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Volumn 43, Issue 21, 2004, Pages 6772-6782

Iron bound to the high-affinity Mn-binding site of the oxygen-evolving complex shifts the pK of a component controlling electron transport via Y Z

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANES; ELECTRON TRANSPORT PROPERTIES; FLUORESCENCE; IRON; MANGANESE; PH EFFECTS; REACTION KINETICS; SPECTROSCOPIC ANALYSIS;

EID: 2542549804     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi036047p     Document Type: Article
Times cited : (16)

References (78)
  • 1
    • 0002766044 scopus 로고    scopus 로고
    • P680, the primary electron donor of photosystem II
    • Barber, J., and Archer, M. D. (2001) P680, the primary electron donor of photosystem II, J. Photochem. Photobiol., A 142, 97-106.
    • (2001) J. Photochem. Photobiol., A , vol.142 , pp. 97-106
    • Barber, J.1    Archer, M.D.2
  • 3
    • 0000970644 scopus 로고
    • II reduction kinetics with nanosecond time resolution in oxygen-evolving photosystem II particles from Synechococcus at 680 and 824 nm
    • II reduction kinetics with nanosecond time resolution in oxygen-evolving photosystem II particles from Synechococcus at 680 and 824 nm, Biochim. Biophys. Acta 765, 178-185.
    • (1984) Biochim. Biophys. Acta , vol.765 , pp. 178-185
    • Schlodder, E.1    Brettel, K.2    Schatz, G.H.3    Witt, H.T.4
  • 4
    • 0032570284 scopus 로고    scopus 로고
    • Function of tyrosin Z in water oxidation by photosystem II: Electrostatical promotor instead of hydrogen abstractor
    • Ahlbrink, R., Haumann, M., Cherepanov, D., Bögershausen, O., Mulkidjanian, A., and Junge, W. (1998) Function of tyrosin Z in water oxidation by photosystem II: electrostatical promotor instead of hydrogen abstractor, Biochemistry 37, 1131-1142.
    • (1998) Biochemistry , vol.37 , pp. 1131-1142
    • Ahlbrink, R.1    Haumann, M.2    Cherepanov, D.3    Bögershausen, O.4    Mulkidjanian, A.5    Junge, W.6
  • 5
    • 0023426051 scopus 로고
    • Tyrosine radicals are involved in the photosynthetic oxygen-evolving system
    • Barry, B. A., and Babcock, G. T. (1987) Tyrosine radicals are involved in the photosynthetic oxygen-evolving system, Proc. Natl. Acad. Sci. U.S.A. 84, 7099-7103.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 7099-7103
    • Barry, B.A.1    Babcock, G.T.2
  • 9
    • 0032527668 scopus 로고    scopus 로고
    • 55Mn Pulsed ENDOR demonstrates that the photosystem II "split" EPR signal arises from a magnetically-coupled mangano-tyrosyl complex
    • 55Mn Pulsed ENDOR demonstrates that the photosystem II "split" EPR signal arises from a magnetically-coupled mangano-tyrosyl complex, J. Am. Chem. Soc. 120, 6840-6841.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 6840-6841
    • Peloquin, J.M.1    Campbell, K.A.2    Britt, R.D.3
  • 10
    • 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. (2001) Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution, Nature 409, 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
  • 12
    • 33749081612 scopus 로고    scopus 로고
    • A mechanistic and structural model for the formation and reactivity of a Mn-V=O species in photosynthetic water oxidation
    • Limburg, J., Szalai, V. A., and Brudvig, G. W. (1999) A mechanistic and structural model for the formation and reactivity of a Mn-V=O species in photosynthetic water oxidation, J. Chem. Soc., Dalton Trans., 1353-1361.
    • (1999) J. Chem. Soc., Dalton Trans. , pp. 1353-1361
    • Limburg, J.1    Szalai, V.A.2    Brudvig, G.W.3
  • 13
    • 0033874086 scopus 로고    scopus 로고
    • Pulsed and parallel-polarization EPR characterization of the photosystem II oxygen-evolving complex
    • Britt, R. D., Peloquin, J. M., and Campbell, K. A. (2000) Pulsed and parallel-polarization EPR characterization of the photosystem II oxygen-evolving complex, Annu. Rev. Biophys. Biomol. Struct. 29, 463-495.
    • (2000) Annu. Rev. Biophys. Biomol. Struct. , vol.29 , pp. 463-495
    • Britt, R.D.1    Peloquin, J.M.2    Campbell, K.A.3
  • 16
    • 0034640197 scopus 로고    scopus 로고
    • Proton and hydrogen currents in photosynthetic water oxidation
    • Thommos, C., and Babcock, G. T. (2000) Proton and hydrogen currents in photosynthetic water oxidation, Biochim. Biophys. Acta 1458, 199-219.
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 199-219
    • Thommos, C.1    Babcock, G.T.2
  • 17
    • 0031882184 scopus 로고    scopus 로고
    • D of photosystem II: Comparison of optical spectra to those of tyrosine oxidised by pulsed radiolysis
    • D of photosystem II: Comparison of optical spectra to those of tyrosine oxidised by pulsed radiolysis, Biochim. Biophys. Acta 1363, 1-5.
    • (1998) Biochim. Biophys. Acta , vol.1363 , pp. 1-5
    • Candeias, L.P.1    Turconi, S.2    Nugent, J.H.A.3
  • 20
    • 0032575361 scopus 로고    scopus 로고
    • Hydrogen bonding of redox-active tyrosine Z of photosystem II probed by FTIR difference spectroscopy
    • 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.
    • (1998) Biochemistry , vol.37 , pp. 10547-10554
    • Berthomieu, C.1    Hienerwadel, R.2    Boussac, A.3    Breton, J.4    Diner, B.A.5
  • 21
    • 0025298292 scopus 로고
    • Structure of donor side components in photosystem II predicted by computer modelling
    • Svensson, B., Vass, I., Cedergren, E., and Styring, S. (1990) Structure of donor side components in photosystem II predicted by computer modelling, EMBO J. 9, 2051-2059.
    • (1990) EMBO J. , vol.9 , pp. 2051-2059
    • Svensson, B.1    Vass, I.2    Cedergren, E.3    Styring, S.4
  • 23
    • 0028242817 scopus 로고
    • Lumenal side histidine mutations in the D1 protein of photosystem II affect donor side electron transfer in Chlamydomonas reinhardtii
    • Roffey, R. A., Kramer, D. M., Govindjee, and Sayre, R. T. (1994) Lumenal side histidine mutations in the D1 protein of photosystem II affect donor side electron transfer in Chlamydomonas reinhardtii, Biochim. Biophys. Acta 1185, 257-270.
    • (1994) Biochim. Biophys. Acta , vol.1185 , pp. 257-270
    • Roffey, R.A.1    Kramer, D.M.2    Govindjee3    Sayre, R.T.4
  • 24
    • 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
    • Mamedov, F., Sayre, R. T., and Sryring, 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.
    • (1998) Biochemistry , vol.37 , pp. 14245-14256
    • Mamedov, F.1    Sayre, R.T.2    Sryring, S.3
  • 25
    • 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
  • 27
    • 0035808702 scopus 로고    scopus 로고
    • Amino acid residues involved in the coordination and assembly of the manganese cluster of photosystem II. Proton-coupled electron transport of the redox-active tyrosines and its relationship to water oxidation
    • Diner, B. A. (2001) Amino acid residues involved in the coordination and assembly of the manganese cluster of photosystem II. Proton-coupled electron transport of the redox-active tyrosines and its relationship to water oxidation, Biochim. Biophys. Acta 1503, 147-163.
    • (2001) Biochim. Biophys. Acta , vol.1503 , pp. 147-163
    • Diner, B.A.1
  • 28
    • 0035808665 scopus 로고    scopus 로고
    • Z and the manganese cluster in the water oxidizing complex of photosystem II
    • Z and the manganese cluster in the water oxidizing complex of photosystem II, Biochim. Biophys. Acta 1503, 164-186.
    • (2001) Biochim. Biophys. Acta , vol.1503 , pp. 164-186
    • Debus, R.J.1
  • 30
    • 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
  • 31
    • 8544246786 scopus 로고    scopus 로고
    • The role of protonation steps in electron transfer reactions in Tris-treated photosystem 2 membrane
    • Christen, G., Karge, M., Eckert, H.-J., and Renger, G. (1997) The role of protonation steps in electron transfer reactions in Tris-treated photosystem 2 membrane, Photosynthetica 33, 529-539.
    • (1997) Photosynthetica , vol.33 , pp. 529-539
    • Christen, G.1    Karge, M.2    Eckert, H.-J.3    Renger, G.4
  • 32
    • 0026569892 scopus 로고
    • Aspartate 170 of the photosystem II reaction center polypeptide D1 is involved in the assembly of the oxygen-evolving manganese cluster
    • Nixon, P. J., and Diner, B. A. (1992) Aspartate 170 of the photosystem II reaction center polypeptide D1 is involved in the assembly of the oxygen-evolving manganese cluster, Biochemistry 31, 942-948.
    • (1992) Biochemistry , vol.31 , pp. 942-948
    • Nixon, P.J.1    Diner, B.A.2
  • 33
    • 0001780455 scopus 로고
    • Lack of photoactivation capacity in Scenedesmus obliquus LF-1 results from loss of half the high-affinity manganese-binding site. Relationship to the unprocessed D1 protein
    • Seibert, M., Tamura, N., and Inoue, Y. (1989) Lack of photoactivation capacity in Scenedesmus obliquus LF-1 results from loss of half the high-affinity manganese-binding site. Relationship to the unprocessed D1 protein, Biochim. Biophys. Acta 974, 185-191.
    • (1989) Biochim. Biophys. Acta , vol.974 , pp. 185-191
    • Seibert, M.1    Tamura, N.2    Inoue, Y.3
  • 34
    • 0033153216 scopus 로고    scopus 로고
    • 2+) binding to the manganese site of the apo-water oxidation complex of photosystem II
    • 2+) binding to the manganese site of the apo-water oxidation complex of photosystem II, Biochemistry 38, 7200-7209.
    • (1999) Biochemistry , vol.38 , pp. 7200-7209
    • Ananyev, G.M.1    Murphy, A.2    Abe, Y.3    Dismukes, G.C.4
  • 35
    • 0025942237 scopus 로고
    • The carboxyl modifier 1-ethyl-3-[3-(dimethylamino)propyl]carbodiimide (EDC) inhibits half of the high-affinity manganese-binding site in photosystem II membrane fragments
    • Preston, C., and Seibert, M. (1991) The carboxyl modifier 1-ethyl-3-[3-(dimethylamino)propyl]carbodiimide (EDC) inhibits half of the high-affinity manganese-binding site in photosystem II membrane fragments, Biochemistry 30, 9615-9624.
    • (1991) Biochemistry , vol.30 , pp. 9615-9624
    • Preston, C.1    Seibert, M.2
  • 36
    • 0026042670 scopus 로고
    • Protease treatments of photosystem II membrane fragments reveal that these are four separate high-affinity manganese-binding site
    • Preston, C., and Seibert, M. (1991) Protease treatments of photosystem II membrane fragments reveal that these are four separate high-affinity manganese-binding site, Biochemistry 30, 9625-9633.
    • (1991) Biochemistry , vol.30 , pp. 9625-9633
    • Preston, C.1    Seibert, M.2
  • 37
    • 0026635213 scopus 로고
    • 2+ is slowed in a site-directed mutant, at aspartate 170 of polypeptide D1 of photosystem II, inactive for photosynthetic oxygen evolution
    • 2+ is slowed in a site-directed mutant, at aspartate 170 of polypeptide D1 of photosystem II, inactive for photosynthetic oxygen evolution, Biochim. Biophys. Acta 1101, 134-138.
    • (1992) Biochim. Biophys. Acta , vol.1101 , pp. 134-138
    • Diner, B.A.1    Nixon, P.J.2
  • 38
    • 0030047238 scopus 로고    scopus 로고
    • Interactions between diphenylcarbazide, zinc, cobalt, and manganese on the oxidizing side of photosystem II
    • Ghirardi, M. L., Lutton, T. W., and Seibert, M. (1996) Interactions between diphenylcarbazide, zinc, cobalt, and manganese on the oxidizing side of photosystem II, Biochemistry 35, 1820-1828.
    • (1996) Biochemistry , vol.35 , pp. 1820-1828
    • Ghirardi, M.L.1    Lutton, T.W.2    Seibert, M.3
  • 39
    • 0342378161 scopus 로고    scopus 로고
    • Different manganese binding sites in photosystem II probed by selective chemical modification of histidyl and carboxylic acid residues
    • Magnuson, A., and Andréasson, L.-E. (1997) Different manganese binding sites in photosystem II probed by selective chemical modification of histidyl and carboxylic acid residues, Biochemistry 36, 3254-3261.
    • (1997) Biochemistry , vol.36 , pp. 3254-3261
    • Magnuson, A.1    Andréasson, L.-E.2
  • 40
    • 0032578443 scopus 로고    scopus 로고
    • Effects of carboxyl amino acid modification on the properties of the high-affinity, manganese-binding site in photosystem II
    • Ghirardi, M. L., Lutton, T. W., and Seibert, M. (1998) Effects of carboxyl amino acid modification on the properties of the high-affinity, manganese-binding site in photosystem II, Biochemistry 37, 13559-13566.
    • (1998) Biochemistry , vol.37 , pp. 13559-13566
    • Ghirardi, M.L.1    Lutton, T.W.2    Seibert, M.3
  • 41
    • 0032578561 scopus 로고    scopus 로고
    • Use of a novel histidyl modifier to probe for residues on tris-treated photosystem II membrane fragments that may bind functional manganese
    • Ghirardi, M. L., Preston, C., and Seibert, M. (1998) Use of a novel histidyl modifier to probe for residues on tris-treated photosystem II membrane fragments that may bind functional manganese, Biochemistry 37, 13567-13574.
    • (1998) Biochemistry , vol.37 , pp. 13567-13574
    • Ghirardi, M.L.1    Preston, C.2    Seibert, M.3
  • 42
    • 0033529206 scopus 로고    scopus 로고
    • Z tyrosine in manganese-depleted photosystem II membranes
    • Z tyrosine in manganese-depleted photosystem II membranes, Biochemistry 38, 8778-8785.
    • (1999) Biochemistry , vol.38 , pp. 8778-8785
    • Ono, T.-A.1    Mino, H.2
  • 43
    • 0034685473 scopus 로고    scopus 로고
    • Dual-mode EPR detects the initial intermediate in photoassembly of the photosystem II Mn cluster: The influence of amino acid residue 170 of the D1 polypeptide on Mn coordinating
    • Campbell, K. A., Force, D. A., Nixon, P. J., Dole, F., Diner, B. A., and Britt, R. D. (2000) Dual-mode EPR detects the initial intermediate in photoassembly of the photosystem II Mn cluster: the influence of amino acid residue 170 of the D1 polypeptide on Mn coordinating, J. Am. Chem. Soc. 122, 3754-3761.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 3754-3761
    • Campbell, K.A.1    Force, D.A.2    Nixon, P.J.3    Dole, F.4    Diner, B.A.5    Britt, R.D.6
  • 44
    • 0000052348 scopus 로고
    • Photoassembly of the photosystem II manganese cluster
    • (Murata, N., Ed.), Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Blubaugh, D. J., and Cheniae, G. M. (1992) Photoassembly of the photosystem II manganese cluster, in Research in Photosynthesis (Murata, N., Ed.) Vol. II, pp 361-364, Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1992) Research in Photosynthesis , vol.2 , pp. 361-364
    • Blubaugh, D.J.1    Cheniae, G.M.2
  • 45
    • 0002223158 scopus 로고
    • The high-affinity binding site for manganese on the oxidizing side of photosystem II
    • Hsu, B.-D., Lee, J.-I., and Pan, R.-L. (1987) The high-affinity binding site for manganese on the oxidizing side of photosystem II, Biochim. Biophys. Acta 890, 89-96.
    • (1987) Biochim. Biophys. Acta , vol.890 , pp. 89-96
    • Hsu, B.-D.1    Lee, J.-I.2    Pan, R.-L.3
  • 46
    • 0028867252 scopus 로고
    • High-specific binding of Fe(II) at the Mn-binding site in Mn-depleted PSII membranes from spinach
    • Semin, B. K., Ivanov, I. I., Rubin, A. B., and Parak, F. (1995) High-specific binding of Fe(II) at the Mn-binding site in Mn-depleted PSII membranes from spinach, FEBS Lett. 375, 223-226.
    • (1995) FEBS Lett. , vol.375 , pp. 223-226
    • Semin, B.K.1    Ivanov, I.I.2    Rubin, A.B.3    Parak, F.4
  • 47
    • 0008943824 scopus 로고    scopus 로고
    • Formation of dinuclear Fe(III) center by interaction of Fe(II) with the Mn-binding site of Mn-deleted PSII membranes
    • (Garab, G., Ed.), Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Semin, B. K., Davletschina, L., Ivanov, I. I., Reiner, M., and Parak, F. (1998) Formation of dinuclear Fe(III) center by interaction of Fe(II) with the Mn-binding site of Mn-deleted PSII membranes, in Photosynthesis: Mechanism and Effects (Garab, G., Ed.) Vol. II, pp 1415-1418, Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1998) Photosynthesis: Mechanism and Effects , vol.2 , pp. 1415-1418
    • Semin, B.K.1    Davletschina, L.2    Ivanov, I.I.3    Reiner, M.4    Parak, F.5
  • 48
    • 0031036741 scopus 로고    scopus 로고
    • Coordination sphere and structure of the Mn cluster of the oxygen-evolving complex in photosynthetic organisms
    • Semin, B. K., and Parak, F. (1997) Coordination sphere and structure of the Mn cluster of the oxygen-evolving complex in photosynthetic organisms, FEBS Lett. 400, 259-262.
    • (1997) FEBS Lett. , vol.400 , pp. 259-262
    • Semin, B.K.1    Parak, F.2
  • 49
    • 0037035551 scopus 로고    scopus 로고
    • Z· following incubation of Mn-depleted photosystem II membranes with Fe(II) in the light
    • Z· following incubation of Mn-depleted photosystem II membranes with Fe(II) in the light, Biochemistry 41, 5854-5864.
    • (2002) Biochemistry , vol.41 , pp. 5854-5864
    • Semin, B.K.1    Ghirardi, M.L.2    Seibert, M.3
  • 50
    • 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., Tompson, W. A., and Kriedemann, P. E. (1989) 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, 384-394.
    • (1989) Biochim. Biophys. Acta , vol.975 , pp. 384-394
    • Porra, R.J.1    Tompson, W.A.2    Kriedemann, P.E.3
  • 51
    • 0025785346 scopus 로고
    • Construction and characterization of cyanobacterial mutants lacking the manganese-stabilizing polypeptide of photosystem II
    • Philbrick, J. B., Diner, B. A., and Zilinskas, B. A. (1991) Construction and characterization of cyanobacterial mutants lacking the manganese-stabilizing polypeptide of photosystem II, J. Biol. Chem. 266, 13370-13376.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13370-13376
    • Philbrick, J.B.1    Diner, B.A.2    Zilinskas, B.A.3
  • 52
    • 46149142812 scopus 로고
    • Primary-charge separation and excitation of chlorophyll a in photosystem II particles from spinach as studied 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 studied by picosecond absorbance-difference spectroscopy, Biochim. Biophys. Acta 848, 167-175.
    • (1986) Biochim. Biophys. Acta , vol.848 , pp. 167-175
    • Nuijs, A.M.1    Van Gorkom, H.J.2    Plijter, J.J.3    Duysens, L.M.N.4
  • 53
    • 0001708374 scopus 로고
    • Primary nature of fluorescence yield changes associated with photosynthesis
    • Butler, W. L. (1972) Primary nature of fluorescence yield changes associated with photosynthesis, Proc. Natl. Acad. Sci. U.S.A. 69, 3420-3422.
    • (1972) Proc. Natl. Acad. Sci. U.S.A. , vol.69 , pp. 3420-3422
    • Butler, W.L.1
  • 54
    • 49049126264 scopus 로고
    • Kinetics of the oxidation-reduction reactions of the photosystem II quinone acceptor complex, and the pathway for deactivation
    • Robinson, H. H., and Crofts, A. R. (1983) Kinetics of the oxidation-reduction reactions of the photosystem II quinone acceptor complex, and the pathway for deactivation, FEBS Lett. 153, 221-226.
    • (1983) FEBS Lett. , vol.153 , pp. 221-226
    • Robinson, H.H.1    Crofts, A.R.2
  • 55
    • 0030660560 scopus 로고    scopus 로고
    • Charge recombination and proton transfer in manganese-depleted photosystem II
    • Rappaport, F., and Lavergne, J. (1997) Charge recombination and proton transfer in manganese-depleted photosystem II, Biochemistry 36, 15294-15302.
    • (1997) Biochemistry , vol.36 , pp. 15294-15302
    • Rappaport, F.1    Lavergne, J.2
  • 56
    • 0029033834 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. (1995) 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.
    • (1995) Biochemistry , vol.34 , pp. 5839-5858
    • Chu, H.-A.1    Nguyen, A.P.2    Debus, R.J.3
  • 57
    • 0030660643 scopus 로고    scopus 로고
    • Modification of the photosystem II acceptor side function in a D1 mutant (arginine-269-glycine) of Chlamydomonas reinhardti
    • Xiong, J., Hutchison, R. S., Sayre, R. T., and Govindjee (1997) Modification of the photosystem II acceptor side function in a D1 mutant (arginine-269-glycine) of Chlamydomonas reinhardti, Biochim. Biophys. Acta 1322, 60-76.
    • (1997) Biochim. Biophys. Acta , vol.1322 , pp. 60-76
    • Xiong, J.1    Hutchison, R.S.2    Sayre, R.T.3    Govindjee4
  • 58
    • 0032551753 scopus 로고    scopus 로고
    • Loss of inhibition by formate in newly constructed photosystem II D1 mutants, D1-R257E and D1-R257M, of Chlamydomonas reinhardtii
    • Xiong, J., Minagawa, J., Crofts, A., and Govindjee (1998) Loss of inhibition by formate in newly constructed photosystem II D1 mutants, D1-R257E and D1-R257M, of Chlamydomonas reinhardtii, Biochim. Biophys. Acta 1365, 473-491.
    • (1998) Biochim. Biophys. Acta , vol.1365 , pp. 473-491
    • Xiong, J.1    Minagawa, J.2    Crofts, A.3    Govindjee4
  • 59
    • 0000946086 scopus 로고
    • Quantitative analysis of the inactivation of photosynthetic oxygen evolution and the release of polypeptides and manganese in the photosystem-II particles of spinach chloroplasts
    • Kuwabara, T., and Murata, N. (1983) Quantitative analysis of the inactivation of photosynthetic oxygen evolution and the release of polypeptides and manganese in the photosystem-II particles of spinach chloroplasts, Plant Cell Physiol. 24, 741-747.
    • (1983) Plant Cell Physiol. , vol.24 , pp. 741-747
    • Kuwabara, T.1    Murata, N.2
  • 62
    • 0035808688 scopus 로고    scopus 로고
    • Coupling of electron and proton transfer in the photosynthetic water oxidase
    • Rappaport, F., and Lavergne, J. (2001) Coupling of electron and proton transfer in the photosynthetic water oxidase, Biochim. Biophys. Acta 1503, 246-259.
    • (2001) Biochim. Biophys. Acta , vol.1503 , pp. 246-259
    • Rappaport, F.1    Lavergne, J.2
  • 64
    • 0037183499 scopus 로고    scopus 로고
    • Biochemical, Mössbauer, and EPR studies of the diiron cluster of phenol hydroxylase from Pseudomonas sp. strain CF 600
    • Cadieux, E., Vrajmasu, V., Achim, C., Powlowski, J., and Münck, E. (2002) Biochemical, Mössbauer, and EPR studies of the diiron cluster of phenol hydroxylase from Pseudomonas sp. strain CF 600, Biochemistry 41, 10680-10691.
    • (2002) Biochemistry , vol.41 , pp. 10680-10691
    • Cadieux, E.1    Vrajmasu, V.2    Achim, C.3    Powlowski, J.4    Münck, E.5
  • 66
    • 0025370526 scopus 로고
    • Kinetics of photoinhibition in hydroxylamine-extracted photosystem II membranes: Relevance to photoactivation and sites of electron donation
    • Blubaugh, D. J., and Cheniae, G. M. (1990) Kinetics of photoinhibition in hydroxylamine-extracted photosystem II membranes: relevance to photoactivation and sites of electron donation, Biochemistry 29, 5109-5118.
    • (1990) Biochemistry , vol.29 , pp. 5109-5118
    • Blubaugh, D.J.1    Cheniae, G.M.2
  • 67
    • 0017063825 scopus 로고
    • Flash-induced absorption changes of the primary donor of photosystem II at 820 nm in chloroplasts inhibited by low pH or tris-treatment
    • Haveman, J., and Mathis, P. (1976) Flash-induced absorption changes of the primary donor of photosystem II at 820 nm in chloroplasts inhibited by low pH or tris-treatment, Biochim. Biophys. Acta 440, 346-355.
    • (1976) Biochim. Biophys. Acta , vol.440 , pp. 346-355
    • Haveman, J.1    Mathis, P.2
  • 68
    • 0017284530 scopus 로고
    • The existence of a high photochemical turnover rate at the reaction centers of system II in Tris-washed chloroplasts
    • Renger, G., and Wolff, C. H. (1976) The existence of a high photochemical turnover rate at the reaction centers of system II in Tris-washed chloroplasts, Biochim. Biophys. Acta 423, 610-614.
    • (1976) Biochim. Biophys. Acta , vol.423 , pp. 610-614
    • Renger, G.1    Wolff, C.H.2
  • 69
    • 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. Acad. Sci. Paris 258, 4622-4625.
    • (1964) C. R. Acad. Sci. Paris , vol.258 , pp. 4622-4625
    • Joliot, A.1    Joliot, P.2
  • 70
    • 0018197718 scopus 로고
    • 2+ on the photochemistry at one type of reaction center in photosystem II of chloroplasts
    • 2+ on the photochemistry at one type of reaction center in photosystem II of chloroplasts, Arch. Biochem. Biophys. 190, 523-530.
    • (1978) Arch. Biochem. Biophys. , vol.190 , pp. 523-530
    • Melis, A.1    Homann, P.H.2
  • 72
    • 0037158924 scopus 로고    scopus 로고
    • Proton-coupled electron transfer involving tyrosine Z in photosystem II
    • Kühne, H., and Brudvig, G. W. (2002) Proton-coupled electron transfer involving tyrosine Z in photosystem II, J. Phys. Chem. B 106, 8189-8196.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 8189-8196
    • Kühne, H.1    Brudvig, G.W.2
  • 73
    • 0033604868 scopus 로고    scopus 로고
    • Tyrosine-Z in oxygen-evolving photosystem II: A hydrogen-bonded tyrosinate
    • Haumann, M., Mulkijanian, A., and Junge, W. (1999) Tyrosine-Z in oxygen-evolving photosystem II: a hydrogen-bonded tyrosinate, Biochemistry 38, 1258-1267.
    • (1999) Biochemistry , vol.38 , pp. 1258-1267
    • Haumann, M.1    Mulkijanian, A.2    Junge, W.3
  • 75
    • 0037928595 scopus 로고    scopus 로고
    • The iron-oxygen reconstitution reaction in protein R2-Tyr-177 mutants of mouse ribonucleotide reductase. EPR and electron nuclear double resonance studies on a new transiet tryptophan radical
    • Pötsch, S., Lendzian, F., Ingemarson, R., Hörngerg, A., Thelander, L., Lubitz, W., Lassmann, G., and Gräslund, A. (1999) The iron-oxygen reconstitution reaction in protein R2-Tyr-177 mutants of mouse ribonucleotide reductase. EPR and electron nuclear double resonance studies on a new transiet tryptophan radical, J. Biol. Chem. 274, 17696-17704.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17696-17704
    • Pötsch, S.1    Lendzian, F.2    Ingemarson, R.3    Hörngerg, A.4    Thelander, L.5    Lubitz, W.6    Lassmann, G.7    Gräslund, A.8
  • 76
    • 45949125703 scopus 로고
    • Photoactivation of the water-oxidizing complex in photosystem II membranes depleted of Mn and extrinsic proteins. I. Biochemical and kinetic characterization
    • Tamura, N., and Cheniae, G. M. (1987) Photoactivation of the water-oxidizing complex in photosystem II membranes depleted of Mn and extrinsic proteins. I. Biochemical and kinetic characterization, Biochim. Biophys. Acta 890, 179-194.
    • (1987) Biochim. Biophys. Acta , vol.890 , pp. 179-194
    • Tamura, N.1    Cheniae, G.M.2
  • 77
    • 0032879783 scopus 로고    scopus 로고
    • Voltammetric detection of superoxide production by photosystem II
    • Cleland, R. E., and Grace, S. C. (1999) Voltammetric detection of superoxide production by photosystem II, FEBS Lett. 457, 348-352.
    • (1999) FEBS Lett. , vol.457 , pp. 348-352
    • Cleland, R.E.1    Grace, S.C.2
  • 78
    • 0037298085 scopus 로고    scopus 로고
    • Participation of photosynthetic electron transport in production and scavenging of reactive oxygen species
    • Ivanov, B., and Khorobrykh, S. (2003) Participation of photosynthetic electron transport in production and scavenging of reactive oxygen species, Antioxid. Redox Signaling 5, 43-53.
    • (2003) Antioxid. Redox Signaling , vol.5 , pp. 43-53
    • Ivanov, B.1    Khorobrykh, S.2


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