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Volumn 86, Issue 3, 2004, Pages 1807-1812

Structural Studies of the Manganese Stabilizing Subunit in Photosystem II

Author keywords

[No Author keywords available]

Indexed keywords

MANGANESE STABILIZING PROTEIN; PROTEIN; UNCLASSIFIED DRUG;

EID: 1542375179     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(04)74247-2     Document Type: Article
Times cited : (16)

References (38)
  • 1
    • 0028907510 scopus 로고
    • A quantitative secondary structure analysis of the 33 kDa extrinsic polypeptide of photosystem II by FTIR spectroscopy
    • Ahmed, A., H. A. Tajmir-Riahi, and R. Carpentier. 1995. A quantitative secondary structure analysis of the 33 kDa extrinsic polypeptide of photosystem II by FTIR spectroscopy. FEBS Lett. 363:65-68.
    • (1995) FEBS Lett. , vol.363 , pp. 65-68
    • Ahmed, A.1    Tajmir-Riahi, H.A.2    Carpentier, R.3
  • 2
    • 0034681371 scopus 로고    scopus 로고
    • Probing the primary structure of photosystem II with amines and phenylhydrazine
    • Anderson, L. B., A. J. A. Ouellette, and B. A. Barry. 2000. Probing the primary structure of photosystem II with amines and phenylhydrazine. J. Biol. Chem. 275:4920-4927.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4920-4927
    • Anderson, L.B.1    Ouellette, A.J.A.2    Barry, B.A.3
  • 3
    • 0000075484 scopus 로고
    • A highly resolved, oxygen-evolving Photosystem II preparation from spinach thylakoid membranes
    • Berthold, D. A., G. T. Babcock, and C. F. Yocum. 1981. A highly resolved, oxygen-evolving Photosystem II preparation from spinach thylakoid membranes. FEBS Lett. 134:231-234.
    • (1981) FEBS Lett. , vol.134 , pp. 231-234
    • Berthold, D.A.1    Babcock, G.T.2    Yocum, C.F.3
  • 4
    • 0028518814 scopus 로고
    • Reconstitution of the spinach oxygen-evolving complex with recombinant Arabidopsis manganese-stabilitzing protein
    • Betts, S. D., T. M. Hachigian, E. Pichersky, and C. F. Yocum. 1994. Reconstitution of the spinach oxygen-evolving complex with recombinant Arabidopsis manganese-stabilitzing protein. Plant Mol. Biol. 26:117-130.
    • (1994) Plant Mol. Biol. , vol.26 , pp. 117-130
    • Betts, S.D.1    Hachigian, T.M.2    Pichersky, E.3    Yocum, C.F.4
  • 5
    • 0034711009 scopus 로고    scopus 로고
    • Conformational changes in Photosystem II supercomplexes upon removal of extrinsic subunits
    • Boekema, E. J., J. F. L. van Breemen, H. van Roon, and J. P. Dekker. 2000. Conformational changes in Photosystem II supercomplexes upon removal of extrinsic subunits. Biochemistry. 39:12907-12915.
    • (2000) Biochemistry , vol.39 , pp. 12907-12915
    • Boekema, E.J.1    Van Breemen, J.F.L.2    Van Roon, H.3    Dekker, J.P.4
  • 6
    • 0031853225 scopus 로고    scopus 로고
    • The structure and function of the 33 kDa extrinsic protein of Photosystem II: A critical assessment
    • Bricker, T., and L. Frankel. 1998. The structure and function of the 33 kDa extrinsic protein of Photosystem II: a critical assessment. Photosynth, Res. 56:157-173.
    • (1998) Photosynth. Res. , vol.56 , pp. 157-173
    • Bricker, T.1    Frankel, L.2
  • 7
    • 0000561603 scopus 로고    scopus 로고
    • Oxygen evolution
    • D. R. Ort and C. F. Yocum, editors. Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Britt, R. D. 1996. Oxygen evolution. In Oxygenic Photosynthesis: The Light Reactions, Vol. 4. D. R. Ort and C. F. Yocum, editors. Kluwer Academic Publishers, Dordrecht, The Netherlands. 137-164.
    • (1996) Oxygenic Photosynthesis: The Light Reactions , vol.4 , pp. 137-164
    • Britt, R.D.1
  • 8
    • 0032703843 scopus 로고    scopus 로고
    • Structural predictions on the 33 kDa extrinsic protein associated to the oxygen evolving complex of photosynthetic organisms
    • De Las Rivas, J., and P. Heredia. 1999. Structural predictions on the 33 kDa extrinsic protein associated to the oxygen evolving complex of photosynthetic organisms. Photosynth. Res. 61:11-21.
    • (1999) Photosynth. Res. , vol.61 , pp. 11-21
    • De Las Rivas, J.1    Heredia, P.2
  • 9
    • 0032549019 scopus 로고    scopus 로고
    • Intramolecular cross-linking of the extrinsic 33-kDa protein leads to loss of oxygen evolution but not its ability of binding to Photosystem II and stabilization of the manganese cluster
    • Enami, I., M. Kamo, H. Ohta, S. Takahashi, T. Miura, M. Kusayanagi, S. Tanabe, A. Kamei, A. Motoki, M. Hirano, T. Tomo, and K. Satoh. 1998. Intramolecular cross-linking of the extrinsic 33-kDa protein leads to loss of oxygen evolution but not its ability of binding to Photosystem II and stabilization of the manganese cluster. J. Biol. Chem. 273:4629-4634.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4629-4634
    • Enami, I.1    Kamo, M.2    Ohta, H.3    Takahashi, S.4    Miura, T.5    Kusayanagi, M.6    Tanabe, S.7    Kamei, A.8    Motoki, A.9    Hirano, M.10    Tomo, T.11    Satoh, K.12
  • 10
    • 0030794237 scopus 로고    scopus 로고
    • Structural analysis of photosystem II: Comparative study of cyanobacterial and higher plant photosystem II complexes
    • Hasler, L., D. Ghanotakis, B. Fedtke, A. Spyridaki, M. Miller, S. A. Müller, A. Engel, and G. Tsiotis. 1997. Structural analysis of photosystem II: comparative study of cyanobacterial and higher plant photosystem II complexes. J. Struct. Biol. 119:273-283.
    • (1997) J. Struct. Biol. , vol.119 , pp. 273-283
    • Hasler, L.1    Ghanotakis, D.2    Fedtke, B.3    Spyridaki, A.4    Miller, M.5    Müller, S.A.6    Engel, A.7    Tsiotis, G.8
  • 11
    • 0141885292 scopus 로고    scopus 로고
    • Calcium-dependent conformational change and thermal stability of the isolated PsbO protein detected by FT-IR spectroscopy
    • Heredia, P., and J. De Las Rivas. 2003. Calcium-dependent conformational change and thermal stability of the isolated PsbO protein detected by FT-IR spectroscopy. Biochemistry. 42:11831-11838.
    • (2003) Biochemistry , vol.42 , pp. 11831-11838
    • Heredia, P.1    De Las Rivas, J.2
  • 12
    • 0030115165 scopus 로고    scopus 로고
    • Photosystem II: Mapping the location of the oxygen evolution-enhancing subunit by electron microscopy
    • Holzenburg, A., T. D. Flint, F. H. Shepherd, and R. C. Ford. 1996. Photosystem II: mapping the location of the oxygen evolution-enhancing subunit by electron microscopy. Micron. 27:121-127.
    • (1996) Micron , vol.27 , pp. 121-127
    • Holzenburg, A.1    Flint, T.D.2    Shepherd, F.H.3    Ford, R.C.4
  • 13
    • 0027576642 scopus 로고
    • X-ray powder diffraction analysis of silver behenate, a possible low-angle diffraction standard
    • Huang, T. C., H, Toraya, T. N. Blanton, and Y. Wu. 1993. X-ray powder diffraction analysis of silver behenate, a possible low-angle diffraction standard. J. Appl. Crystallogr. 26:180-184.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 180-184
    • Huang, T.C.1    Toraya, H.2    Blanton, T.N.3    Wu, Y.4
  • 14
    • 0032554633 scopus 로고    scopus 로고
    • Conformational changes in the extrinsic manganese-stabilizing protein can occur upon binding to the photosystem II reaction center: An isotope editing and FT-IR study
    • Hutchison, R. S., S. D. Betts, C. F. Yocum, and B. A. Barry. 1998. Conformational changes in the extrinsic manganese-stabilizing protein can occur upon binding to the photosystem II reaction center: an isotope editing and FT-IR study. Biochemistry. 37:5643-5653.
    • (1998) Biochemistry , vol.37 , pp. 5643-5653
    • Hutchison, R.S.1    Betts, S.D.2    Yocum, C.F.3    Barry, B.A.4
  • 15
    • 0037422557 scopus 로고    scopus 로고
    • Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7 A resolution
    • Kamiya, N., and J.-R. Shen. 2003. Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7 A resolution. Proc. Natl. Acad. Sci. USA. 100:98-103.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 98-103
    • Kamiya, N.1    Shen, J.-R.2
  • 16
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
    • C. B. Anfinsen, J. T. Edsall, and F. M. Richards, editors. Academic Press, New York
    • Krimm, S., and J. Bandekar. 1986. Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. In Advances in Protein Chemistry, Vol. 38. C. B. Anfinsen, J. T. Edsall, and F. M. Richards, editors. Academic Press, New York. 181-364.
    • (1986) Advances in Protein Chemistry , vol.38 , pp. 181-364
    • Krimm, S.1    Bandekar, J.2
  • 17
    • 0001628742 scopus 로고
    • Partial degradation of the 18-kDa protein of the photosynthetic oxgyen-evolving complex: A study of a binding site
    • Kuwabara, T., T. Murata, M. Miyao, and N. Murata. 1986. Partial degradation of the 18-kDa protein of the photosynthetic oxgyen-evolving complex: a study of a binding site. Biochim. Biophys. Acta. 850:146-155.
    • (1986) Biochim. Biophys. Acta , vol.850 , pp. 146-155
    • Kuwabara, T.1    Murata, T.2    Miyao, M.3    Murata, N.4
  • 18
    • 0033524432 scopus 로고    scopus 로고
    • Manganese stabilizing protein of photosystem II is a thermostable, natively unfolded protein
    • Lydakis-Simantiris, N., R. S, Hutchison, S. D. Betts, B. A. Barry, and C. F. Yocum. 1999. Manganese stabilizing protein of photosystem II is a thermostable, natively unfolded protein. Biochemistry. 38:404-414.
    • (1999) Biochemistry , vol.38 , pp. 404-414
    • Lydakis-Simantiris, N.1    Hutchison, R.S.2    Betts, S.D.3    Barry, B.A.4    Yocum, C.F.5
  • 19
    • 0039243690 scopus 로고
    • Partial reconstitution of the photosynthetic oxygen evolution system by rebinding of the 33-kDa polypeptide
    • Miyao, M., and N. Murata. 1983. Partial reconstitution of the photosynthetic oxygen evolution system by rebinding of the 33-kDa polypeptide. FEBS Lett. 164:375-378.
    • (1983) FEBS Lett. , vol.164 , pp. 375-378
    • Miyao, M.1    Murata, N.2
  • 20
    • 0037177852 scopus 로고    scopus 로고
    • Three-dimensional electron cryo-microscopy study of the extrinsic domain of the oxygen evolving complex of spinach
    • Nield, J., M. Balsera, J. De Las Rivas, and J. Barber. 2002. Three-dimensional electron cryo-microscopy study of the extrinsic domain of the oxygen evolving complex of spinach. J. Biol. Chem. 277: 15006-15012.
    • (2002) J. Biol. Chem. , vol.277 , pp. 15006-15012
    • Nield, J.1    Balsera, M.2    De Las Rivas, J.3    Barber, J.4
  • 21
    • 0002181672 scopus 로고
    • Complete amino acid sequence of 33 kDa protein isolated from spinach photosystem II particles
    • Oh-oka, H., S. Tanaka, K. Wada, T. Kuwabara, and N. Murata. 1986. Complete amino acid sequence of 33 kDa protein isolated from spinach photosystem II particles. FEBS Lett. 197:63-66.
    • (1986) FEBS Lett. , vol.197 , pp. 63-66
    • Oh-Oka, H.1    Tanaka, S.2    Wada, K.3    Kuwabara, T.4    Murata, N.5
  • 22
    • 48749146415 scopus 로고
    • 2-evolving PSII particles by divalent salt-washing
    • 2-evolving PSII particles by divalent salt-washing. FEBS Lett. 164:252-260.
    • (1983) FEBS Lett. , vol.164 , pp. 252-260
    • Ono, T.1    Inoue, Y.2
  • 23
    • 0032478207 scopus 로고    scopus 로고
    • Amine binding and oxidation at the catalytic site of photosynthetic water oxidation
    • Ouellette, A. J. A., L. B. Anderson, and B. A. Barry. 1998. Amine binding and oxidation at the catalytic site of photosynthetic water oxidation. Proc. Natl. Acad. Sci. USA. 95:2204-2209.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2204-2209
    • Ouellette, A.J.A.1    Anderson, L.B.2    Barry, B.A.3
  • 24
    • 0035576338 scopus 로고    scopus 로고
    • Threading structural model of the manganese-stabilizing protein PsbO reveals presence of two possible β-sandwich domains
    • Pazos, F., P. Heredia, A. Valencia, and J. De Las Rivas. 2001. Threading structural model of the manganese-stabilizing protein PsbO reveals presence of two possible β-sandwich domains. Proteins. 45:372-381.
    • (2001) Proteins , vol.45 , pp. 372-381
    • Pazos, F.1    Heredia, P.2    Valencia, A.3    De Las Rivas, J.4
  • 25
    • 0002579706 scopus 로고
    • Methods of polyacrylamide gel electrophoresis in the analysis and preparation of plant polypeptides
    • H. Edelman, R. B. Hallick, and N.-H. Chua, editors. Elsevier, Amsterdam, The Netherlands
    • Piccioni, R., G. Bellemare, and N. Chua. 1982. Methods of polyacrylamide gel electrophoresis in the analysis and preparation of plant polypeptides. In Methods in Chloroplast Molecular Biology. H. Edelman, R. B. Hallick, and N.-H. Chua, editors. Elsevier, Amsterdam, The Netherlands. 985-1014.
    • (1982) Methods in Chloroplast Molecular Biology , pp. 985-1014
    • Piccioni, R.1    Bellemare, G.2    Chua, N.3
  • 26
    • 0029966774 scopus 로고    scopus 로고
    • The extrinsic polypeptides of Photosystem II
    • Seidler, A. 1996. The extrinsic polypeptides of Photosystem II. Biochim. Biophys. Acta. 1277:35-60.
    • (1996) Biochim. Biophys. Acta , vol.1277 , pp. 35-60
    • Seidler, A.1
  • 27
    • 0033975097 scopus 로고    scopus 로고
    • Is the manganese stabilizing 33 kDa protein of photosystem II attaining a 'natively unfolded' or 'molten globule' structure in solution?
    • Shutova, T., K.-D. Irrgang, V. V. Klimov, and G. Renger. 2000. Is the manganese stabilizing 33 kDa protein of photosystem II attaining a 'natively unfolded' or 'molten globule' structure in solution? FEBS Lett. 467:137-140.
    • (2000) FEBS Lett. , vol.467 , pp. 137-140
    • Shutova, T.1    Irrgang, K.-D.2    Klimov, V.V.3    Renger, G.4
  • 28
    • 0030943887 scopus 로고    scopus 로고
    • Analysis of pH-induced structural changes of the isolated extrinsic 33 kilodalton protein of photosystem II
    • Shutova, T., K.-D. Irrgang, V. Shubin, V. V. Klimov, and G. Renger. 1997. Analysis of pH-induced structural changes of the isolated extrinsic 33 kilodalton protein of photosystem II. Biochemistry. 36:6350-6358.
    • (1997) Biochemistry , vol.36 , pp. 6350-6358
    • Shutova, T.1    Irrgang, K.-D.2    Shubin, V.3    Klimov, V.V.4    Renger, G.5
  • 29
    • 0027492164 scopus 로고
    • Determination of protein secondary structure by Fourier transform infrared spectroscopy: A critical assessment
    • Surewicz, W. K., H. A. Mantsch, and D. Chapman. 1993. Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment. Biochemistry. 32:389-394.
    • (1993) Biochemistry , vol.32 , pp. 389-394
    • Surewicz, W.K.1    Mantsch, H.A.2    Chapman, D.3
  • 30
    • 0037194924 scopus 로고    scopus 로고
    • Small-angle X-ray scattering studies of the manganese stabilizing subunit in photosystem II
    • Svensson, B., D. M. Tiede, and B. A. Barry. 2002. Small-angle X-ray scattering studies of the manganese stabilizing subunit in photosystem II. J. Phys. Chem. B. 106:8485-8488.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 8485-8488
    • Svensson, B.1    Tiede, D.M.2    Barry, B.A.3
  • 31
    • 0026244044 scopus 로고
    • GNOM - A program package for small angle scattering data processing
    • Svergun, D. I. 1991. GNOM - a program package for small angle scattering data processing. J. Appl. Crystallogr. 24:537-540.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 537-540
    • Svergun, D.I.1
  • 32
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun, D., C. Barberato, and M. H. J. Koch. 1995. CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallogr. 28:768-773.
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.J.3
  • 33
    • 0037188386 scopus 로고    scopus 로고
    • Protein conformations explored by difference high-angle solution X-ray scattering: Oxidation state and temperature dependent changes in cytochrome c
    • Tiede, D. M., R. Zhang, and S. Seifert. 2002. Protein conformations explored by difference high-angle solution X-ray scattering: oxidation state and temperature dependent changes in cytochrome c. Biochemistry. 41:6605-6614.
    • (2002) Biochemistry , vol.41 , pp. 6605-6614
    • Tiede, D.M.1    Zhang, R.2    Seifert, S.3
  • 35
    • 0028568020 scopus 로고
    • Secondary structure of the 33 kDa, extrinsic protein of photosystem II: A far-UV circular dichroism study
    • Xu, Q., J. Nelson, and T. M. Bricker. 1994. Secondary structure of the 33 kDa, extrinsic protein of photosystem II: a far-UV circular dichroism study. Biochim. Biophys. Acta. 1188:427-431.
    • (1994) Biochim. Biophys. Acta , vol.1188 , pp. 427-431
    • Xu, Q.1    Nelson, J.2    Bricker, T.M.3
  • 36
    • 0034505693 scopus 로고    scopus 로고
    • Probing protein fine structures by wide angle solution X-ray scattering
    • Zhang, R. T., P. Thiyagarajan, and D. M. Tiede. 2000. Probing protein fine structures by wide angle solution X-ray scattering. J. Appl. Crystallogr. 33:565-568.
    • (2000) J. Appl. Crystallogr. , vol.33 , pp. 565-568
    • Zhang, R.T.1    Thiyagarajan, P.2    Tiede, D.M.3
  • 37
    • 0035825682 scopus 로고    scopus 로고
    • Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution
    • Zouni, A., H.-T. Witt, J. Kern, P. Fromme, N. Krauss, W. Saenger, and P. Orth. 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
  • 38
    • 0032578473 scopus 로고    scopus 로고
    • Hydrodynamic studies on the manganese-stabilizing protein of Photosystem II
    • Zubrzycki, I. Z., L. K. Frankel, P. S. Russo, and T. M. Bricker. 1998. Hydrodynamic studies on the manganese-stabilizing protein of Photosystem II. Biochemistry. 37:13553-13558.
    • (1998) Biochemistry , vol.37 , pp. 13553-13558
    • Zubrzycki, I.Z.1    Frankel, L.K.2    Russo, P.S.3    Bricker, T.M.4


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