메뉴 건너뛰기




Volumn 1767, Issue 6, 2007, Pages 404-413

Purification, crystallization and X-ray diffraction analyses of the T. elongatus PSII core dimer with strontium replacing calcium in the oxygen-evolving complex

Author keywords

Fluorescence decay and imaging; Photosynthesis; Photosystem II structure; Strontium replacement; Water splitting; X ray crystallography

Indexed keywords

CALCIUM; DIMER; OXYGEN; STRONTIUM;

EID: 34249807336     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2007.01.007     Document Type: Article
Times cited : (37)

References (47)
  • 1
    • 0036667743 scopus 로고    scopus 로고
    • Photosystem II: a multisubunit membrane protein that oxidises water
    • Barber J. Photosystem II: a multisubunit membrane protein that oxidises water. Curr. Opin. Struct. Biol. 12 (2002) 523-530
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 523-530
    • Barber, J.1
  • 2
    • 84980182243 scopus 로고
    • Un nouveaux modele des centres photochimiques due systeme II
    • Joliot P., Barbieri G., and Chabaud R. Un nouveaux modele des centres photochimiques due systeme II. Photochem. Photobiol. 10 (1969) 309-329
    • (1969) Photochem. Photobiol. , vol.10 , pp. 309-329
    • Joliot, P.1    Barbieri, G.2    Chabaud, R.3
  • 5
    • 0025850488 scopus 로고
    • Calcium activation of photosynthetic water oxidation
    • Yocum C.F. Calcium activation of photosynthetic water oxidation. Biochim. Biophys. Acta 1059 (1991) 1-15
    • (1991) Biochim. Biophys. Acta , vol.1059 , pp. 1-15
    • Yocum, C.F.1
  • 6
    • 0026707522 scopus 로고
    • The manganese and calcium ions of photosynthetic oxygen evolution
    • Debus R.J. 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
  • 8
    • 0001370291 scopus 로고
    • Light-reactivation of (Tris-washed)-DPIP-treated chloroplasts: manganese incorporation, chlorophyll fluorescence, action spectrum and oxygen evolution
    • Yamashita T., and Tomita G. Light-reactivation of (Tris-washed)-DPIP-treated chloroplasts: manganese incorporation, chlorophyll fluorescence, action spectrum and oxygen evolution. Plant Cell Physiol. 17 (1976) 571-582
    • (1976) Plant Cell Physiol. , vol.17 , pp. 571-582
    • Yamashita, T.1    Tomita, G.2
  • 10
    • 0035808693 scopus 로고    scopus 로고
    • The inorganic biochemistry of photosynthetic oxygen evolution/water oxidation
    • Ananyev G.M., Zaltsman L., Vasko C., and Dismukes G.C. The inorganic biochemistry of photosynthetic oxygen evolution/water oxidation. Biochim. Biophys. Acta 1503 (2001) 52-68
    • (2001) Biochim. Biophys. Acta , vol.1503 , pp. 52-68
    • Ananyev, G.M.1    Zaltsman, L.2    Vasko, C.3    Dismukes, G.C.4
  • 12
    • 0029129548 scopus 로고
    • Evidence for the proximity of calcium to the manganese cluster of photosystem II: determination by X-ray absorption spectroscopy
    • Latimer M.J., DeRose V.J., Mukerji I., Yachandra V.K., Sauer K., and Klein M.P. Evidence for the proximity of calcium to the manganese cluster of photosystem II: determination by X-ray absorption spectroscopy. Biochemistry 34 (1995) 10898-10909
    • (1995) Biochemistry , vol.34 , pp. 10898-10909
    • Latimer, M.J.1    DeRose, V.J.2    Mukerji, I.3    Yachandra, V.K.4    Sauer, K.5    Klein, M.P.6
  • 13
    • 0000061390 scopus 로고    scopus 로고
    • Strontium EXAFS reveals the proximity of calcium to the manganese cluster of oxygen-evolving photosystem II
    • Cinco R.M., Robblee J.H., Rompel A., Fernandez C., Yachandra V.K., Sauer K., and Klein M.P. Strontium EXAFS reveals the proximity of calcium to the manganese cluster of oxygen-evolving photosystem II. J. Phys. Chem., B 102 (1998) 8248-8256
    • (1998) J. Phys. Chem., B , vol.102 , pp. 8248-8256
    • Cinco, R.M.1    Robblee, J.H.2    Rompel, A.3    Fernandez, C.4    Yachandra, V.K.5    Sauer, K.6    Klein, M.P.7
  • 15
    • 0036357745 scopus 로고    scopus 로고
    • An evaluation of structural models for the photosynthetic water-oxidizing complex derived from spectroscopic and X-ray diffraction signatures
    • Carrell T.G., Tyryshkin A.M., and Dismukes G.C. An evaluation of structural models for the photosynthetic water-oxidizing complex derived from spectroscopic and X-ray diffraction signatures. J. Biol. Inorg. Chem. 7 (2002) 2-22
    • (2002) J. Biol. Inorg. Chem. , vol.7 , pp. 2-22
    • Carrell, T.G.1    Tyryshkin, A.M.2    Dismukes, G.C.3
  • 18
    • 30744445692 scopus 로고    scopus 로고
    • Towards complete cofactor arrangement in the 3.0 A resolution structure of photosystem II
    • Loll B., Kern J., Saenger W., Zouni A., and Biesiadka J. Towards complete cofactor arrangement in the 3.0 A resolution structure of photosystem II. Nature 438 (2005) 1040-1044
    • (2005) Nature , vol.438 , pp. 1040-1044
    • Loll, B.1    Kern, J.2    Saenger, W.3    Zouni, A.4    Biesiadka, J.5
  • 20
    • 33645552565 scopus 로고    scopus 로고
    • Identification of a calcium-binding site in the PsbO protein of photosystem II
    • Murray J.W., and Barber J. Identification of a calcium-binding site in the PsbO protein of photosystem II. Biochemistry 45 (2006) 4128-4130
    • (2006) Biochemistry , vol.45 , pp. 4128-4130
    • Murray, J.W.1    Barber, J.2
  • 22
    • 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
    • Sugiura M., and Inoue Y. 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
  • 23
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger H., and von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166 (1987) 368-379
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    von Jagow, G.2
  • 24
    • 0037072291 scopus 로고    scopus 로고
    • The mechanism of UV-A radiation-induced inhibition of photosystem II electron transport studied by EPR and chlorophyll fluorescence
    • Vass I., Turcsanyi E., Touloupakis E., Ghanotakis D., and Petrouleas V. The mechanism of UV-A radiation-induced inhibition of photosystem II electron transport studied by EPR and chlorophyll fluorescence. Biochemistry 41 (2002) 10200-10208
    • (2002) Biochemistry , vol.41 , pp. 10200-10208
    • Vass, I.1    Turcsanyi, E.2    Touloupakis, E.3    Ghanotakis, D.4    Petrouleas, V.5
  • 25
    • 0003076963 scopus 로고
    • Recent changes to the MOSFLM package for processing film and image plate data. Joint CCP4 + ESF-EAMCB Newsletter on Protein
    • Leslie A.G.W. Recent changes to the MOSFLM package for processing film and image plate data. Joint CCP4 + ESF-EAMCB Newsletter on Protein. Crystallography (1992) 26
    • (1992) Crystallography , pp. 26
    • Leslie, A.G.W.1
  • 28
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53 (1997) 240-255
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 29
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • The CCP4 Consortium. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50 (1994) 760-763
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
    • The CCP4 Consortium1
  • 31
    • 0003845223 scopus 로고    scopus 로고
    • DeLano Scientific, San Carlos, CA, USA http://www.pymol.org
    • DeLano W.L. The PyMOL Molecular Graphics System (2002), DeLano Scientific, San Carlos, CA, USA. http://www.pymol.org http://www.pymol.org
    • (2002) The PyMOL Molecular Graphics System
    • DeLano, W.L.1
  • 32
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel E., and Henrick K. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr. D 60 (2004) 2256-2268
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 33
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60 (2004) 2126-2132
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 34
    • 0000981541 scopus 로고
    • Calcium reconstitutes high rates of oxygen evolution in polypeptide depleted photosystem II preparations
    • Ghanotakis D.F., Babcock G.T., and Yocum C.F. 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
  • 36
    • 0034617209 scopus 로고    scopus 로고
    • Towards structural determination of the water-splitting enzyme. Purification, crystallization, and preliminary crystallographic studies of photosystem II from a thermophilic cyanobacterium
    • Kuhl H., Kruip J., Seidler A., Krieger-Liszkay A., Bunker M., Bald D., Scheidig A.J., and Rogner M. Towards structural determination of the water-splitting enzyme. Purification, crystallization, and preliminary crystallographic studies of photosystem II from a thermophilic cyanobacterium. J. Biol. Chem. 275 (2000) 20652-20659
    • (2000) J. Biol. Chem. , vol.275 , pp. 20652-20659
    • Kuhl, H.1    Kruip, J.2    Seidler, A.3    Krieger-Liszkay, A.4    Bunker, M.5    Bald, D.6    Scheidig, A.J.7    Rogner, M.8
  • 37
    • 0034649367 scopus 로고    scopus 로고
    • EPR study of the oxygen evolving complex in His-tagged photosystem II from the cyanobacterium Synechococcus elongatus
    • Boussac A., Sugiura M., Inoue Y., and Rutherford A.W. EPR study of the oxygen evolving complex in His-tagged photosystem II from the cyanobacterium Synechococcus elongatus. Biochemistry 39 (2000) 13788-13799
    • (2000) Biochemistry , vol.39 , pp. 13788-13799
    • Boussac, A.1    Sugiura, M.2    Inoue, Y.3    Rutherford, A.W.4
  • 38
    • 48749143707 scopus 로고
    • The electrochemical domain of photosynthesis
    • Crofts A.R., and Wraight C.A. The electrochemical domain of photosynthesis. Biochim. Biophys. Acta 726 (1983) 149-185
    • (1983) Biochim. Biophys. Acta , vol.726 , pp. 149-185
    • Crofts, A.R.1    Wraight, C.A.2
  • 41
    • 0033567177 scopus 로고    scopus 로고
    • Herbicide resistance and supersensitivity in photosystem II
    • Oettmeier W. Herbicide resistance and supersensitivity in photosystem II. Cell. Mol. Life Sci. 55 (1999) 1255-1277
    • (1999) Cell. Mol. Life Sci. , vol.55 , pp. 1255-1277
    • Oettmeier, W.1
  • 42
    • 0026604580 scopus 로고
    • Reversible and irreversible intermediates during photoinhibition of photosystem II: stable reduced QA species promote chlorophyll triplet formation
    • Vass I., Styring S., Hundal T., Koivuniemi A., Aro E., and Andersson B. Reversible and irreversible intermediates during photoinhibition of photosystem II: stable reduced QA species promote chlorophyll triplet formation. Proc. Natl. Acad. Sci. U.S.A. 89 (1992) 1408-1412
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 1408-1412
    • Vass, I.1    Styring, S.2    Hundal, T.3    Koivuniemi, A.4    Aro, E.5    Andersson, B.6
  • 43
    • 33644939406 scopus 로고    scopus 로고
    • Herbicide binding and thermal stability of photosystem II isolated from Thermosynechococcus elongatus
    • Zimmermann K., Heck M., Frank J., Kern J., Vass I., and Zouni A. Herbicide binding and thermal stability of photosystem II isolated from Thermosynechococcus elongatus. Biochim. Biophys. Acta 1757 (2006) 106-114
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 106-114
    • Zimmermann, K.1    Heck, M.2    Frank, J.3    Kern, J.4    Vass, I.5    Zouni, A.6
  • 45
    • 0034719030 scopus 로고    scopus 로고
    • 2+-substitution on the reduction rates of Yz* in PSII membranes-evidence for concerted hydrogen-atom transfer in oxygen evolution
    • 2+-substitution on the reduction rates of Yz* in PSII membranes-evidence for concerted hydrogen-atom transfer in oxygen evolution. Biochemistry 39 (2000) 16220-16229
    • (2000) Biochemistry , vol.39 , pp. 16220-16229
    • Westphal, K.L.1    Lydakis-Simantiris, N.2    Cukier, R.I.3    Babcock, G.T.4
  • 46
    • 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
    • Strickler M.A., Walker L.M., Hillier W., and Debus R.J. 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
  • 47
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.