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Volumn 1767, Issue 6, 2007, Pages 565-574

Photosynthetic dioxygen formation studied by time-resolved delayed fluorescence measurements - Method, rationale, and results on the activation energy of dioxygen formation

Author keywords

Chlorophyll fluorescence; Delayed fluorescence; Oxygen evolution; Oxygenic photosynthesis; Photosystem II; Water oxidation

Indexed keywords

CHLOROPHYLL; OXYGEN;

EID: 34249860034     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2007.04.003     Document Type: Article
Times cited : (47)

References (55)
  • 1
    • 0035825682 scopus 로고    scopus 로고
    • Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution
    • Zouni A., Witt H.T., Kern J., Fromme P., Krauss N., Saenger W., and Orth P. Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution. Nature 409 (2001) 739-743
    • (2001) Nature , vol.409 , pp. 739-743
    • Zouni, A.1    Witt, H.T.2    Kern, J.3    Fromme, P.4    Krauss, N.5    Saenger, W.6    Orth, P.7
  • 2
    • 0037422557 scopus 로고    scopus 로고
    • Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7-Å resolution
    • Kamiya N., and Shen J.-R. Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7-Å resolution. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 98-103
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 98-103
    • Kamiya, N.1    Shen, J.-R.2
  • 4
    • 30744445692 scopus 로고    scopus 로고
    • Towards complete cofactor arrangement in the 3.0 A resolution structure of photosystem II
    • Loll B., Kern J., Saenger W., Zouni A., and Biesiadka J. Towards complete cofactor arrangement in the 3.0 A resolution structure of photosystem II. Nature 438 (2005) 1040-1044
    • (2005) Nature , vol.438 , pp. 1040-1044
    • Loll, B.1    Kern, J.2    Saenger, W.3    Zouni, A.4    Biesiadka, J.5
  • 6
    • 13644253100 scopus 로고    scopus 로고
    • A novel BioXAS technique with sub-millisecond time resolution to track oxidation state and structural changes at biological metal centers
    • Haumann M., Müller C., Liebisch P., Neisius T., and Dau H. A novel BioXAS technique with sub-millisecond time resolution to track oxidation state and structural changes at biological metal centers. J. Synchrotron Radiat. 12 (2005) 35-44
    • (2005) J. Synchrotron Radiat. , vol.12 , pp. 35-44
    • Haumann, M.1    Müller, C.2    Liebisch, P.3    Neisius, T.4    Dau, H.5
  • 8
    • 0037208361 scopus 로고    scopus 로고
    • X-ray absorption spectroscopy to watch catalysis by metalloenzymes: status and perspectives discussed for the water-splitting manganese complex of photosynthesis
    • Dau H., and Haumann M. X-ray absorption spectroscopy to watch catalysis by metalloenzymes: status and perspectives discussed for the water-splitting manganese complex of photosynthesis. J. Synchrotron Radiat. 10 (2003) 76-85
    • (2003) J. Synchrotron Radiat. , vol.10 , pp. 76-85
    • Dau, H.1    Haumann, M.2
  • 10
    • 0028155190 scopus 로고
    • Molecular mechanisms and quantitative models of variable photosystem II fluorescence
    • Dau H. Molecular mechanisms and quantitative models of variable photosystem II fluorescence. Photochem. Photobiol. 60 (1994) 1-23
    • (1994) Photochem. Photobiol. , vol.60 , pp. 1-23
    • Dau, H.1
  • 11
    • 0029670893 scopus 로고    scopus 로고
    • Exciton equilibration and photosystem II exciton dynamics - a fluorescence study on photosystem II membrane particles of spinach
    • Dau H., and Sauer K. Exciton equilibration and photosystem II exciton dynamics - a fluorescence study on photosystem II membrane particles of spinach. Biochim. Biophys. Acta 1273 (1996) 175-190
    • (1996) Biochim. Biophys. Acta , vol.1273 , pp. 175-190
    • Dau, H.1    Sauer, K.2
  • 12
    • 3343026433 scopus 로고    scopus 로고
    • Detection of an intermediate of photosynthetic water oxidation
    • Clausen J., and Junge W. Detection of an intermediate of photosynthetic water oxidation. Nature 430 (2004) 480-483
    • (2004) Nature , vol.430 , pp. 480-483
    • Clausen, J.1    Junge, W.2
  • 13
    • 25644458333 scopus 로고    scopus 로고
    • 2 backpressure monitored by delayed chlorophyll fluorescence
    • 2 backpressure monitored by delayed chlorophyll fluorescence. Biochemistry 44 (2005) 12775-12779
    • (2005) Biochemistry , vol.44 , pp. 12775-12779
    • Clausen, J.1    Junge, W.2    Dau, H.3    Haumann, M.4
  • 14
    • 20444495397 scopus 로고    scopus 로고
    • Energetics of primary and secondary electron transfer in Photosystem II membrane particles of spinach revisited on basis of recombination-fluorescence measurements
    • Grabolle M., and Dau H. Energetics of primary and secondary electron transfer in Photosystem II membrane particles of spinach revisited on basis of recombination-fluorescence measurements. Biochim. Biophys. Acta 1708 (2005) 209-218
    • (2005) Biochim. Biophys. Acta , vol.1708 , pp. 209-218
    • Grabolle, M.1    Dau, H.2
  • 15
    • 0014805072 scopus 로고
    • Cooperation of charges in photosynthetic O2 evolution - I
    • Kok B., Forbush B., and McGloin M. Cooperation of charges in photosynthetic O2 evolution - I. Photochem. Photobiol. 11 (1970) 457-475
    • (1970) Photochem. Photobiol. , vol.11 , pp. 457-475
    • Kok, B.1    Forbush, B.2    McGloin, M.3
  • 16
    • 33744992236 scopus 로고    scopus 로고
    • Reaction cycle of photosynthetic water oxidation in plants and cyanobacteria
    • Dau H., and Haumann M. Reaction cycle of photosynthetic water oxidation in plants and cyanobacteria. Science 312 (2006) 1471-1472
    • (2006) Science , vol.312 , pp. 1471-1472
    • Dau, H.1    Haumann, M.2
  • 17
    • 34249847311 scopus 로고    scopus 로고
    • Eight steps preceding O-O bond formation in oxygenic photosynthesis -a basic reaction cycle of the Photosystem II manganese complex
    • 10.1016/j.bbabio.2007.02.022
    • Dau H., and Haumann M. Eight steps preceding O-O bond formation in oxygenic photosynthesis -a basic reaction cycle of the Photosystem II manganese complex. Biochim. Biophys. Acta (2007-this issue) 10.1016/j.bbabio.2007.02.022
    • (2007) Biochim. Biophys. Acta
    • Dau, H.1    Haumann, M.2
  • 18
    • 34249847161 scopus 로고    scopus 로고
    • H. Dau, M. Haumann, Time-resolved X-ray spectroscopy leads to an extension of the classical S-state cycle model of photosynthetic oxygen evolution, Photosynth. Res. (in press).
  • 19
    • 0042846218 scopus 로고
    • Mechanism of delayed light emission by plant leaves and of energy storage in photosynthesis centers
    • Shuvalov V.A., and Litvin F.F. Mechanism of delayed light emission by plant leaves and of energy storage in photosynthesis centers. Mol. Biol. 3 (1969) 59-73
    • (1969) Mol. Biol. , vol.3 , pp. 59-73
    • Shuvalov, V.A.1    Litvin, F.F.2
  • 20
  • 21
    • 0017806672 scopus 로고
    • Interactions of protons with transitions of the watersplitting enzyme of photosystem II as measured by delayed fluorescence
    • Bowes J.M., and Crofts A.R. Interactions of protons with transitions of the watersplitting enzyme of photosystem II as measured by delayed fluorescence. Z. Naturforsch. 33c (1978) 271-275
    • (1978) Z. Naturforsch. , vol.33 c , pp. 271-275
    • Bowes, J.M.1    Crofts, A.R.2
  • 22
    • 0018790158 scopus 로고
    • Effects of pH on reactions on the donor side of photosystem II
    • Bowes J.M., Crofts A.R., and Itoh S. Effects of pH on reactions on the donor side of photosystem II. Biochim. Biophys. Acta 547 (1979) 336-346
    • (1979) Biochim. Biophys. Acta , vol.547 , pp. 336-346
    • Bowes, J.M.1    Crofts, A.R.2    Itoh, S.3
  • 24
    • 0035873926 scopus 로고    scopus 로고
    • Secondary stabilization reactions and proton-coupled electron transport in photosystem II investigated by electroluminescence and fluorescence spectroscopy
    • de Wijn R., Schrama T., and van Gorkom H.J. Secondary stabilization reactions and proton-coupled electron transport in photosystem II investigated by electroluminescence and fluorescence spectroscopy. Biochemistry 40 (2001) 5821-5834
    • (2001) Biochemistry , vol.40 , pp. 5821-5834
    • de Wijn, R.1    Schrama, T.2    van Gorkom, H.J.3
  • 25
    • 0016849620 scopus 로고
    • Identification of the 120 μs phase in the decay of delayed fluorescence in spinach chloroplasts and subchloroplast particles as the intrinsic back reaction. The dependence of the level of this phase on the thylakoids internal pH
    • Haveman J., and Lavorel J. Identification of the 120 μs phase in the decay of delayed fluorescence in spinach chloroplasts and subchloroplast particles as the intrinsic back reaction. The dependence of the level of this phase on the thylakoids internal pH. Biochim. Biophys. Acta 408 (1975) 269-283
    • (1975) Biochim. Biophys. Acta , vol.408 , pp. 269-283
    • Haveman, J.1    Lavorel, J.2
  • 26
    • 0026566266 scopus 로고
    • Studies on the reaction coordinates of the water oxidase in PS II membrane fragments from spinach
    • Renger G., and Hanssum B. Studies on the reaction coordinates of the water oxidase in PS II membrane fragments from spinach. FEBS Lett. 299 (1992) 28-32
    • (1992) FEBS Lett. , vol.299 , pp. 28-32
    • Renger, G.1    Hanssum, B.2
  • 27
    • 1942504766 scopus 로고    scopus 로고
    • Time-resolved oxygen production by PSII: chasing chemical intermediates
    • Clausen J., Debus R.J., and Junge W. Time-resolved oxygen production by PSII: chasing chemical intermediates. Biochim. Biophys. Acta 1655 (2004) 184-194
    • (2004) Biochim. Biophys. Acta , vol.1655 , pp. 184-194
    • Clausen, J.1    Debus, R.J.2    Junge, W.3
  • 28
    • 0033923947 scopus 로고    scopus 로고
    • Preparation protocols for high-activity Photosystem II membrane particles of green algae and higher plants, pH dependence of oxygen evolution and comparison of the S2-state multiline signal by X-band EPR spectroscopy
    • Schiller H., and Dau H. Preparation protocols for high-activity Photosystem II membrane particles of green algae and higher plants, pH dependence of oxygen evolution and comparison of the S2-state multiline signal by X-band EPR spectroscopy. J. Photochem. Photobiol., B Biol. 55 (2000) 138-144
    • (2000) J. Photochem. Photobiol., B Biol. , vol.55 , pp. 138-144
    • Schiller, H.1    Dau, H.2
  • 29
    • 3042829732 scopus 로고
    • Light production by green plants
    • Strehler B., and Arnold W. Light production by green plants. J. Gen. Physiol. 34 (1951) 809-820
    • (1951) J. Gen. Physiol. , vol.34 , pp. 809-820
    • Strehler, B.1    Arnold, W.2
  • 31
    • 0033916252 scopus 로고    scopus 로고
    • Quinone-dependent delayed fluorescence from the reaction center of photosynthetic bacteria
    • Turzó K., Laczkó G., Filus Z., and Maróti P. Quinone-dependent delayed fluorescence from the reaction center of photosynthetic bacteria. Biophys. J. 79 (2000) 14-25
    • (2000) Biophys. J. , vol.79 , pp. 14-25
    • Turzó, K.1    Laczkó, G.2    Filus, Z.3    Maróti, P.4
  • 32
    • 0035873926 scopus 로고    scopus 로고
    • Secondary stabilization reactions and proton-coupled electron transport in photosystem II investigated by electroluminescence and fluorescence spectroscopy
    • de Wijn R., Schrama T., and van Gorkom H.J. Secondary stabilization reactions and proton-coupled electron transport in photosystem II investigated by electroluminescence and fluorescence spectroscopy. Biochemistry 40 (2001) 5821-5834
    • (2001) Biochemistry , vol.40 , pp. 5821-5834
    • de Wijn, R.1    Schrama, T.2    van Gorkom, H.J.3
  • 33
    • 0000463343 scopus 로고
    • Charge accumulation and photochemistry in leaves studied by thermoluminescence and delayed light emission
    • Rutherford A.W., Govindjee, and Inoue Y. Charge accumulation and photochemistry in leaves studied by thermoluminescence and delayed light emission. Proc. Natl. Acad. Sci. U. S. A. 81 (1983) 1107-1111
    • (1983) Proc. Natl. Acad. Sci. U. S. A. , vol.81 , pp. 1107-1111
    • Rutherford, A.W.1    Govindjee2    Inoue, Y.3
  • 34
    • 0019879486 scopus 로고
    • Photosynthetic energy conservation investigated by thermoluminescence. Activation energies and half-lives of thermoluminescence bands of chloroplasts determined by mathematical resolution of glow curves
    • Vass I., Horvath G., Herczeg T., and Demeter S. Photosynthetic energy conservation investigated by thermoluminescence. Activation energies and half-lives of thermoluminescence bands of chloroplasts determined by mathematical resolution of glow curves. Biochim. Biophys. Acta 634 (1981) 140-152
    • (1981) Biochim. Biophys. Acta , vol.634 , pp. 140-152
    • Vass, I.1    Horvath, G.2    Herczeg, T.3    Demeter, S.4
  • 35
    • 0029998586 scopus 로고    scopus 로고
    • Thermoluminescence from the photosynthetic apparatus
    • Vass I., and Govindjee. Thermoluminescence from the photosynthetic apparatus. Photosynth. Res. 48 (1996) 117-126
    • (1996) Photosynth. Res. , vol.48 , pp. 117-126
    • Vass, I.1    Govindjee2
  • 36
    • 34249851838 scopus 로고    scopus 로고
    • A.D. Tsamaloukas, Fluoreszenzspektroskopie zur Excitonendynamik in den Chlorophyll-Antennen des Photosystems II der Pflanzen, Diploma thesis, FB Physik, FU Berlin (2001).
  • 37
    • 0014400748 scopus 로고
    • Analysis of the interactions between the two photosystems in isolated chloroplasts
    • Joliot P., and Joliot A. Analysis of the interactions between the two photosystems in isolated chloroplasts. Biochim. Biophys. Acta 153 (1968) 635-652
    • (1968) Biochim. Biophys. Acta , vol.153 , pp. 635-652
    • Joliot, P.1    Joliot, A.2
  • 38
    • 0029006897 scopus 로고
    • Theory of fluorescence induction in photosystem II: derivation of analytical expressions in a model including exciton-radical-pair equilibrium and restricted energy transfer between photosynthetic units
    • Lavergne J., and Trissl H.W. Theory of fluorescence induction in photosystem II: derivation of analytical expressions in a model including exciton-radical-pair equilibrium and restricted energy transfer between photosynthetic units. Biophys. J. 68 (1995) 2474-2492
    • (1995) Biophys. J. , vol.68 , pp. 2474-2492
    • Lavergne, J.1    Trissl, H.W.2
  • 40
    • 0033578366 scopus 로고    scopus 로고
    • Modulation of flash-induced photosystem II fluorescence by events occurring at the water oxidizing complex
    • Putrenko II, Vasil'ev S., and Bruce S.D. Modulation of flash-induced photosystem II fluorescence by events occurring at the water oxidizing complex. Biochemistry 38 (1999) 10632-10641
    • (1999) Biochemistry , vol.38 , pp. 10632-10641
    • Putrenko II1    Vasil'ev, S.2    Bruce, S.D.3
  • 41
    • 0028290024 scopus 로고
    • The rates of proton uptake and electron transfer at the reducing side of photosystem II in thylakoids
    • Haumann M., and Junge W. The rates of proton uptake and electron transfer at the reducing side of photosystem II in thylakoids. FEBS Lett. 347 (1994) 45-50
    • (1994) FEBS Lett. , vol.347 , pp. 45-50
    • Haumann, M.1    Junge, W.2
  • 42
    • 48749143707 scopus 로고
    • The electrochemical domain of photosynthesis
    • Crofts A.R., and Wraight C.A. The electrochemical domain of photosynthesis. Biochim. Biophys. Acta 726 (1983) 149-185
    • (1983) Biochim. Biophys. Acta , vol.726 , pp. 149-185
    • Crofts, A.R.1    Wraight, C.A.2
  • 43
    • 0019320156 scopus 로고
    • Binary oscillations in the rate of reoxidation of the primary acceptor of photosystem
    • Bowes J.M., and Crofts A.R. Binary oscillations in the rate of reoxidation of the primary acceptor of photosystem. Biochim. Biophys. Acta 590 (1980) 373-384
    • (1980) Biochim. Biophys. Acta , vol.590 , pp. 373-384
    • Bowes, J.M.1    Crofts, A.R.2
  • 44
    • 0041622652 scopus 로고    scopus 로고
    • Coupling of light-induced electron transfer to proton uptake in photosynthesis
    • Remy A., and Gerwert K. Coupling of light-induced electron transfer to proton uptake in photosynthesis. Nat. Struct. Biol. 10 (2003) 637-644
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 637-644
    • Remy, A.1    Gerwert, K.2
  • 46
    • 34249849848 scopus 로고    scopus 로고
    • M. Grabolle, Die Donorseite des Photosystems II: Rekombinationsfluoreszenz- und Röntgenabsorptionsstudien (thesis), Fachbereich Physik, Freie Univ. Berlin, http://www.diss.fu-berlin.de/2005/174/ (2005).
  • 47
    • 23444440334 scopus 로고    scopus 로고
    • Specific loss of the extrinsic 18 KDa protein from photosystem II upon heating to 47 degrees C causes inactivation of oxygen evolution likely due to Ca release from the Mn-complex
    • Barra M., Haumann M., and Dau H. Specific loss of the extrinsic 18 KDa protein from photosystem II upon heating to 47 degrees C causes inactivation of oxygen evolution likely due to Ca release from the Mn-complex. Photosynth. Res. 84 (2005) 231-237
    • (2005) Photosynth. Res. , vol.84 , pp. 231-237
    • Barra, M.1    Haumann, M.2    Dau, H.3
  • 48
    • 33845307608 scopus 로고    scopus 로고
    • Intermediates in assembly by photoactivation after thermally accelerated disassembly of the manganese complex of photosynthetic water oxidation
    • Barra M., Haumann M., Loja P., Krivanek R., Grundmeier A., and Dau H. Intermediates in assembly by photoactivation after thermally accelerated disassembly of the manganese complex of photosynthetic water oxidation. Biochemistry 45 (2006) 14523-14532
    • (2006) Biochemistry , vol.45 , pp. 14523-14532
    • Barra, M.1    Haumann, M.2    Loja, P.3    Krivanek, R.4    Grundmeier, A.5    Dau, H.6
  • 50
    • 27744509042 scopus 로고    scopus 로고
    • Photosynthetic O2 formation tracked by time-resolved X-ray experiments
    • Haumann M., Liebisch P., Muller C., Barra M., Grabolle M., and Dau H. Photosynthetic O2 formation tracked by time-resolved X-ray experiments. Science 310 (2005) 1019-1021
    • (2005) Science , vol.310 , pp. 1019-1021
    • Haumann, M.1    Liebisch, P.2    Muller, C.3    Barra, M.4    Grabolle, M.5    Dau, H.6
  • 51
    • 0030970415 scopus 로고    scopus 로고
    • Photosynthetic oxygen evolution: H/D isotope effects and the coupling between electron and proton transfer during the redox reactions at the oxidizing side of Photosystem
    • Haumann M., Bögershausen O., Cherepanov D., Ahlbrink R., and Junge W. Photosynthetic oxygen evolution: H/D isotope effects and the coupling between electron and proton transfer during the redox reactions at the oxidizing side of Photosystem. Photosynth. Res. 51 (1997) 193-208
    • (1997) Photosynth. Res. , vol.51 , pp. 193-208
    • Haumann, M.1    Bögershausen, O.2    Cherepanov, D.3    Ahlbrink, R.4    Junge, W.5
  • 52
    • 0028047699 scopus 로고
    • Extent and rate of proton release by photosynthetic water oxidation in thylakoids: electrostatic relaxation versus chemical production
    • Haumann M., and Junge W. Extent and rate of proton release by photosynthetic water oxidation in thylakoids: electrostatic relaxation versus chemical production. Biochemistry 33 (1994) 864-872
    • (1994) Biochemistry , vol.33 , pp. 864-872
    • Haumann, M.1    Junge, W.2
  • 53
    • 0000575451 scopus 로고
    • Temperature dependence of S-state transition in a thermophilic cyanobacterium, Synechococcus vulcanus Copeland measured by absorption changes in the ultraviolet region
    • Koike H., Hanssum B., Inoue Y., and Renger G. Temperature dependence of S-state transition in a thermophilic cyanobacterium, Synechococcus vulcanus Copeland measured by absorption changes in the ultraviolet region. Biochim. Biophys. Acta 893 (1987) 524-533
    • (1987) Biochim. Biophys. Acta , vol.893 , pp. 524-533
    • Koike, H.1    Hanssum, B.2    Inoue, Y.3    Renger, G.4
  • 54
    • 33144471312 scopus 로고    scopus 로고
    • Energetics of a possible proton exit pathway for water oxidation in photosystem II
    • Ishikita H., Saenger W., Loll B., Biesiadka J., and Knapp E.W. Energetics of a possible proton exit pathway for water oxidation in photosystem II. Biochemistry 45 (2006) 2063-2071
    • (2006) Biochemistry , vol.45 , pp. 2063-2071
    • Ishikita, H.1    Saenger, W.2    Loll, B.3    Biesiadka, J.4    Knapp, E.W.5
  • 55
    • 0028344645 scopus 로고
    • Kinetics of electron transfer and electrochromic change during the redox transition of the photosynthetic oxygen-evolving complex
    • Rappaport F., Blanchard-Desce M., and Lavergne J. Kinetics of electron transfer and electrochromic change during the redox transition of the photosynthetic oxygen-evolving complex. Biochim. Biophys. Acta 1184 (1994) 178-192
    • (1994) Biochim. Biophys. Acta , vol.1184 , pp. 178-192
    • Rappaport, F.1    Blanchard-Desce, M.2    Lavergne, J.3


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