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Volumn 48, Issue 40, 2009, Pages 9393-9404

The S0 state of the water oxidizing complex in photosystem II: pH dependence of the EPR split signal induction and mechanistic implications

Author keywords

[No Author keywords available]

Indexed keywords

ACIDIC PH; ALKALINE PH; EPR SIGNALS; EXTREME TEMPERATURES; HYDROGEN BOND PATTERNS; MAGNETIC INTERACTIONS; NEUTRAL RADICAL; PH DEPENDENCE; PH INDEPENDENT; PH RANGE; PHOTOSYSTEM II; RADICAL SPECIES; REDOX-ACTIVE TYROSINES; ROOM TEMPERATURE; SIGNAL DECAY; SIGNAL INDUCTION; SIGNAL INTENSITIES; STABLE RADICALS; WATER OXIDATION;

EID: 70350140360     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi901177w     Document Type: Article
Times cited : (11)

References (62)
  • 1
    • 0037295369 scopus 로고    scopus 로고
    • Photosystem II: The engine of life
    • Barber, J. (2003) Photosystem II: The engine of life. Q. Rev. Biophys. 36, 71-89.
    • (2003) Q. Rev. Biophys. , vol.36 , pp. 71-89
    • Barber, J.1
  • 2
    • 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
    • Dau, H., and Haumann, M. (2007) Eight steps preceding O-O bond formation in oxygenic photosynthesis - A basic reaction cycle of the photosystem II manganese complex. Biochim. Biophys. Acta 1767, 472-483.
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 472-483
    • Dau, H.1    Haumann, M.2
  • 3
    • 33751424725 scopus 로고    scopus 로고
    • Water-splitting chemistry of photosystem II
    • McEvoy, J. P., and Brudvig, G. W. (2006) Water-splitting chemistry of photosystem II. Chem. Rev. 106, 4455-4483.
    • (2006) Chem. Rev. , vol.106 , pp. 4455-4483
    • McEvoy, J.P.1    Brudvig, G.W.2
  • 4
    • 0030832914 scopus 로고    scopus 로고
    • Structural coupling between the oxygen-evolving Mn cluster and a tyrosine residue in photosystem II as revealed by fourier transform infrared spectroscopy
    • DOI 10.1021/bi971760y
    • Noguchi, T., Inoue, Y., and Tang, X. S. (1997) Structural coupling between the oxygen-evolving Mn cluster and a tyrosine residue in photosystem II as revealed by Fourier transform infrared spectroscopy. Biochemistry 36, 14705-14711. (Pubitemid 27524391)
    • (1997) Biochemistry , vol.36 , Issue.48 , pp. 14705-14711
    • Noguchi, T.1    Inoue, Y.2    Tang, X.-S.3
  • 5
    • 0032575361 scopus 로고    scopus 로고
    • Hydrogen bonding of redox-active tyrosine Z of photosystem II probed by FTIR difference spectroscopy
    • DOI 10.1021/bi980788m
    • Berthomieu, C., Hienerwadel, R., Boussac, A., Breton, J., and Diner, B. A. (1998) Hydrogen bonding of redox-active tyrosine Z of photosystem II probed by FTIR difference spectroscopy. Biochemistry 37, 10547-10554. (Pubitemid 28357854)
    • (1998) Biochemistry , vol.37 , Issue.30 , pp. 10547-10554
    • Berthomieu, C.1    Hienerwadel, R.2    Boussac, A.3    Breton, J.4    Diner, B.A.5
  • 8
    • 0032485936 scopus 로고    scopus 로고
    • +• reduction in photosystem II with an intact water oxidising complex
    • +• reduction in photosystem II with an intact water oxidising complex. FEBS Lett. 429, 49-52.
    • (1998) FEBS Lett , vol.429 , pp. 49-52
    • Christen, G.1    Reifarth, F.2    Renger, G.3
  • 10
    • 0028344645 scopus 로고
    • Kinetics of electron transfer and electrochromic change during the redox transitions of the photosynthetic oxygen-evolving complex
    • Rappaport, F., Blanchard-Desce, M., and Lavergne, J. (1994) Kinetics of electron transfer and electrochromic change during the redox transitions of the photosynthetic oxygen-evolving complex. Biochim. Biophys. Acta 1184, 178-192.
    • (1994) Biochim. Biophys. Acta , vol.1184 , pp. 178-192
    • Rappaport, F.1    Blanchard-Desce, M.2    Lavergne, J.3
  • 11
    • 0032491189 scopus 로고    scopus 로고
    • Involvement of histidine 190 on the D1 protein in electron/proton transfer reactions on the donor side of photosystem II
    • DOI 10.1021/bi980194j
    • Mamedov, F., Sayre, R. T., and Styring, S. (1998) Involvement of histidine 190 on the D1 protein in electron/proton transfer reactions on the donor side of photosystem II. Biochemistry 37, 14245-14256. (Pubitemid 28471261)
    • (1998) Biochemistry , vol.37 , Issue.40 , pp. 14245-14256
    • Mamedov, F.1    Sayre, R.T.2    Styring, S.3
  • 12
    • 0032508393 scopus 로고    scopus 로고
    • Role of D1-His190 in proton-coupled electron transfer reactions in photosystem II: A chemical complementation study
    • Hays, A. M. A., Vassiliev, I. R., Golbeck, J. H., and Debus, R. J. (1998) Role of D1-His190 in proton-coupled electron transfer reactions in photosystem II: A chemical complementation study. Biochemistry 37, 11352-11365.
    • (1998) Biochemistry , vol.37 , pp. 11352-11365
    • Hays, A.M.A.1    Vassiliev, I.R.2    Golbeck, J.H.3    Debus, R.J.4
  • 14
    • 0030854151 scopus 로고    scopus 로고
    • A metalloradical mechanism for the generation of oxygen from water in photosynthesis
    • DOI 10.1126/science.277.5334.1953
    • Hoganson, C. W., and Babcock, G. T. (1997) A metalloradical mechanism for the generation of oxygen from water in photosynthesis. Science 277, 1953-1956. (Pubitemid 27449129)
    • (1997) Science , vol.277 , Issue.5334 , pp. 1953-1956
    • Hoganson, C.W.1    Babcock, G.T.2
  • 15
    • 0033545726 scopus 로고    scopus 로고
    • +• reduction kinetics and redox transition probability of the water oxidizing complex as a function of pH and H/D isotope exchange in spinach thylakoids
    • Christen, G., Seeliger, A., and Renger, G. (1999) P680+• reduction kinetics and redox transition probability of the water oxidizing complex as a function of pH and H/D isotope exchange in spinach thylakoids. Biochemistry 38, 6082-6092. (Pubitemid 129514899)
    • (1999) Biochemistry , vol.38 , Issue.19 , pp. 6082-6092
    • Christen, G.1    Seeliger, A.2    Renger, G.3
  • 16
    • 0000385466 scopus 로고
    • i of the water oxidizing system
    • i 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
  • 17
    • 0032570284 scopus 로고    scopus 로고
    • Function of tyrosine Z in water oxidation by photosystem II: Electrostatical promotor instead of hydrogen abstractor
    • DOI 10.1021/bi9719152
    • Ahlbrink, R., Haumann, M., Cherepanov, D., Bogershausen, O., Mulkidjanian, A., and Junge, W. (1998) Function of tyrosine Z in water oxidation by photosystem II: Electrostatical promotor instead of hydrogen abstractor. Biochemistry 37, 1131-1142. (Pubitemid 28100616)
    • (1998) Biochemistry , vol.37 , Issue.4 , pp. 1131-1142
    • Ahlbrink, R.1    Haumann, M.2    Cherepanov, D.3    Bogershausen, O.4    Mulkidjanian, A.5    Junge, W.6
  • 19
    • 0001404648 scopus 로고
    • Deactivation kinetics and temperature-dependence of the S-state transitions in the oxygen-evolving system of photosystem II measured by EPR spectroscopy
    • Styring, S., and Rutherford, A. W. (1988) Deactivation kinetics and temperature-dependence of the S-state transitions in the oxygen-evolving system of photosystem II measured by EPR spectroscopy. Biochim. Biophys. Acta 933, 378-387.
    • (1988) Biochim. Biophys. Acta , vol.933 , pp. 378-387
    • Styring, S.1    Rutherford, A.W.2
  • 21
    • 0038385474 scopus 로고    scopus 로고
    • 1 states of the oxygen-evolving complex
    • 1 states of the oxygen-evolving complex. Biochemistry 42, 8066-8076.
    • (2003) Biochemistry , vol.42 , pp. 8066-8076
    • Zhang, C.1    Styring, S.2
  • 22
    • 7244240549 scopus 로고    scopus 로고
    • Low-temperature electron transfer in photosystem II: A tyrosyl radical and semiquinone charge pair
    • DOI 10.1021/bi048631j
    • Zhang, C., Boussac, A., and Rutherford, A. W. (2004) Low-temperature electron transfer in photosystem II: A tyrosyl radical and semiquinone charge pair. Biochemistry 43, 13787-13795. (Pubitemid 39431062)
    • (2004) Biochemistry , vol.43 , Issue.43 , pp. 13787-13795
    • Zhang, C.1    Boussac, A.2    Rutherford, A.W.3
  • 24
    • 1642331709 scopus 로고    scopus 로고
    • Architecture of the photosynthetic oxygen-evolving center
    • Ferreira, K. N., Iverson, T. M., Maghlaoui, K., Barber, J., and Iwata, S. (2004) Architecture of the photosynthetic oxygen-evolving center. Science 303, 1831-1838.
    • (2004) Science , vol.303 , pp. 1831-1838
    • Ferreira, K.N.1    Iverson, T.M.2    Maghlaoui, K.3    Barber, J.4    Iwata, S.5
  • 25
    • 30744445692 scopus 로고    scopus 로고
    • Towards complete cofactor arrangement in the 3.0 Å resolution structure of photosystem II
    • DOI 10.1038/nature04224, PII NATURE04224
    • Loll, B., Kern, J., Saenger, W., Zouni, A., and Biesiadka, J. (2005) Towards complete cofactor arrangement in the 3.0 Å resolution structure of photosystem II. Nature 438, 1040-1044. (Pubitemid 43093979)
    • (2005) Nature , vol.438 , Issue.7070 , pp. 1040-1044
    • Loll, B.1    Kern, J.2    Saenger, W.3    Zouni, A.4    Biesiadka, J.5
  • 26
    • 0026707522 scopus 로고
    • The manganese and calcium ions of photosynthetic oxygen evolution
    • Debus, R. J. (1992) The manganese and calcium ions of photosynthetic oxygen evolution. Biochim. Biophys. Acta 1102, 269-352.
    • (1992) Biochim. Biophys. Acta , vol.1102 , pp. 269-352
    • Debus, R.J.1
  • 27
    • 18244404033 scopus 로고    scopus 로고
    • Trapping of metalloradical intermediates of the S-states at liquid helium temperatures. Overview of the phenomenology and mechanistic implications
    • Petrouleas, V., Koulougliotis, D., and Ioannidis, N. (2005) Trapping of metalloradical intermediates of the S-states at liquid helium temperatures. Overview of the phenomenology and mechanistic implications. Biochemistry 44, 6723-6728.
    • (2005) Biochemistry , vol.44 , pp. 6723-6728
    • Petrouleas, V.1    Koulougliotis, D.2    Ioannidis, N.3
  • 29
    • 34347386893 scopus 로고    scopus 로고
    • D in photosystem II probed by illumination at 5 K
    • D in photosystem II probed by illumination at 5 K. Biochemistry 46, 7865-7874.
    • (2007) Biochemistry , vol.46 , pp. 7865-7874
    • Havelius, K.G.1    Styring, S.2
  • 30
    • 33746555334 scopus 로고    scopus 로고
    • Z and substrate water in active photosystem II
    • Z and substrate water in active photosystem II. Biochim. Biophys. Acta 1757, 781-786.
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 781-786
    • Zhang, C.1
  • 31
    • 0037035522 scopus 로고    scopus 로고
    • PH dependence of the four individual transitions in the catalytic S-cycle during photosynthetic oxygen evolution
    • DOI 10.1021/bi011691u
    • Bernat, G., Morvaridi, F., Feyziyev, Y., and Styring, S. (2002) pH dependence of the four individual transitions in the catalytic S-cycle during photosynthetic oxygen evolution. Biochemistry 41, 5830-5843. (Pubitemid 34462704)
    • (2002) Biochemistry , vol.41 , Issue.18 , pp. 5830-5843
    • Bernat, G.1    Morvaridi, F.2    Feyziyev, Y.3    Styring, S.4
  • 32
    • 13444301152 scopus 로고    scopus 로고
    • PH dependence of the flash-induced S-state transitions in the oxygen-evolving center of photosystem II from Thermosynechoccocus elongatus as revealed by fourier transform infrared spectroscopy
    • DOI 10.1021/bi0483312
    • Suzuki, H., Sugiura, M., and Noguchi, T. (2005) pH dependence of the flash-induced S-state transitions in the oxygen-evolving center of photosystem II from Thermosynechoccocus elongatus as revealed by Fourier transform infrared spectroscopy. Biochemistry 44, 1708-1718. (Pubitemid 40204412)
    • (2005) Biochemistry , vol.44 , Issue.5 , pp. 1708-1718
    • Suzuki, H.1    Sugiura, M.2    Noguchi, T.3
  • 33
    • 0039596979 scopus 로고    scopus 로고
    • 2 state g ∼ 2 electron paramagnetic resonance signals
    • 2 state g ∼ 2 electron paramagnetic resonance signals. Biochemistry 39, 6763-6772.
    • (2000) Biochemistry , vol.39 , pp. 6763-6772
    • Geijer, P.1    Deak, Z.2    Styring, S.3
  • 34
    • 44749086999 scopus 로고    scopus 로고
    • Direct quantification of the four individual S states in photosystem II using EPR spectroscopy
    • Han, G., Ho, F. M., Havelius, K. G. V., Morvaridi, S. F., Mamedov, F., and Styring, S. (2008) Direct quantification of the four individual S states in photosystem II using EPR spectroscopy. Biochim. Biophys. Acta 1777, 496-503.
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 496-503
    • Han, G.1    Ho, F.M.2    Havelius, K.G.V.3    Morvaridi, S.F.4    Mamedov, F.5    Styring, S.6
  • 36
    • 0026025417 scopus 로고
    • A guide to electron paramagnetic resonance spectroscopy of photosystem II membranes
    • Miller, A.-F., and Brudvig, G. W. (1991) A guide to electron paramagnetic resonance spectroscopy of photosystem II membranes. Biochim. Biophys. Acta 1056, 1-18.
    • (1991) Biochim. Biophys. Acta , vol.1056 , pp. 1-18
    • Miller, A.-F.1    Brudvig, G.W.2
  • 37
    • 0043167778 scopus 로고    scopus 로고
    • Two redox-active β-carotene molecules in photosystem II
    • Tracewell, C. A., and Brudvig, G. W. (2003) Two redox-active β-carotene molecules in photosystem II. Biochemistry 42, 9127-9136.
    • (2003) Biochemistry , vol.42 , pp. 9127-9136
    • Tracewell, C.A.1    Brudvig, G.W.2
  • 38
    • 0001563454 scopus 로고
    • slow varies with the redox state of the oxygen-evolving complex in photosystem-II
    • slow varies with the redox state of the oxygen-evolving complex in photosystem-II. Biochemistry 27, 4915-4923.
    • (1988) Biochemistry , vol.27 , pp. 4915-4923
    • Styring, S.A.1    Rutherford, A.W.2
  • 39
    • 0033576217 scopus 로고    scopus 로고
    • 2 states of the Mn cluster in photosystem II relax differently
    • 2 states of the Mn cluster in photosystem II relax differently. Biochemistry 38, 15223-15230.
    • (1999) Biochemistry , vol.38 , pp. 15223-15230
    • Peterson, S.1    Ahrling, K.A.2    Styring, S.3
  • 40
    • 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, 155-164.
    • (1995) Biochim. Biophys. Acta , vol.1230 , pp. 155-164
    • Andreasson, L.E.1    Vass, I.2    Styring, S.3
  • 42
    • 0001451266 scopus 로고
    • EPR relaxation measurements of photosystem II reaction centers - Influence of S-state oxidation and temperature
    • Evelo, R. G., Styring, S., Rutherford, A. W., and Hoff, A. J. (1989) EPR relaxation measurements of photosystem II reaction centers - Influence of S-state oxidation and temperature. Biochim. Biophys. Acta 973, 428-442.
    • (1989) Biochim. Biophys. Acta , vol.973 , pp. 428-442
    • Evelo, R.G.1    Styring, S.2    Rutherford, A.W.3    Hoff, A.J.4
  • 43
    • 0344074652 scopus 로고    scopus 로고
    • Characterization of the interaction between manganese and tyrosine Z in acetate-inhibited photosystem II
    • DOI 10.1021/bi9813025
    • Szalai, V. A., Kühne, H., Lakshmi, K. V., and Brudvig, G. W. (1998) Characterization of the interaction between manganese and tyrosine Z in acetate-inhibited photosystem II. Biochemistry 37, 13594-13603. (Pubitemid 28455534)
    • (1998) Biochemistry , vol.37 , Issue.39 , pp. 13594-13603
    • Szalai, V.A.1    Kuhne, H.2    Lakshmi, K.V.3    Brudvig, G.W.4
  • 44
    • 37249045907 scopus 로고    scopus 로고
    • •. An application of rapid-scan EPR to the study of intermediates of the water splitting mechanism of photosystem II
    • •. An application of rapid-scan EPR to the study of intermediates of the water splitting mechanism of photosystem II. Biochemistry 46, 14335-14341.
    • (2007) Biochemistry , vol.46 , pp. 14335-14341
    • Zahariou, G.1    Ioannidis, N.2    Sioros, G.3    Petrouleas, V.4
  • 46
    • 0037195238 scopus 로고    scopus 로고
    • Tyrosine D oxidation at cryogenic temperature in photosystem II
    • DOI 10.1021/bi026588z
    • Faller, P., Rutherford, A. W., and Debus, R. J. (2002) Tyrosine D oxidation at cryogenic temperature in photosystem II. Biochemistry 41, 12914-12920. (Pubitemid 35215773)
    • (2002) Biochemistry , vol.41 , Issue.43 , pp. 12914-12920
    • Faller, P.1    Rutherford, A.W.2    Debus, R.J.3
  • 47
    • 0035830370 scopus 로고    scopus 로고
    • Characterization of carotenoid and chlorophyll photooxidation in photosystem II
    • DOI 10.1021/bi001992o
    • Tracewell, C. A., Cua, A., Stewart, D. H., Bocian, D. F., and Brudvig, G. W. (2001) Characterization of carotenoid and chlorophyll photooxidation in photosystem II. Biochemistry 40, 193-203. (Pubitemid 32052692)
    • (2001) Biochemistry , vol.40 , Issue.1 , pp. 193-203
    • Tracewell, C.A.1    Cua, A.2    Stewart, D.H.3    Bocian, D.F.4    Brudvig, G.W.5
  • 48
    • 0033573843 scopus 로고    scopus 로고
    • Z in photosystem II with intact oxygen evolution capacity. Analysis of kinetic H/D isotope exchange effects
    • Z in photosystem II with intact oxygen evolution capacity. Analysis of kinetic H/D isotope exchange effects. Biochemistry 38, 2068-2077.
    • (1999) Biochemistry , vol.38 , pp. 2068-2077
    • Christen, G.1    Renger, G.2
  • 50
    • 0030046368 scopus 로고    scopus 로고
    • Effects of hydrogen/deuterium exchange on photosynthetic water cleavage in PS II core complexes from spinach
    • DOI 10.1016/0014-5793(95)01433-0
    • Karge, M., Irrgang, K. D., Sellin, S., Feinaugle, R., Liu, B., Eckert, H. J., Eichler, H. J., and Renger, G. (1996) Effects of hydrogen deuterium exchange on photosynthetic water cleavage in PS II core complexes from spinach. FEBS Lett. 378, 140-144. (Pubitemid 26015561)
    • (1996) FEBS Letters , vol.378 , Issue.2 , pp. 140-144
    • Karge, M.1    Irrgang, K.-D.2    Sellin, S.3    Feinaugle, R.4    Liu, B.5    Eckert, H.-J.6    Eichler, H.J.7    Renger, G.8
  • 51
    • 0002091376 scopus 로고
    • II (P-680) in photosystem II particles from Synechococcus sp
    • II (P-680) in photosystem II particles from Synechococcus sp. Biochim. Biophys. Acta 890, 23-31.
    • (1987) Biochim. Biophys. Acta , vol.890 , pp. 23-31
    • Schlodder, E.1    Meyer, B.2
  • 54
    • 0029033834 scopus 로고    scopus 로고
    • Amino acid residues that influence the binding of manganese or calcium to photosystem II. 1. The lumenal interhelical domains of the D1 polypeptide
    • Chu, H.-A., Nguyen, A. P., and Debus, R. J. (2002) Amino acid residues that influence the binding of manganese or calcium to photosystem II. 1. The lumenal interhelical domains of the D1 polypeptide. Biochemistry 34, 5839-5858.
    • (2002) Biochemistry , vol.34 , pp. 5839-5858
    • Chu, H.-A.1    Nguyen, A.P.2    Debus, R.J.3
  • 55
    • 0026215160 scopus 로고
    • Sequence analysis of the D1 and D2 reaction center proteins of photosystem II
    • Svensson, B., Vass, I., and Styring, S. (1991) Sequence analysis of the D1 and D2 reaction center proteins of photosystem II. Z. Naturforsch. C 46, 765-776.
    • (1991) Z. Naturforsch. C , vol.46 , pp. 765-776
    • Svensson, B.1    Vass, I.2    Styring, S.3
  • 56
    • 44649122732 scopus 로고    scopus 로고
    • Molecular origin of the pH dependence of tyrosine D oxidation kinetics and radical stability in photosystem II
    • Hienerwadel, R., Diner, B. A., and Berthomieu, C. (2008) Molecular origin of the pH dependence of tyrosine D oxidation kinetics and radical stability in photosystem II. Biochim. Biophys. Acta 1777, 525-531.
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 525-531
    • Hienerwadel, R.1    Diner, B.A.2    Berthomieu, C.3
  • 57
    • 0026096798 scopus 로고
    • PH-dependent charge equilibria between tyrosine-D and the S states in photosystem II. Estimation of relative midpoint redox potentials
    • Vass, I., and Styring, S. (1991) pH-dependent charge equilibria between tyrosine-D and the S states in photosystem II. Estimation of relative midpoint redox potentials. Biochemistry 30, 830-839.
    • (1991) Biochemistry , vol.30 , pp. 830-839
    • Vass, I.1    Styring, S.2
  • 59
    • 0019320139 scopus 로고
    • The effect of pH on the reduction kinetics of P-680 in tris-treated chloroplasts
    • Conjeaud, H., and Mathis, P. (1980) The effect of pH on the reduction kinetics of P-680 in tris-treated chloroplasts. Biochim. Biophys. Acta 590, 353-359.
    • (1980) Biochim. Biophys. Acta , vol.590 , pp. 353-359
    • Conjeaud, H.1    Mathis, P.2


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