메뉴 건너뛰기




Volumn 1817, Issue 11, 2012, Pages 1998-2004

Influence of the PsbA1/PsbA3, Ca2+/Sr2+ and Cl -/Br- exchanges on the redox potential of the primary quinone QA in Photosystem II from Thermosynechococcus elongatus as revealed by spectroelectrochemistry

Author keywords

D1 protein; Electron transfer; Photosystem II; PsbA protein; Redox potential

Indexed keywords

BACTERIAL PROTEIN; BROMINE; CALCIUM; CHLORIDE; PROTEIN PSBA1; PROTEIN PSBA3; QUINONE DERIVATIVE; STRONTIUM; UNCLASSIFIED DRUG;

EID: 84865682899     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2012.06.006     Document Type: Article
Times cited : (30)

References (64)
  • 1
    • 85028099698 scopus 로고    scopus 로고
    • Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9 Å
    • Y. Umena, K. Kawakami, J.-R. Shen, and N. Kamiya Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9 Å Nature 473 2011 55 60
    • (2011) Nature , vol.473 , pp. 55-60
    • Umena, Y.1    Kawakami, K.2    Shen, J.-R.3    Kamiya, N.4
  • 2
    • 0014805072 scopus 로고
    • Cooperation of charges in photosynthetic oxygen evolution. I. A linear four step mechanism
    • B. Kok, B. Forbush, and M. McGloin Cooperation of charges in photosynthetic oxygen evolution. I. A linear four step mechanism Photochem. Photobiol. 11 1970 457 475
    • (1970) Photochem. Photobiol. , vol.11 , pp. 457-475
    • Kok, B.1    Forbush, B.2    McGloin, M.3
  • 3
    • 0042360203 scopus 로고    scopus 로고
    • Period-four oscillations of the flash-induced oxygen formation in photosynthesis
    • P. Joliot Period-four oscillations of the flash-induced oxygen formation in photosynthesis Photosynth. Res. 76 2003 65 72
    • (2003) Photosynth. Res. , vol.76 , pp. 65-72
    • Joliot, P.1
  • 4
  • 5
    • 0026707522 scopus 로고
    • The manganese and calcium ions of photosynthetic oxygen evolution
    • R.J. Debus The manganese and calcium ions of photosynthetic oxygen evolution Biochim. Biophys. Acta 1102 1992 269 352
    • (1992) Biochim. Biophys. Acta , vol.1102 , pp. 269-352
    • Debus, R.J.1
  • 6
    • 0025008019 scopus 로고
    • Histidine oxidation in the oxygen-evolving photosystem II enzyme
    • A. Boussac, J.-L. Zimmermann, A.W. Rutherford, and J. Lavergne Histidine oxidation in the oxygen-evolving photosystem II enzyme Nature 347 1990 303 306
    • (1990) Nature , vol.347 , pp. 303-306
    • Boussac, A.1    Zimmermann, J.-L.2    Rutherford, A.W.3    Lavergne, J.4
  • 7
    • 0029760320 scopus 로고    scopus 로고
    • Manganese-tyrosine interaction in the Photosystem II oxygen-evolving complex
    • X.-S. Tang, D.W. Randall, D.A. Force, B.A. Diner, and R.D. Britt Manganese-tyrosine interaction in the Photosystem II oxygen-evolving complex J. Am. Chem. Soc. 118 1996 7638 7639
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 7638-7639
    • Tang, X.-S.1    Randall, D.W.2    Force, D.A.3    Diner, B.A.4    Britt, R.D.5
  • 8
    • 0000981541 scopus 로고
    • Calcium reconstitutes high rates of oxygen evolution in polypeptide depleted Photosystem II preparations
    • D.F. Ghanotakis, G.T. Babcock, and C.F. Yocum Calcium reconstitutes high rates of oxygen evolution in polypeptide depleted Photosystem II preparations FEBS Lett. 167 1984 127 130
    • (1984) FEBS Lett. , vol.167 , pp. 127-130
    • Ghanotakis, D.F.1    Babcock, G.T.2    Yocum, C.F.3
  • 10
    • 33947371680 scopus 로고    scopus 로고
    • 2+ in the oxygen-evolving complex of photosystem II by metal ion inhibition
    • 2+ in the oxygen-evolving complex of photosystem II by metal ion inhibition Biochemistry 46 2007 3211 3233
    • (2007) Biochemistry , vol.46 , pp. 3211-3233
    • Lee, C.-I.1    Lakshmi, K.V.2    Brudvig, G.W.3
  • 11
    • 79953709742 scopus 로고    scopus 로고
    • Chloride regulation of enzyme turnover: Application to the role of chloride in photosystem II
    • R. Pokhrel, I.L. McConnell, and G.W. Brudvig Chloride regulation of enzyme turnover: application to the role of chloride in photosystem II Biochemistry 50 2011 2725 2734
    • (2011) Biochemistry , vol.50 , pp. 2725-2734
    • Pokhrel, R.1    McConnell, I.L.2    Brudvig, G.W.3
  • 13
    • 66649106614 scopus 로고    scopus 로고
    • Location of chloride and its possible functions in oxygen-evolving photosystem II revealed by X-ray crystallography
    • K. Kawakami, Y. Umena, N. Kamiya, and J.-R. Shen Location of chloride and its possible functions in oxygen-evolving photosystem II revealed by X-ray crystallography Proc. Natl. Acad. Sci. U. S. A. 106 2009 8567 8572
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 8567-8572
    • Kawakami, K.1    Umena, Y.2    Kamiya, N.3    Shen, J.-R.4
  • 14
    • 84858723493 scopus 로고    scopus 로고
    • Probing the role of chloride in Photosystem II from Thermosynechococcus elongatus by exchanging chloride for iodide
    • A. Boussac, N. Ishida, M. Sugiura, and F. Rappaport Probing the role of chloride in Photosystem II from Thermosynechococcus elongatus by exchanging chloride for iodide Biochim. Biophys. Acta 1817 2012 802 810
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 802-810
    • Boussac, A.1    Ishida, N.2    Sugiura, M.3    Rappaport, F.4
  • 16
    • 0017798923 scopus 로고
    • The role of chloride ion in Photosystem II: I. Effects of chloride ion on Photosystem II electron transport and on hydroxylamine inhibition
    • P.M. Kelley, and S. Izawa The role of chloride ion in Photosystem II: I. Effects of chloride ion on Photosystem II electron transport and on hydroxylamine inhibition Biochim. Biophys. Acta 502 1978 198 210
    • (1978) Biochim. Biophys. Acta , vol.502 , pp. 198-210
    • Kelley, P.M.1    Izawa, S.2
  • 17
    • 45149089916 scopus 로고    scopus 로고
    • Biosynthetic exchange of bromide for calcium in the photosystem II oxygen-evolving enzymes
    • N. Ishida, M. Sugiura, F. Rappaport, T.-L. Lai, A.W. Rutherford, and A. Boussac Biosynthetic exchange of bromide for calcium in the photosystem II oxygen-evolving enzymes J. Biol. Chem. 283 2008 13330 13340
    • (2008) J. Biol. Chem. , vol.283 , pp. 13330-13340
    • Ishida, N.1    Sugiura, M.2    Rappaport, F.3    Lai, T.-L.4    Rutherford, A.W.5    Boussac, A.6
  • 19
    • 79959820864 scopus 로고    scopus 로고
    • 2+ determines the entropy changes associated with the formation of transition states during water oxidation by Photosystem II
    • 2+ determines the entropy changes associated with the formation of transition states during water oxidation by Photosystem II Energy Environ. Sci. 4 2011 2520 2524
    • (2011) Energy Environ. Sci. , vol.4 , pp. 2520-2524
    • Rappaport, F.1    Ishida, N.2    Sugiura, M.3    Boussac, A.4
  • 20
    • 34249807336 scopus 로고    scopus 로고
    • Purification, crystallization and X-ray diffraction analyses of the T. elongatus PSII core dimer with strontium replacing calcium in the oxygen-evolving complex
    • J. Kargul, K. Maghlaoui, J.W. Murray, Z. Deak, A. Boussac, A.W. Rutherford, I. Vass, and J. Barber Purification, crystallization and X-ray diffraction analyses of the T. elongatus PSII core dimer with strontium replacing calcium in the oxygen-evolving complex Biochim. Biophys. Acta 1767 2007 404 413
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 404-413
    • Kargul, J.1    Maghlaoui, K.2    Murray, J.W.3    Deak, Z.4    Boussac, A.5    Rutherford, A.W.6    Vass, I.7    Barber, J.8
  • 21
    • 0028980975 scopus 로고
    • 2+ depletion modifies the electron transfer on both donor and acceptor sides in Photosystem II from spinach
    • 2+ depletion modifies the electron transfer on both donor and acceptor sides in Photosystem II from spinach Biochim. Biophys. Acta 1230 1995 155 164
    • (1995) Biochim. Biophys. Acta , vol.1230 , pp. 155-164
    • Andréasson, L.-E.1    Vass, I.2    Styring, S.3
  • 22
    • 73449135829 scopus 로고    scopus 로고
    • Documentation of significant electron transport defects on the reducing side of photosystem II upon removal of the PsbP and PsbQ extrinsic proteins
    • J.L. Roose, L.K. Ranckel, and T.M. Bricker Documentation of significant electron transport defects on the reducing side of photosystem II upon removal of the PsbP and PsbQ extrinsic proteins Biochemistry 49 2010 36 41
    • (2010) Biochemistry , vol.49 , pp. 36-41
    • Roose, J.L.1    Ranckel, L.K.2    Bricker, T.M.3
  • 23
    • 0002561024 scopus 로고
    • Energy-dependent of chlorophyll-a-fluorescence: The involvement of proton-calcium exchange at photosystem 2
    • A. Krieger, and E. Weis Energy-dependent of chlorophyll-a-fluorescence: the involvement of proton-calcium exchange at photosystem 2 Photosynthetica 27 1992 89 98
    • (1992) Photosynthetica , vol.27 , pp. 89-98
    • Krieger, A.1    Weis, E.2
  • 26
    • 70449580488 scopus 로고    scopus 로고
    • A in photosystem II from Thermosynechococcus elongatus determined by spectroelectrochemistry
    • A in photosystem II from Thermosynechococcus elongatus determined by spectroelectrochemistry Biochemistry 48 2009 10682 10684
    • (2009) Biochemistry , vol.48 , pp. 10682-10684
    • Shibamoto, T.1    Kato, Y.2    Sugiura, M.3    Watanabe, T.4
  • 28
    • 41249098659 scopus 로고    scopus 로고
    • Influence of Histidine-198 of the D1 subunit on the properties of the primary electron donor, P680, of photosystem II in Thermosynechococcus elongatus
    • M. Sugiura, A. Boussac, T. Noguchi, and F. Rappaport Influence of Histidine-198 of the D1 subunit on the properties of the primary electron donor, P680, of photosystem II in Thermosynechococcus elongatus Biochim. Biophys. Acta 1777 2008 331 342
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 331-342
    • Sugiura, M.1    Boussac, A.2    Noguchi, T.3    Rappaport, F.4
  • 29
    • 70749136825 scopus 로고    scopus 로고
    • Cyanobacterial psbA gene family: Optimization of oxygenic photosynthesis
    • P. Mulo, C. Sicora, and E.-M. Aro Cyanobacterial psbA gene family: optimization of oxygenic photosynthesis Cell. Mol. Life Sci. 66 2009 3697 3710
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 3697-3710
    • Mulo, P.1    Sicora, C.2    Aro, E.-M.3
  • 31
    • 37549052159 scopus 로고    scopus 로고
    • Differential regulation of psbA and psbD gene expression, and the role of the different D1 protein copies in the cyanobacterium Thermosynechococcus elongatus BP-1
    • P.B. Kós, Z. Deak, O. Cheregi, and I. Vass Differential regulation of psbA and psbD gene expression, and the role of the different D1 protein copies in the cyanobacterium Thermosynechococcus elongatus BP-1 Biochim. Biophys. Acta 1777 2008 74 83
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 74-83
    • Kós, P.B.1    Deak, Z.2    Cheregi, O.3    Vass, I.4
  • 32
    • 45749102065 scopus 로고    scopus 로고
    • Modeling of variant copies of subunit D1 in the structure of photosystem II from Thermosynechococcus elongatus
    • B. Loll, M. Broser, P.B. Kós, J. Kern, J. Biesiadka, I. Vass, W. Saenger, and A. Zouni Modeling of variant copies of subunit D1 in the structure of photosystem II from Thermosynechococcus elongatus Biol. Chem. 389 2008 609 617
    • (2008) Biol. Chem. , vol.389 , pp. 609-617
    • Loll, B.1    Broser, M.2    Kós, P.B.3    Kern, J.4    Biesiadka, J.5    Vass, I.6    Saenger, W.7    Zouni, A.8
  • 33
    • 77956899459 scopus 로고    scopus 로고
    • Functional characterization and quantification of the alternative PsbA copies in Thermosynechococcus elongatus and their role in photoprotection
    • J. Sander, M. Nowaczyk, J. Buchta, H. Dau, I. Vass, Z. Deák, M. Dorogi, M. Iwai, and M. Rögner Functional characterization and quantification of the alternative PsbA copies in Thermosynechococcus elongatus and their role in photoprotection J. Biol. Chem. 285 2010 29851 29856
    • (2010) J. Biol. Chem. , vol.285 , pp. 29851-29856
    • Sander, J.1    Nowaczyk, M.2    Buchta, J.3    Dau, H.4    Vass, I.5    Deák, Z.6    Dorogi, M.7    Iwai, M.8    Rögner, M.9
  • 34
    • 58649102249 scopus 로고    scopus 로고
    • Transcription of a "silent" cyanobacterial psbA gene is induced by microaerobic conditions
    • C.I. Sicora, F.M. Ho, T. Salminen, S. Styring, and E.-M. Aro Transcription of a "silent" cyanobacterial psbA gene is induced by microaerobic conditions Biochim. Biophys. Acta 1787 2009 105 112
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 105-112
    • Sicora, C.I.1    Ho, F.M.2    Salminen, T.3    Styring, S.4    Aro, E.-M.5
  • 36
    • 84859760209 scopus 로고    scopus 로고
    • Environment of TyrZ in Photosystem II from Thermosynechococcus elongatus in which PsbA2 is the D1 protein
    • M. Sugiura, S. Ogami, M. Kusumi, S. Un, F. Rappaport, and A. Boussac Environment of TyrZ in Photosystem II from Thermosynechococcus elongatus in which PsbA2 is the D1 protein J. Biol. Chem. 287 2012 13336 13347
    • (2012) J. Biol. Chem. , vol.287 , pp. 13336-13347
    • Sugiura, M.1    Ogami, S.2    Kusumi, M.3    Un, S.4    Rappaport, F.5    Boussac, A.6
  • 37
    • 84862236719 scopus 로고    scopus 로고
    • Deactivation processes in PsbA1-Photosystem II and PsbA3-Photosystem II under photoinhibitory conditions in the cyanobacterium Thermosynechococcus elongatus
    • S. Ogami, A. Boussac, and M. Sugiura Deactivation processes in PsbA1-Photosystem II and PsbA3-Photosystem II under photoinhibitory conditions in the cyanobacterium Thermosynechococcus elongatus Biochim. Biophys. Acta 1817 2012 1322 1330
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 1322-1330
    • Ogami, S.1    Boussac, A.2    Sugiura, M.3
  • 38
    • 0033401728 scopus 로고    scopus 로고
    • Highly purified thermo-stable oxygen-evolving photosystem II core complex from the thermophilic Cyanobacterium Synechococcus elongatus having His-tagged CP43
    • M. Sugiura, and Y. Inoue Highly purified thermo-stable oxygen-evolving photosystem II core complex from the thermophilic Cyanobacterium Synechococcus elongatus having His-tagged CP43 Plant Cell Physiol. 40 1999 1219 1231
    • (1999) Plant Cell Physiol. , vol.40 , pp. 1219-1231
    • Sugiura, M.1    Inoue, Y.2
  • 39
    • 4444296961 scopus 로고    scopus 로고
    • Spectroelectrochemical determination of the redox potential of P700 in spinach with an optically transparent thin-layer electrode
    • A. Nakamura, T. Suzawa, and T. Watanabe Spectroelectrochemical determination of the redox potential of P700 in spinach with an optically transparent thin-layer electrode Chem. Lett. 33 2004 688 689
    • (2004) Chem. Lett. , vol.33 , pp. 688-689
    • Nakamura, A.1    Suzawa, T.2    Watanabe, T.3
  • 40
    • 15744401383 scopus 로고    scopus 로고
    • Functional consequences of the organization of the photosynthetic apparatus in Rhodobacter sphaeroides
    • F. Comayras, C. Jungas, and J. Lavergne Functional consequences of the organization of the photosynthetic apparatus in Rhodobacter sphaeroides J. Biol. Chem. 280 2005 11203 11213
    • (2005) J. Biol. Chem. , vol.280 , pp. 11203-11213
    • Comayras, F.1    Jungas, C.2    Lavergne, J.3
  • 41
    • 70350434324 scopus 로고    scopus 로고
    • Spectroelectrochemical determination of the redox potential of pheophytin a, the primary electron acceptor in photosystem II
    • Y. Kato, M. Sugiura, A. Oda, and T. Watanabe Spectroelectrochemical determination of the redox potential of pheophytin a, the primary electron acceptor in photosystem II Proc. Natl. Acad. Sci. U. S. A. 106 2009 17365 17370
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 17365-17370
    • Kato, Y.1    Sugiura, M.2    Oda, A.3    Watanabe, T.4
  • 42
    • 74949118292 scopus 로고    scopus 로고
    • Hydrogen bond interactions of the pheophytin electron acceptor and its radical anion in photosystem II as revealed by Fourier transform infrared difference spectroscopy
    • Y. Shibuya, R. Takahashi, T. Okubo, H. Suzuki, M. Sugiura, and T. Noguchi Hydrogen bond interactions of the pheophytin electron acceptor and its radical anion in photosystem II as revealed by Fourier transform infrared difference spectroscopy Biochemistry 49 2010 493 501
    • (2010) Biochemistry , vol.49 , pp. 493-501
    • Shibuya, Y.1    Takahashi, R.2    Okubo, T.3    Suzuki, H.4    Sugiura, M.5    Noguchi, T.6
  • 43
    • 17144386774 scopus 로고    scopus 로고
    • Charge recombination and thermoluminescence in Photosystem II
    • F. Rappaport, A. Cuni, L. Xiong, R. Sayre, and J. Lavergne Charge recombination and thermoluminescence in Photosystem II Biophys. J. 88 2005 1948 1958
    • (2005) Biophys. J. , vol.88 , pp. 1948-1958
    • Rappaport, F.1    Cuni, A.2    Xiong, L.3    Sayre, R.4    Lavergne, J.5
  • 45
    • 0030068901 scopus 로고    scopus 로고
    • Comparison of primary charge separation in the Photosystem II reaction center complex isolated from wild-type and D1-130 mutants of the cyanobacterium Synechocystis PCC 6803
    • L.B. Giorgi, P.J. Nixon, S.A.P. Merry, D.M. Joseph, J.R. Durrant, J.D.L. Rivas, J. Barber, G. Porter, and D.R. Klug Comparison of primary charge separation in the Photosystem II reaction center complex isolated from wild-type and D1-130 mutants of the cyanobacterium Synechocystis PCC 6803 J. Biol. Chem. 271 1996 2093 2101
    • (1996) J. Biol. Chem. , vol.271 , pp. 2093-2101
    • Giorgi, L.B.1    Nixon, P.J.2    Merry, S.A.P.3    Joseph, D.M.4    Durrant, J.R.5    Rivas, J.D.L.6    Barber, J.7    Porter, G.8    Klug, D.R.9
  • 46
    • 0032534935 scopus 로고    scopus 로고
    • Modulation of quantum yield of primary radical pair formation in Photosystem II by site-directed mutagenesis affecting radical cations and anions
    • S.A.P. Merry, P.J. Nixon, L.M.C. Barter, M. Schilstra, G. Porter, J. Barger, J.R. Durrant, and D.R. Klug Modulation of quantum yield of primary radical pair formation in Photosystem II by site-directed mutagenesis affecting radical cations and anions Biochemistry 37 1998 17439 17447
    • (1998) Biochemistry , vol.37 , pp. 17439-17447
    • Merry, S.A.P.1    Nixon, P.J.2    Barter, L.M.C.3    Schilstra, M.4    Porter, G.5    Barger, J.6    Durrant, J.R.7    Klug, D.R.8
  • 47
    • 33947139255 scopus 로고    scopus 로고
    • Radiative and non-radiative charge recombination pathways in Photosystem II studied by thermoluminescence and chlorophyll fluorescence in the cyanobacterium Synechocystis 6803
    • K. Cser, and I. Vass Radiative and non-radiative charge recombination pathways in Photosystem II studied by thermoluminescence and chlorophyll fluorescence in the cyanobacterium Synechocystis 6803 Biochim. Biophys. Acta 1767 2007 233 243
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 233-243
    • Cser, K.1    Vass, I.2
  • 48
    • 38949201008 scopus 로고    scopus 로고
    • Low-temperature photochemistry in photosystem II from Thermosynechococcus elongatus induced by visible and near-infrared light
    • A. Boussac, M. Sugiura, T.-L. Lai, and A.W. Rutherford Low-temperature photochemistry in photosystem II from Thermosynechococcus elongatus induced by visible and near-infrared light Philos. Trans. R. Soc. B Biol Sci 363 2008 1203 1210
    • (2008) Philos. Trans. R. Soc. B Biol Sci , vol.363 , pp. 1203-1210
    • Boussac, A.1    Sugiura, M.2    Lai, T.-L.3    Rutherford, A.W.4
  • 49
    • 20544470177 scopus 로고    scopus 로고
    • Evidence from biosynthetically incorporated strontium and FTIR difference spectroscopy that the C-terminus of the D1 polypeptide of photosystem II does not ligate calcium
    • M.A. Strickler, L.M. Walker, W. Hillier, and R.J. Debus Evidence from biosynthetically incorporated strontium and FTIR difference spectroscopy that the C-terminus of the D1 polypeptide of photosystem II does not ligate calcium Biochemistry 44 2005 8571 8577
    • (2005) Biochemistry , vol.44 , pp. 8571-8577
    • Strickler, M.A.1    Walker, L.M.2    Hillier, W.3    Debus, R.J.4
  • 50
    • 23444446347 scopus 로고    scopus 로고
    • Studies on photosynthetic oxygen-evolving complex by means of Fourier transform infrared spectroscopy: Calcium and chloride cofactors
    • Y. Kimura, K. Hasegawa, T. Yamanari, and T.-A. Ono Studies on photosynthetic oxygen-evolving complex by means of Fourier transform infrared spectroscopy: calcium and chloride cofactors Photosynth. Res. 84 2005 245 250
    • (2005) Photosynth. Res. , vol.84 , pp. 245-250
    • Kimura, Y.1    Hasegawa, K.2    Yamanari, T.3    Ono, T.-A.4
  • 51
    • 33751005603 scopus 로고    scopus 로고
    • 2+ exchange in the S-state cycle of photosynthetic oxygen evolution as studied by flash-induced FTIR difference spectroscopy
    • 2+ exchange in the S-state cycle of photosynthetic oxygen evolution as studied by flash-induced FTIR difference spectroscopy Biochemistry 45 2006 13454 13464
    • (2006) Biochemistry , vol.45 , pp. 13454-13464
    • Suzuki, H.1    Taguchi, Y.2    Sugiura, M.3    Boussac, A.4    Noguchi, T.5
  • 54
    • 49049126264 scopus 로고
    • Kinetics of the oxidation-reductions of the photosystem II quinone acceptor complex, and the pathway for deactivation
    • H.H. Robinson, and A.R. Crofts Kinetics of the oxidation-reductions of the photosystem II quinone acceptor complex, and the pathway for deactivation FEBS Lett. 153 1983 221 226
    • (1983) FEBS Lett. , vol.153 , pp. 221-226
    • Robinson, H.H.1    Crofts, A.R.2
  • 55
    • 0009914004 scopus 로고
    • Comparative thermoluminescence study of triazine-resistant and -susceptible biotypes of Erigeron canadensis L
    • S. Demeter, I. Vass, É. Hideg, and A. Sallai Comparative thermoluminescence study of triazine-resistant and -susceptible biotypes of Erigeron canadensis L Biochim. Biophys. Acta 806 1985 16 24
    • (1985) Biochim. Biophys. Acta , vol.806 , pp. 16-24
    • Demeter, S.1    Vass, I.2    Hideg, É.3    Sallai, A.4
  • 56
    • 38049011376 scopus 로고    scopus 로고
    • 4Ca cluster and to the evolution of molecular oxygen in Photosystem II
    • 4Ca cluster and to the evolution of molecular oxygen in Photosystem II Coord. Chem. Rev. 252 2008 259 272
    • (2008) Coord. Chem. Rev. , vol.252 , pp. 259-272
    • Rappaport, F.1    Diner, B.A.2
  • 58
    • 78249233837 scopus 로고    scopus 로고
    • Probing the quinone binding site of photosystem II from Thermosynechococcus elongatus containing either PsbA1 or PsbA3 as the D1 protein through the binding characteristics of herbicides
    • A. Boussac, M. Sugiura, and F. Rappaport Probing the quinone binding site of photosystem II from Thermosynechococcus elongatus containing either PsbA1 or PsbA3 as the D1 protein through the binding characteristics of herbicides Biochim. Biophys. Acta 1807 2011 119 129
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 119-129
    • Boussac, A.1    Sugiura, M.2    Rappaport, F.3
  • 59
    • 63549106377 scopus 로고    scopus 로고
    • Janus-faced charge recombinations in photosystem II photoinhibition
    • I. Vass, and K. Cser Janus-faced charge recombinations in photosystem II photoinhibition Trends Plant Sci. 14 2009 200 205
    • (2009) Trends Plant Sci. , vol.14 , pp. 200-205
    • Vass, I.1    Cser, K.2
  • 60
    • 57849150806 scopus 로고    scopus 로고
    • Singlet oxygen production in photosystem II and related protection mechanism
    • A. Krieger-Liszkay, C. Fufezan, and A. Trebst Singlet oxygen production in photosystem II and related protection mechanism Photosynth. Res. 98 2008 551 564
    • (2008) Photosynth. Res. , vol.98 , pp. 551-564
    • Krieger-Liszkay, A.1    Fufezan, C.2    Trebst, A.3
  • 62
    • 8144219978 scopus 로고    scopus 로고
    • Modification of the pheophytin midpoint potential in Photosystem II: Modulation of the quantum yield of charge separation and of charge recombination pathways
    • A. Cuni, L. Xiong, R.T. Sayre, F. Rappaport, and J. Lavergne Modification of the pheophytin midpoint potential in Photosystem II: modulation of the quantum yield of charge separation and of charge recombination pathways Phys. Chem. Chem. Phys. 6 2004 4825 4831
    • (2004) Phys. Chem. Chem. Phys. , vol.6 , pp. 4825-4831
    • Cuni, A.1    Xiong, L.2    Sayre, R.T.3    Rappaport, F.4    Lavergne, J.5
  • 63
    • 49049151877 scopus 로고
    • Electron-dependent competition between plastoquinone and inhibitors for binding to photosystem II
    • B.R. Velthuys Electron-dependent competition between plastoquinone and inhibitors for binding to photosystem II FEBS Lett. 126 1981 277 281
    • (1981) FEBS Lett. , vol.126 , pp. 277-281
    • Velthuys, B.R.1
  • 64
    • 0020355705 scopus 로고
    • Mode of action of 3-(3, 4-dichlorophenyl)-1,1-dimethylurea: Evidence that the inhibitor competes with plastoquinone for binding to a common site on the acceptor side of Photosystem-II
    • J. Lavergne Mode of action of 3-(3, 4-dichlorophenyl)-1,1-dimethylurea: evidence that the inhibitor competes with plastoquinone for binding to a common site on the acceptor side of Photosystem-II Biochim. Biophys. Acta 682 1982 345 353
    • (1982) Biochim. Biophys. Acta , vol.682 , pp. 345-353
    • Lavergne, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.