메뉴 건너뛰기




Volumn 1757, Issue 11, 2006, Pages 1547-1556

Interaction of N,N,N′,N′-tetramethyl-p-phenylenediamine with photosystem II as revealed by thermoluminescence: Reduction of the higher oxidation states of the Mn cluster and displacement of plastoquinone from the QB niche

Author keywords

Charge recombination; Manganese cluster; Photosystem; Plastoquinone; Thermoluminescence; Thylakoid membrane

Indexed keywords

CARBONYL CYANIDE CHLOROPHENYLHYDRAZONE; DIURON; MANGANESE; N,N,N',N' TETRAMETHYL 4 PHENYLENEDIAMINE; PHENYLENEDIAMINE DERIVATIVE; PLASTOQUINONE; UNCLASSIFIED DRUG;

EID: 33750506937     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2006.09.005     Document Type: Article
Times cited : (14)

References (50)
  • 1
    • 45749150851 scopus 로고    scopus 로고
    • Photosystem II: the light-driven water-plastoquinone-oxidoreductase
    • Wydrzynski T., and Satoh K. (Eds), Springer-Verlag
    • Wydrzynski T., and Satoh K. Photosystem II: the light-driven water-plastoquinone-oxidoreductase. In: Wydrzynski T., and Satoh K. (Eds). Advances in Photosynthesis and Respiration (2006), Springer-Verlag
    • (2006) Advances in Photosynthesis and Respiration
    • Wydrzynski, T.1    Satoh, K.2
  • 2
    • 0033679186 scopus 로고    scopus 로고
    • Primary charge separation in photosystem II
    • Dekker J.P., and van Grondelle R. Primary charge separation in photosystem II. Photosyn. Res. 63 (2000) 195-208
    • (2000) Photosyn. Res. , vol.63 , pp. 195-208
    • Dekker, J.P.1    van Grondelle, R.2
  • 3
    • 0001577142 scopus 로고    scopus 로고
    • Structure, dynamics, and energy conversion efficiency in photosystem II
    • Ort D.R., and Yocum C.F. (Eds), Kluwer Academic Publishers, Dordrecht
    • Diner B.A., and Babcock G.T. Structure, dynamics, and energy conversion efficiency in photosystem II. In: Ort D.R., and Yocum C.F. (Eds). Oxygenic Photosynthesis: The Light Reactions (1996), Kluwer Academic Publishers, Dordrecht 213-247
    • (1996) Oxygenic Photosynthesis: The Light Reactions , pp. 213-247
    • Diner, B.A.1    Babcock, G.T.2
  • 4
    • 0019320156 scopus 로고
    • Binary oscillations in the rate of re-oxidation of the primary acceptor of photosystem II
    • Bowes J., and Crofts A.R. Binary oscillations in the rate of re-oxidation of the primary acceptor of photosystem II. Biochim. Biophys. Acta 590 (1980) 373-384
    • (1980) Biochim. Biophys. Acta , vol.590 , pp. 373-384
    • Bowes, J.1    Crofts, A.R.2
  • 5
    • 30744445692 scopus 로고    scopus 로고
    • Towards complete cofactor arrangement in the 3.0 angstrom resolution structure of photosystem II
    • Loll B., Kern J., Saenger W., Zouni A., and Biesiadka J. Towards complete cofactor arrangement in the 3.0 angstrom 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
  • 8
    • 0035808704 scopus 로고    scopus 로고
    • Photosynthetic water oxidation to molecular oxygen: apparatus and mechanism
    • Renger G. Photosynthetic water oxidation to molecular oxygen: apparatus and mechanism. Biochim. Biophys. Acta 1503 (2001) 210-228
    • (2001) Biochim. Biophys. Acta , vol.1503 , pp. 210-228
    • Renger, G.1
  • 9
    • 33847453635 scopus 로고
    • Kinetics of manganese redox transitions in the oxygen-evolving apparatus of photosynthesis
    • Dekker J.P., Plijter J.J., Ouwehand L., and van Gorkom H.J. Kinetics of manganese redox transitions in the oxygen-evolving apparatus of photosynthesis. Biochim. Biophys. Acta 767 (1984) 176-179
    • (1984) Biochim. Biophys. Acta , vol.767 , pp. 176-179
    • Dekker, J.P.1    Plijter, J.J.2    Ouwehand, L.3    van Gorkom, H.J.4
  • 10
    • 0015212656 scopus 로고
    • Action de faibles concentrations d'hydroxylamine sur l'emission d'oxygene des algues Chlorella et des chloroplastes d'epinards
    • Bouges B. Action de faibles concentrations d'hydroxylamine sur l'emission d'oxygene des algues Chlorella et des chloroplastes d'epinards. Biochim. Biophys. Acta 234 (1971) 102-112
    • (1971) Biochim. Biophys. Acta , vol.234 , pp. 102-112
    • Bouges, B.1
  • 11
    • 0025598137 scopus 로고
    • The reactivity of hydrazine with photosystem-II strongly depends on the redox state of the water oxidizing system
    • Messinger J., and Renger G. The reactivity of hydrazine with photosystem-II strongly depends on the redox state of the water oxidizing system. FEBS Lett. 277 (1990) 141-146
    • (1990) FEBS Lett. , vol.277 , pp. 141-146
    • Messinger, J.1    Renger, G.2
  • 12
    • 0025946303 scopus 로고
    • 2-induced modifications of flash-induced oxygen evolution in isolated spinach thylakoids
    • 2-induced modifications of flash-induced oxygen evolution in isolated spinach thylakoids. Biochemistry 30 (1991) 7852-7862
    • (1991) Biochemistry , vol.30 , pp. 7852-7862
    • Messinger, J.1    Wacker, U.2    Renger, G.3
  • 13
    • 0027384113 scopus 로고
    • - 2 of the water oxidase in isolated spinach thylakoids
    • - 2 of the water oxidase in isolated spinach thylakoids. Biochemistry 32 (1993) 9379-9386
    • (1993) Biochemistry , vol.32 , pp. 9379-9386
    • Messinger, J.1    Renger, G.2
  • 14
    • 0037544020 scopus 로고    scopus 로고
    • Effect of hydroxylamine on photosystem II: reinvestigation of electron paramagnetic resonance characteristics reveals possible S state intermediates
    • Nugent J.H.A., Muhiuddin I.P., and Evans M.C.W. Effect of hydroxylamine on photosystem II: reinvestigation of electron paramagnetic resonance characteristics reveals possible S state intermediates. Biochemistry 42 (2003) 5500-5507
    • (2003) Biochemistry , vol.42 , pp. 5500-5507
    • Nugent, J.H.A.1    Muhiuddin, I.P.2    Evans, M.C.W.3
  • 15
    • 0038740869 scopus 로고    scopus 로고
    • Interaction of exogenous quinones with membranes of higher plant chloroplasts: modulation of quinone capacities as photochemical and non-photochemical quenchers of energy in photosystem II during light-dark transitions
    • Bukhov N.G., Sridharan G., Egorova E.A., and Carpentier R. Interaction of exogenous quinones with membranes of higher plant chloroplasts: modulation of quinone capacities as photochemical and non-photochemical quenchers of energy in photosystem II during light-dark transitions. Biochim. Biophys. Acta 1604 (2003) 115-123
    • (2003) Biochim. Biophys. Acta , vol.1604 , pp. 115-123
    • Bukhov, N.G.1    Sridharan, G.2    Egorova, E.A.3    Carpentier, R.4
  • 16
    • 3242658192 scopus 로고    scopus 로고
    • Changes in polyphasic chlorophyll a fluorescence induction curve upon inhibition of donor or acceptor side of photosystem II in isolated thylakoids
    • Bukhov N.G., Egorova E.A., Govindachary S., and Carpentier R. Changes in polyphasic chlorophyll a fluorescence induction curve upon inhibition of donor or acceptor side of photosystem II in isolated thylakoids. Biochim. Biophys. Acta 1657 (2004) 121-130
    • (2004) Biochim. Biophys. Acta , vol.1657 , pp. 121-130
    • Bukhov, N.G.1    Egorova, E.A.2    Govindachary, S.3    Carpentier, R.4
  • 17
    • 0344196922 scopus 로고    scopus 로고
    • N,N,N′,N′-tetramethyl-p-phenylenediamine initiates the appearance of a well-resolved I peak in the kinetics of chlorophyll fluorescence rise in isolated thylakoids
    • Bukhov N.G., Govindachary S., Egorova E.A., Joly D., and Carpentier R. N,N,N′,N′-tetramethyl-p-phenylenediamine initiates the appearance of a well-resolved I peak in the kinetics of chlorophyll fluorescence rise in isolated thylakoids. Biochim. Biophys. Acta 1607 (2003) 91-96
    • (2003) Biochim. Biophys. Acta , vol.1607 , pp. 91-96
    • Bukhov, N.G.1    Govindachary, S.2    Egorova, E.A.3    Joly, D.4    Carpentier, R.5
  • 18
    • 23444436210 scopus 로고    scopus 로고
    • Kinetic analyses of the OJIP chlorophyll fluorescence rise in thylakoid membranes
    • Joly D., Bigras C., Harnois J., Govindachary S., and Carpentier R. Kinetic analyses of the OJIP chlorophyll fluorescence rise in thylakoid membranes. Photosyn. Res. 84 (2005) 107-112
    • (2005) Photosyn. Res. , vol.84 , pp. 107-112
    • Joly, D.1    Bigras, C.2    Harnois, J.3    Govindachary, S.4    Carpentier, R.5
  • 19
    • 8144221719 scopus 로고    scopus 로고
    • Probing reactive sites within the photosystem II manganese cluster: evidence for separate populations of manganese that differ in redox potential
    • Kuntzleman T., McCarrick M., Penner-Hahn J., and Yocum C. Probing reactive sites within the photosystem II manganese cluster: evidence for separate populations of manganese that differ in redox potential. Phys. Chem. Chem. Phys. 6 (2004) 4897-4904
    • (2004) Phys. Chem. Chem. Phys. , vol.6 , pp. 4897-4904
    • Kuntzleman, T.1    McCarrick, M.2    Penner-Hahn, J.3    Yocum, C.4
  • 20
    • 0242459668 scopus 로고    scopus 로고
    • Chlorophyll thermoluminescence of leaf discs: simple instruments and progress in signal interpretation open the way to new ecophysiological indicators
    • Ducruet J.M. Chlorophyll thermoluminescence of leaf discs: simple instruments and progress in signal interpretation open the way to new ecophysiological indicators. J. Exp. Bot. 54 (2003) 2419-2430
    • (2003) J. Exp. Bot. , vol.54 , pp. 2419-2430
    • Ducruet, J.M.1
  • 21
    • 0002136083 scopus 로고    scopus 로고
    • Photosynthetics thermoluminescence as a simple probe of photosystem II electron transport
    • Amesz J., and Hoff A.J. (Eds), Kluwer Academic, Dordrecht
    • Inoue Y. Photosynthetics thermoluminescence as a simple probe of photosystem II electron transport. In: Amesz J., and Hoff A.J. (Eds). Biophysical Techniques in Photosynthesis (1996), Kluwer Academic, Dordrecht 93-107
    • (1996) Biophysical Techniques in Photosynthesis , pp. 93-107
    • Inoue, Y.1
  • 22
    • 4544220381 scopus 로고    scopus 로고
    • Thermoluminescence: a technique for probing photosystem II
    • Carpentier R. (Ed), Humana Press, Totova, NJ, USA
    • Sane P.V. Thermoluminescence: a technique for probing photosystem II. In: Carpentier R. (Ed). Photosynthesis Research Protocols (2004), Humana Press, Totova, NJ, USA 229-248
    • (2004) Photosynthesis Research Protocols , pp. 229-248
    • Sane, P.V.1
  • 23
    • 0029998586 scopus 로고    scopus 로고
    • Thermoluminescence from the photosynthetic apparatus
    • Vass I., and Govindjee. Thermoluminescence from the photosynthetic apparatus. Photosyn. Res. 48 (1996) 117-126
    • (1996) Photosyn. Res. , vol.48 , pp. 117-126
    • Vass, I.1    Govindjee2
  • 24
    • 0028180062 scopus 로고
    • The Origin of 40-50 °C thermoluminescence bands in photosystem II
    • Johnson G.N., Boussac A., and Rutherford A.W. The Origin of 40-50 °C thermoluminescence bands in photosystem II. Biochim. Biophys. Acta 1184 (1994) 85-92
    • (1994) Biochim. Biophys. Acta , vol.1184 , pp. 85-92
    • Johnson, G.N.1    Boussac, A.2    Rutherford, A.W.3
  • 25
    • 0025130137 scopus 로고
    • Heat-Stress stimulation of electron flow in a photosystem-I submembrane fraction
    • Boucher N., Harnois J., and Carpentier R. Heat-Stress stimulation of electron flow in a photosystem-I submembrane fraction. Biochem. Cell Biol. Biochim. Biol. Cell. 68 (1990) 999-1004
    • (1990) Biochem. Cell Biol. Biochim. Biol. Cell. , vol.68 , pp. 999-1004
    • Boucher, N.1    Harnois, J.2    Carpentier, R.3
  • 26
    • 26044440113 scopus 로고
    • Determination of accurate extinction coefficients and simultaneous-equations for assaying chlorophyll-a and chlorophyll-b extracted with 4 different solvents. Verification of the concentration of chlorophyll standards by atomic absorption spectroscopy
    • Porra R.J., Thompson W.A., and Kriedemann P.E. Determination of accurate extinction coefficients and simultaneous-equations for assaying chlorophyll-a and chlorophyll-b extracted with 4 different solvents. Verification of the concentration of chlorophyll standards by atomic absorption spectroscopy. Biochim. Biophys. Acta 975 (1989) 384-394
    • (1989) Biochim. Biophys. Acta , vol.975 , pp. 384-394
    • Porra, R.J.1    Thompson, W.A.2    Kriedemann, P.E.3
  • 29
    • 0016175830 scopus 로고
    • Simple explanation of the misses in the cooperation of charges in photosynthetic oxygen evolution
    • Delrieau M.J. Simple explanation of the misses in the cooperation of charges in photosynthetic oxygen evolution. Photochem. Photobiol. 20 (1974) 441-454
    • (1974) Photochem. Photobiol. , vol.20 , pp. 441-454
    • Delrieau, M.J.1
  • 30
    • 0001488895 scopus 로고
    • Thermoluminescence as a probe of photosystem II photochemistry
    • Rutherford A.W., Crofts A.R., and Inoue Y. Thermoluminescence as a probe of photosystem II photochemistry. Biochim. Biophys. Acta 682 (1982) 457-465
    • (1982) Biochim. Biophys. Acta , vol.682 , pp. 457-465
    • Rutherford, A.W.1    Crofts, A.R.2    Inoue, Y.3
  • 33
    • 0015526673 scopus 로고
    • The action of 2-anilinothiophenes as accelerators of the deactivation reactions in the watersplitting enzyme system of photosynthesis
    • Renger G. The action of 2-anilinothiophenes as accelerators of the deactivation reactions in the watersplitting enzyme system of photosynthesis. Biochim. Biophys. Acta 256 (1972) 428-439
    • (1972) Biochim. Biophys. Acta , vol.256 , pp. 428-439
    • Renger, G.1
  • 36
    • 0038650623 scopus 로고    scopus 로고
    • Oxygen evolution in photosynthesis: simple analytical solution for the Kok model
    • Shinkarev V.P. Oxygen evolution in photosynthesis: simple analytical solution for the Kok model. Biophys. J. 85 (2003) 435-441
    • (2003) Biophys. J. , vol.85 , pp. 435-441
    • Shinkarev, V.P.1
  • 37
    • 0023657038 scopus 로고
    • Reactions of hydroxylamine with the electron-donor side of photosystem II
    • Beck W.F., and Brudvig G.W. Reactions of hydroxylamine with the electron-donor side of photosystem II. Biochemistry 26 (1987) 8285-8295
    • (1987) Biochemistry , vol.26 , pp. 8285-8295
    • Beck, W.F.1    Brudvig, G.W.2
  • 38
    • 15844409181 scopus 로고    scopus 로고
    • Reduced derivatives of the Mn cluster in the oxygen-evolving complex of photosystem II: an EXAFS study
    • Riggs-Gelasco P.J., Mei R., Yocum C.F., and Penner-Hahn J. Reduced derivatives of the Mn cluster in the oxygen-evolving complex of photosystem II: an EXAFS study. J. Am. Chem. Soc. 118 (1996) 2387-2399
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 2387-2399
    • Riggs-Gelasco, P.J.1    Mei, R.2    Yocum, C.F.3    Penner-Hahn, J.4
  • 39
    • 0342521085 scopus 로고
    • Oxidation-reduction and ligand-substitution reactions of the oxygen-evolving center of PSII
    • Pecoraro V.L. (Ed), VCH Publishers, New York
    • Brudvig G.W., and Beck W.F. Oxidation-reduction and ligand-substitution reactions of the oxygen-evolving center of PSII. In: Pecoraro V.L. (Ed). Manganese Redox Enzymes (1992), VCH Publishers, New York 119-140
    • (1992) Manganese Redox Enzymes , pp. 119-140
    • Brudvig, G.W.1    Beck, W.F.2
  • 40
    • 0033503712 scopus 로고    scopus 로고
    • 0 fluorescence and a shift in the electronic equilibrium at the acceptor side of photosystem 2
    • 0 fluorescence and a shift in the electronic equilibrium at the acceptor side of photosystem 2. Photosynthetica 37 (1999) 335-338
    • (1999) Photosynthetica , vol.37 , pp. 335-338
    • Ducruet, J.M.1
  • 41
    • 0039990009 scopus 로고
    • Depletion of photosystem II extrinsic proteins. II. Analysis of the PSII/water-oxidizing complex by measurements of N,N,N′,N′-tetramethyl-p-phenylenediamine oxidation following an actinic flash
    • Tamura N., Radmer R., Lantz S., Cammarata K., and Cheniae G. Depletion of photosystem II extrinsic proteins. II. Analysis of the PSII/water-oxidizing complex by measurements of N,N,N′,N′-tetramethyl-p-phenylenediamine oxidation following an actinic flash. Biochim. Biophys. Acta 850 (1986) 369-379
    • (1986) Biochim. Biophys. Acta , vol.850 , pp. 369-379
    • Tamura, N.1    Radmer, R.2    Lantz, S.3    Cammarata, K.4    Cheniae, G.5
  • 43
    • 2642606979 scopus 로고    scopus 로고
    • Biophysical, biochemical, and physiological characterization of Chlamydomonas reinhardtii mutants with amino acid substitutions at the Ala (251) residue in the D1 protein that result in varying levels of photosynthetic competence
    • Lardans A., Forster B., Prasil O., Falkowski P.G., Sobolev V., Edelman M., Osmond C.B., Gillham N.W., and Boynton J.E. Biophysical, biochemical, and physiological characterization of Chlamydomonas reinhardtii mutants with amino acid substitutions at the Ala (251) residue in the D1 protein that result in varying levels of photosynthetic competence. J. Biol. Chem. 273 (1998) 11082-11091
    • (1998) J. Biol. Chem. , vol.273 , pp. 11082-11091
    • Lardans, A.1    Forster, B.2    Prasil, O.3    Falkowski, P.G.4    Sobolev, V.5    Edelman, M.6    Osmond, C.B.7    Gillham, N.W.8    Boynton, J.E.9
  • 44
    • 0033547703 scopus 로고    scopus 로고
    • B in photosystem II is thermodynamically perturbed in phototolerant mutants of Synechocystis sp. PCC 6803
    • B in photosystem II is thermodynamically perturbed in phototolerant mutants of Synechocystis sp. PCC 6803. Biochemistry 38 (1999) 770-775
    • (1999) Biochemistry , vol.38 , pp. 770-775
    • Minagawa, J.1    Narusaka, Y.2    Inoue, Y.3    Satoh, K.4
  • 45
    • 0034610352 scopus 로고    scopus 로고
    • Mutations in the CD-loop region of the D2 protein in Synechocystis sp PCC 6803 modify charge recombination pathways in photosystem II in vivo
    • Vavilin D.V., and Vermaas W.F.J. Mutations in the CD-loop region of the D2 protein in Synechocystis sp PCC 6803 modify charge recombination pathways in photosystem II in vivo. Biochemistry 39 (2000) 14831-14838
    • (2000) Biochemistry , vol.39 , pp. 14831-14838
    • Vavilin, D.V.1    Vermaas, W.F.J.2
  • 46
    • 8344285837 scopus 로고    scopus 로고
    • Charge stabilization and recombination in Photosystem II containing the D1′ protein product of the psbA1 gene in Synechocystis 6803
    • Sicora C., Wiklund R., Jansson C., and Vass I. Charge stabilization and recombination in Photosystem II containing the D1′ protein product of the psbA1 gene in Synechocystis 6803. Phys. Chem. Chem. Phys. 6 (2004) 4832-4837
    • (2004) Phys. Chem. Chem. Phys. , vol.6 , pp. 4832-4837
    • Sicora, C.1    Wiklund, R.2    Jansson, C.3    Vass, I.4
  • 47
    • 0032008002 scopus 로고    scopus 로고
    • - recombination by delayed thermoluminescence reveal heterogeneity in photosystem II energetics
    • - recombination by delayed thermoluminescence reveal heterogeneity in photosystem II energetics. Phytochemistry 47 (1998) 641-649
    • (1998) Phytochemistry , vol.47 , pp. 641-649
    • Townsend, J.S.1    Kanazawa, A.2    Kramer, D.M.3
  • 48
    • 17144386774 scopus 로고    scopus 로고
    • Charge recombination and thermoluminescence in photosystem II
    • Rappaport F., Cuni A., Xiong L., Sayre R., and Lavergne R.M. 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, R.M.5
  • 49
    • 0035967507 scopus 로고    scopus 로고
    • β-Carotene redox reactions in photosystem II: electron transfer pathway
    • Faller P., Pascal A., and Rutherford A.W. β-Carotene redox reactions in photosystem II: electron transfer pathway. Biochemistry 40 (2001) 6431-6440
    • (2001) Biochemistry , vol.40 , pp. 6431-6440
    • Faller, P.1    Pascal, A.2    Rutherford, A.W.3
  • 50
    • 0030899689 scopus 로고    scopus 로고
    • Evidence for the involvement of cyclic electron transport in the protection of photosystem II against photoinhibition: influence of a new phenolic compound
    • Allakhverdiev S.I., Klimov V.V., and Carpentier R. Evidence for the involvement of cyclic electron transport in the protection of photosystem II against photoinhibition: influence of a new phenolic compound. Biochemistry 36 (1997) 4149-4154
    • (1997) Biochemistry , vol.36 , pp. 4149-4154
    • Allakhverdiev, S.I.1    Klimov, V.V.2    Carpentier, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.