60
    • 0343143115 scopus 로고    scopus 로고
    • Cryoprotectant-induced quenching of chlorophyll a fluorescence from light-harvesting complex 2 in vitro: Time-resolved fluorescence and steady state spectroscopic studies
    • Vasil'ev, S., Schrötter, T., Bergmann, A., Irrgang, K.-D., Eichler, H.-J., and Renger, G. (1997) Cryoprotectant-induced quenching of chlorophyll a fluorescence from light-harvesting complex 2 in vitro: time-resolved fluorescence and steady state spectroscopic studies, Photosynthetica 33, 553-561.
    • (1997) Photosynthetica , vol.33 , pp. 553-561
    • Vasil'ev, S.1    Schrötter, T.2    Bergmann, A.3    Irrgang, K.-D.4    Eichler, H.-J.5    Renger, G.6
  • 61
    • 1842427662 scopus 로고    scopus 로고
    • Fluorescence decay kinetics of solubilized pigment protein complexes from the distal, proximal and core antenna of Photosystem II in the range of 10-277 K and absence or presence of sucrose
    • Huyer, J., Eckert, H.-J., Irrgang, K.-D., Miao, J., Eichler, H.-J., and Renger, G. (2004) Fluorescence decay kinetics of solubilized pigment protein complexes from the distal, proximal and core antenna of Photosystem II in the range of 10-277 K and absence or presence of sucrose, J. Phys. Chem. B 108, 3326-3334.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 3326-3334
    • Huyer, J.1    Eckert, H.-J.2    Irrgang, K.-D.3    Miao, J.4    Eichler, H.-J.5    Renger, G.6
  • 62
    • 0041128436 scopus 로고    scopus 로고
    • Quenching of chlorophyll fluorescence by triplets in solubilized light-harvesting complex II (LHCII)
    • Schödel, R., Irrgang, K. D., Voigt, J., and Renger, G. (1999) Quenching of chlorophyll fluorescence by triplets in solubilized light-harvesting complex II (LHCII), Biophys. J. 76, 2238-2248.
    • (1999) Biophys. J. , vol.76 , pp. 2238-2248
    • Schödel, R.1    Irrgang, K.D.2    Voigt, J.3    Renger, G.4
  • 63
    • 0002132690 scopus 로고
    • Fluorescence Measurements in the Study of Photosystem II Electron Transport
    • Govindjee, Amesz, J., and Fork, D. C., Eds. Academic Press, New York
    • van Gorkom, H. J. (1986) Fluorescence Measurements in the Study of Photosystem II Electron Transport, in Light Emission by Plants and Bacteria (Govindjee, Amesz, J., and Fork, D. C., Eds.) pp 267-289, Academic Press, New York.
    • (1986) Light Emission by Plants and Bacteria , pp. 267-289
    • Van Gorkom, H.J.1
  • 64
    • 0018783449 scopus 로고
    • Chlorophyll a fluorescence as a monitor of nanosecond reduction of the photooxidized primary donor P-680 of photosystem II
    • Sonneveld, A., Rademaker, H., and Duysens, L. N. (1979) Chlorophyll a fluorescence as a monitor of nanosecond reduction of the photooxidized primary donor P-680 Of photosystem II, Biochim. Biophys. Acta 548, 536-551.
    • (1979) Biochim. Biophys. Acta , vol.548 , pp. 536-551
    • Sonneveld, A.1    Rademaker, H.2    Duysens, L.N.3
  • 65
    • 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., Napiwotzki, 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    Napiwotzki, A.4    Eichler, H.-J.5    Renger, G.6
  • 66
    • 0034792833 scopus 로고    scopus 로고
    • Effect of monochromatic UV-B radiation on electron transfer processes in rhodobacter sphaeroides reaction centers
    • Larkum, A. W. D., Karge, M., Reifarth, F., Eckert, H.-J., Post, A., and Renger, G. (2001) Effect of monochromatic UV-B radiation on electron transfer processes in rhodobacter sphaeroides reaction centers, Photosynth. Res. 68, 49-60.
    • (2001) Photosynth. Res. , vol.68 , pp. 49-60
    • Larkum, A.W.D.1    Karge, M.2    Reifarth, F.3    Eckert, H.-J.4    Post, A.5    Renger, G.6
  • 67
    • 33144469231 scopus 로고    scopus 로고
    • The Water/Plastoquinone Oxido-Reductase in Photosynthesis
    • (Wydrzynski, T., and Satoh, K., Eds.), Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Renger, G., and Holzwarth, A.-R. (2005) The Water/Plastoquinone Oxido-Reductase in Photosynthesis, in Photosystem 11 (Wydrzynski, T., and Satoh, K., Eds.), Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (2005) Photosystem , vol.11
    • Renger, G.1    Holzwarth, A.-R.2
  • 68
    • 0001255426 scopus 로고
    • Picosecond kinetics of fluorescence and absorbance changes in photosystem II particles excited by low photon density
    • Schatz, G. H., Brock, H., and Holzwarth, A.-R. (1987) Picosecond kinetics of fluorescence and absorbance changes in photosystem II particles excited by low photon density, Proc. Natl. Acad. Sci. U.S.A. 84, 8414-8418.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 8414-8418
    • Schatz, G.H.1    Brock, H.2    Holzwarth, A.-R.3
  • 69
    • 84914593918 scopus 로고
    • Kinetic and energetic model for the primary processes in photosystem II
    • Schatz, G. H., Brock, H., and Holzwarth, A.-R. (1988) Kinetic and energetic model for the primary processes in photosystem II, Biophys. J. 54, 397-405.
    • (1988) Biophys. J. , vol.54 , pp. 397-405
    • Schatz, G.H.1    Brock, H.2    Holzwarth, A.-R.3
  • 70
    • 1242333128 scopus 로고    scopus 로고
    • Electronic Couplings and Energy Transfer Dynamics in the Oxidized Primary Electron Donor of the Bacterial Reaction Center
    • Jordanides, X. J., Scholes, G. D., Shapley, W. A., Reimers, J. R., and Fleming, G. R. (2004) Electronic Couplings and Energy Transfer Dynamics in the Oxidized Primary Electron Donor of the Bacterial Reaction Center, J. Phys. Chem. B 108, 1753-1765.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 1753-1765
    • Jordanides, X.J.1    Scholes, G.D.2    Shapley, W.A.3    Reimers, J.R.4    Fleming, G.R.5
  • 71
    • 0038938124 scopus 로고
    • Studies on the mechanism of photosynthetic oxygen formation
    • Inoue, Y., Crofts, A. R., Govindjee, Murata, N., Renger, G., and Satoh, K., Eds. Academic Press, Tokyo, Japan
    • Renger, G., Eckert, H. J., and Weiss, W. (1983) Studies on the mechanism of photosynthetic oxygen formation, in The oxygen evolving system in photosynthesis (Inoue, Y., Crofts, A. R., Govindjee, Murata, N., Renger, G., and Satoh, K., Eds.) pp 73-82, Academic Press, Tokyo, Japan.
    • (1983) The Oxygen Evolving System in Photosynthesis , pp. 73-82
    • Renger, G.1    Eckert, H.J.2    Weiss, W.3
  • 73
    • 0000385466 scopus 로고
    • Temperature dependence of P680+ reduction in O2-evolving PS II membrane fragments at different redox states Si of the water oxidizing system
    • Eckert, H.-J., and Renger, G. (1988) Temperature dependence of P680+ reduction in O2-evolving PS II membrane fragments at different redox states Si of the water oxidizing system, FEBS Lett. 236, 425-431.
    • (1988) FEBS Lett. , vol.236 , pp. 425-431
    • Eckert, H.-J.1    Renger, G.2
  • 74
    • 0032539967 scopus 로고    scopus 로고
    • Proton/hydrogen transfer affects the S-state-dependent microsecond phases of P680+ reduction during water splitting
    • Schilstra, M. J., Rappaport, F., Nugent, J. H., Barnett, C. J., and Klug, D. R. (1998) Proton/hydrogen transfer affects the S-state-dependent microsecond phases of P680+ reduction during water splitting, Biochemistry 37, 3974-3981.
    • (1998) Biochemistry , vol.37 , pp. 3974-3981
    • Schilstra, M.J.1    Rappaport, F.2    Nugent, J.H.3    Barnett, C.J.4    Klug, D.R.5
  • 75
    • 8144219977 scopus 로고    scopus 로고
    • +asterisk inside a circle sign reduction pattern and its temperature dependence in oxygen evolving PS II core complexes from thermophilic cyanobacteria and higher plants
    • +asterisk inside a circle sign reduction pattern and its temperature dependence in oxygen evolving PS II core complexes from thermophilic cyanobacteria and higher plants, Phys. Chem. Chem. Phys. 6, 4838-4843.
    • (2004) Phys. Chem. Chem. Phys. , vol.6 , pp. 4838-4843
    • Kühn, P.1    Eckert, H.-J.2    Eichler, H.J.3    Renger, G.4
  • 76
    • 0002232564 scopus 로고
    • Oxygen evolution in photosynthesis
    • Govindjee, Ed. Academic Press, New York
    • Joliot, P., and Kok, B. (1975) Oxygen evolution in photosynthesis, in Bioenergetics of Photosynthesis (Govindjee, Ed.) pp 387-412, Academic Press, New York.
    • (1975) Bioenergetics of Photosynthesis , pp. 387-412
    • Joliot, P.1    Kok, B.2
  • 77
    • 0042666844 scopus 로고    scopus 로고
    • Functional differences of photosystem II from Synechococcus elongatus and spinach characterized by flash induced oxygen evolution patterns
    • Isgandarova, S., Renger, G., and Messinger, J. (2003) Functional differences of photosystem II from Synechococcus elongatus and spinach characterized by flash induced oxygen evolution patterns, Biochemistry 42, 8929-8938.
    • (2003) Biochemistry , vol.42 , pp. 8929-8938
    • Isgandarova, S.1    Renger, G.2    Messinger, J.3


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