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Volumn 1607, Issue 1, 2003, Pages 53-63

Acquisition of photosynthetic capacity by a reaction centre that lacks the QA ubiquinone; possible insights into the evolution of reaction centres?

Author keywords

Reaction centre; Rhodobacter sphaeroides; Ubiquinone

Indexed keywords

ALANINE; BACTERIOPHEOPHYTIN; CYSTEINE; GLYCINE; POLYPEPTIDE; TRYPTOPHAN; UBIQUINONE;

EID: 0141817939     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2003.08.008     Document Type: Article
Times cited : (13)

References (55)
  • 2
    • 0035927420 scopus 로고    scopus 로고
    • Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution
    • Jordan P., Fromme P., Witt H.T., Klukas O., Saenger W., Krauss N. Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution. Nature. 411:2001;909-917.
    • (2001) Nature , vol.411 , pp. 909-917
    • Jordan, P.1    Fromme, P.2    Witt, H.T.3    Klukas, O.4    Saenger, W.5    Krauss, N.6
  • 3
    • 0033053334 scopus 로고    scopus 로고
    • Revealing the structure of the oxygen-evolving core dimer of Photosystem-II by electron crystallography
    • Hankamer B., Morris E.P., Barber J. Revealing the structure of the oxygen-evolving core dimer of Photosystem-II by electron crystallography. Nat. Struct. Biol. 6:1999;560-564.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 560-564
    • Hankamer, B.1    Morris, E.P.2    Barber, J.3
  • 4
    • 0033989509 scopus 로고    scopus 로고
    • 3D map of the plant Photosystem-II supercomplex obtained by cryoelectron microscopy and single particle analysis
    • Nield J., Orlova E.V., Morris E.P., Gowen B., van Heel M., Barber J. 3D map of the plant Photosystem-II supercomplex obtained by cryoelectron microscopy and single particle analysis. Nat. Struct. Biol. 7:2000;44-47.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 44-47
    • Nield, J.1    Orlova, E.V.2    Morris, E.P.3    Gowen, B.4    Van Heel, M.5    Barber, J.6
  • 5
    • 0034610351 scopus 로고    scopus 로고
    • Crystallization and the crystal properties of the oxygen-evolving photosystem II from Synechococcus vulcanus
    • Shen J.-R., Kamiya N. Crystallization and the crystal properties of the oxygen-evolving photosystem II from Synechococcus vulcanus. Biochemistry. 39:2000;14739-14744.
    • (2000) Biochemistry , vol.39 , pp. 14739-14744
    • Shen, J.-R.1    Kamiya, N.2
  • 7
    • 0037422557 scopus 로고    scopus 로고
    • Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7-angstrom resolution
    • Kamiya N., Shen J.-R. Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7-angstrom resolution. Proc. Natl. Acad. Sci. U. S. A. 100:2003;98-103.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 98-103
    • Kamiya, N.1    Shen, J.-R.2
  • 8
    • 45949128393 scopus 로고
    • Photosynthetic reaction centers - A common link
    • Barber J. Photosynthetic reaction centers - a common link. Trends Biochem. Sci. 12:1987;321-326.
    • (1987) Trends Biochem. Sci. , vol.12 , pp. 321-326
    • Barber, J.1
  • 9
    • 0043145962 scopus 로고
    • Relevance of the photosynthetic reaction center from purple bacteria to the structure of Photosystem-II
    • Michel H., Deisenhofer J. Relevance of the photosynthetic reaction center from purple bacteria to the structure of Photosystem-II. Biochemistry. 27:1988;1-7.
    • (1988) Biochemistry , vol.27 , pp. 1-7
    • Michel, H.1    Deisenhofer, J.2
  • 10
    • 0025885119 scopus 로고
    • Photosynthetic reaction centres: Variations on a common structural theme
    • Nitschke W., Rutherford A.W. Photosynthetic reaction centres: variations on a common structural theme. Trends Biochem. Sci. 16:1991;241-245.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 241-245
    • Nitschke, W.1    Rutherford, A.W.2
  • 11
    • 0027105895 scopus 로고
    • Origin and early evolution of photosynthesis
    • Blankenship R.E. Origin and early evolution of photosynthesis. Photosynth. Res. 33:1992;91-111.
    • (1992) Photosynth. Res. , vol.33 , pp. 91-111
    • Blankenship, R.E.1
  • 12
    • 0030592175 scopus 로고    scopus 로고
    • Structure of Photosystem-I at 4.5 Å resolution: A short review including evolutionary aspects
    • Fromme P., Witt H.T., Schubert W.D., Klukas O., Saenger W., Krauss N. Structure of Photosystem-I at 4.5 Å resolution: a short review including evolutionary aspects. Biochim. Biophys. Acta. 1275:1996;76-83.
    • (1996) Biochim. Biophys. Acta , vol.1275 , pp. 76-83
    • Fromme, P.1    Witt, H.T.2    Schubert, W.D.3    Klukas, O.4    Saenger, W.5    Krauss, N.6
  • 13
    • 0032504023 scopus 로고    scopus 로고
    • A common ancestor for oxygenic and anoxygenic photosynthetic systems: A comparison based on the structural model of Photosystem-I
    • Schubert W.D., Klukas O., Saenger W., Witt H.T., Fromme P., Krauss N. A common ancestor for oxygenic and anoxygenic photosynthetic systems: a comparison based on the structural model of Photosystem-I. J. Mol. Biol. 280:1998;297-314.
    • (1998) J. Mol. Biol. , vol.280 , pp. 297-314
    • Schubert, W.D.1    Klukas, O.2    Saenger, W.3    Witt, H.T.4    Fromme, P.5    Krauss, N.6
  • 14
    • 0036469776 scopus 로고    scopus 로고
    • Reaction centres: Structure and mechanism in biological solar power
    • Heathcote P., Fyfe P.K., Jones M.R. Reaction centres: structure and mechanism in biological solar power. Trends Biochem. Sci. 27:2002;79-87.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 79-87
    • Heathcote, P.1    Fyfe, P.K.2    Jones, M.R.3
  • 15
    • 0031208887 scopus 로고    scopus 로고
    • Photophysics of photosynthesis: Structure and spectroscopy of reaction centres of purple bacteria
    • Hoff A.J., Deisenhofer J. Photophysics of photosynthesis: structure and spectroscopy of reaction centres of purple bacteria. Phys. Rep. 287:1997;1-247.
    • (1997) Phys. Rep. , vol.287 , pp. 1-247
    • Hoff, A.J.1    Deisenhofer, J.2
  • 16
    • 0034577649 scopus 로고    scopus 로고
    • Reaction Centres of Purple Bacteria
    • N.S. Scrutton, A. Holzenburg (Eds.), Kluwer Academic/Plenum Publishers, New York, USA
    • M.E. van Brederode, M.R. Jones, Reaction Centres of Purple Bacteria, in: N.S. Scrutton, A. Holzenburg (Eds.), Enzyme-Catalysed Electron and Radical Transfer, Kluwer Academic/Plenum Publishers, New York, USA, 2000, pp. 621-676.
    • (2000) Enzyme-Catalysed Electron and Radical Transfer , pp. 621-676
    • Van Brederode, M.E.1    Jones, M.R.2
  • 17
    • 0018787864 scopus 로고
    • Ubiquinone in Rhodopseudomonas sphaeroides. Some thermodynamic properties
    • Takamiya K.-I., Dutton P.L. Ubiquinone in Rhodopseudomonas sphaeroides. Some thermodynamic properties. Biochim. Biophys. Acta. 546:1979;1-16.
    • (1979) Biochim. Biophys. Acta , vol.546 , pp. 1-16
    • Takamiya, K.-I.1    Dutton, P.L.2
  • 19
    • 0034642179 scopus 로고    scopus 로고
    • Ubiquinone binding, ubiquinone exclusion, and detailed cofactor conformation in a mutant bacterial reaction center
    • McAuley K.E., Fyfe P.K., Ridge J.P., Cogdell R.J., Isaacs N.W., Jones M.R. Ubiquinone binding, ubiquinone exclusion, and detailed cofactor conformation in a mutant bacterial reaction center. Biochemistry. 39:2000;15032-15043.
    • (2000) Biochemistry , vol.39 , pp. 15032-15043
    • McAuley, K.E.1    Fyfe, P.K.2    Ridge, J.P.3    Cogdell, R.J.4    Isaacs, N.W.5    Jones, M.R.6
  • 20
    • 0026586530 scopus 로고
    • Construction of mutants of Rhodobacter sphaeroides lacking one or more pigment-protein complexes and complementation with reaction-centre, LH1, and LH2 genes
    • Jones M.R., Fowler G.J.S., Gibson L.C.D., Grief G.G., Olsen J.D., Crielaard W., Hunter C.N. Construction of mutants of Rhodobacter sphaeroides lacking one or more pigment-protein complexes and complementation with reaction-centre, LH1, and LH2 genes. Mol. Microbiol. 6:1992;1173-1184.
    • (1992) Mol. Microbiol. , vol.6 , pp. 1173-1184
    • Jones, M.R.1    Fowler, G.J.S.2    Gibson, L.C.D.3    Grief, G.G.4    Olsen, J.D.5    Crielaard, W.6    Hunter, C.N.7
  • 21
    • 0028331145 scopus 로고
    • Site-specific mutagenesis of the reaction centre from Rhodobacter sphaeroides studied by Fourier transform Raman spectroscopy: Mutations at tyrosine M210 do not affect the electronic structure of the primary donor
    • Jones M.R., Heer-Dawson M., Mattioli T.A., Hunter C.N., Robert B. Site-specific mutagenesis of the reaction centre from Rhodobacter sphaeroides studied by Fourier transform Raman spectroscopy: mutations at tyrosine M210 do not affect the electronic structure of the primary donor. FEBS Lett. 339:1994;18-24.
    • (1994) FEBS Lett. , vol.339 , pp. 18-24
    • Jones, M.R.1    Heer-Dawson, M.2    Mattioli, T.A.3    Hunter, C.N.4    Robert, B.5
  • 22
    • 0002945129 scopus 로고
    • Media for anaerobic growth of photosynthetic bacteria
    • H. Gest, A. San Pietro, & L.P. Vernon. Yellow Springs, OH: Antioch Press
    • Bose S.K. Media for anaerobic growth of photosynthetic bacteria. Gest H., San Pietro A., Vernon L.P. Bacterial Photosynthesis. 1963;501-510 Antioch Press, Yellow Springs, OH.
    • (1963) Bacterial Photosynthesis , pp. 501-510
    • Bose, S.K.1
  • 23
    • 0015878333 scopus 로고
    • Pigment content and molar extinction coefficients of photochemical reaction centers from Rhodopseudomonas spheroides
    • Straley S.C., Parson W.W., Mauzerall D.C., Clayton R.K. Pigment content and molar extinction coefficients of photochemical reaction centers from Rhodopseudomonas spheroides. Biochim. Biophys. Acta. 305:1973;597-609.
    • (1973) Biochim. Biophys. Acta , vol.305 , pp. 597-609
    • Straley, S.C.1    Parson, W.W.2    Mauzerall, D.C.3    Clayton, R.K.4
  • 24
    • 0034300084 scopus 로고    scopus 로고
    • Identifying the pathways of energy transfer between carotenoids and chlorophylls in LHCII and CP29. A multicolor, femtosecond pump-probe study
    • Gradinaru C.C., van Stokkum I.H.M., Pascal A.A., van Grondelle R., van Amerongen H. Identifying the pathways of energy transfer between carotenoids and chlorophylls in LHCII and CP29. A multicolor, femtosecond pump-probe study. J. Phys. Chem., B. 104:2000;9330-9342.
    • (2000) J. Phys. Chem., B , vol.104 , pp. 9330-9342
    • Gradinaru, C.C.1    Van Stokkum, I.H.M.2    Pascal, A.A.3    Van Grondelle, R.4    Van Amerongen, H.5
  • 25
    • 0001302210 scopus 로고
    • Conformational dynamics of flexibly and semirigidly bridged electron donor-acceptor systems as revealed by spectrotemporal parametrization of fluorescence
    • van Stokkum I.H.M., Scherer T., Brouwer A.M., Verhoeven J.W. Conformational dynamics of flexibly and semirigidly bridged electron donor-acceptor systems as revealed by spectrotemporal parametrization of fluorescence. J. Phys. Chem. 98:1994;852-866.
    • (1994) J. Phys. Chem. , vol.98 , pp. 852-866
    • Van Stokkum, I.H.M.1    Scherer, T.2    Brouwer, A.M.3    Verhoeven, J.W.4
  • 26
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4 The CCP4 suite: programs for protein crystallography. Acta Crystallogr., D. 50:1994;760-763.
    • (1994) Acta Crystallogr., D , vol.50 , pp. 760-763
  • 27
    • 0002705842 scopus 로고
    • XtalView: A visual protein crystallographic software system for XII/Xview
    • McRee D.E. XtalView: a visual protein crystallographic software system for XII/Xview. J. Mol. Graph. 10:1992;44-46.
    • (1992) J. Mol. Graph. , vol.10 , pp. 44-46
    • McRee, D.E.1
  • 28
    • 0021294853 scopus 로고
    • Herbicide-quinone competition in the acceptor complex of photosynthetic reaction centers from Rhodopseudomonas sphaeroides: A bacterial model for PS-II-herbicide activity in plants
    • Stein R.R., Castellvi A.L., Bogacz J.P., Wraight C.A. Herbicide-quinone competition in the acceptor complex of photosynthetic reaction centers from Rhodopseudomonas sphaeroides: a bacterial model for PS-II-herbicide activity in plants. J. Cell. Biochem. 24:1984;243-259.
    • (1984) J. Cell. Biochem. , vol.24 , pp. 243-259
    • Stein, R.R.1    Castellvi, A.L.2    Bogacz, J.P.3    Wraight, C.A.4
  • 29
    • 0016616067 scopus 로고
    • The primary photochemical reaction of bacterial photosynthesis
    • Parson W.W., Cogdell R.J. The primary photochemical reaction of bacterial photosynthesis. Biochim. Biophys. Acta. 416:1975;105-149.
    • (1975) Biochim. Biophys. Acta , vol.416 , pp. 105-149
    • Parson, W.W.1    Cogdell, R.J.2
  • 30
    • 0016852791 scopus 로고
    • Excited states of photosynthetic reaction centers at low redox potentials
    • Parson W.W., Clayton R.K., Cogdell R.J. Excited states of photosynthetic reaction centers at low redox potentials. Biochim. Biophys. Acta. 387:1975;265-278.
    • (1975) Biochim. Biophys. Acta , vol.387 , pp. 265-278
    • Parson, W.W.1    Clayton, R.K.2    Cogdell, R.J.3
  • 32
    • 0032492681 scopus 로고    scopus 로고
    • Structural studies of wild type and mutant reaction centres from an antenna-deficient strain of Rhodobacter sphaeroides: Monitoring the optical properties of the complex from cell to crystal
    • McAuley-Hecht K.E., Fyfe P.K., Ridge J.P., Prince S.M., Hunter C.N., Isaacs N.W., Cogdell R.J., Jones M.R. Structural studies of wild type and mutant reaction centres from an antenna-deficient strain of Rhodobacter sphaeroides: monitoring the optical properties of the complex from cell to crystal. Biochemistry. 37:1998;4740-4750.
    • (1998) Biochemistry , vol.37 , pp. 4740-4750
    • McAuley-Hecht, K.E.1    Fyfe, P.K.2    Ridge, J.P.3    Prince, S.M.4    Hunter, C.N.5    Isaacs, N.W.6    Cogdell, R.J.7    Jones, M.R.8
  • 36
    • 0027717613 scopus 로고
    • Spectroscopic analysis of genetically-modified photosynthetic reaction centers
    • Coleman W.J., Youvan D.C. Spectroscopic analysis of genetically-modified photosynthetic reaction centers. Nature. 366:1993;517-518.
    • (1993) Nature , vol.366 , pp. 517-518
    • Coleman, W.J.1    Youvan, D.C.2
  • 38
    • 0027405698 scopus 로고
    • Pathway of proton-transfer in bacterial reaction centers - 2nd-site mutation Asn-M44→Asp restores electron and proton-transfer in reaction centers from the photosynthetically deficient Asp-L213→Asn mutant of Rhodobacter sphaeroides
    • Rongey S.H., Paddock M.L., Feher G., Okamura M.Y. Pathway of proton-transfer in bacterial reaction centers - 2nd-site mutation Asn-M44→Asp restores electron and proton-transfer in reaction centers from the photosynthetically deficient Asp-L213→Asn mutant of Rhodobacter sphaeroides. Proc. Natl. Acad. Sci. U. S. A. 90:1993;1325-1329.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 1325-1329
    • Rongey, S.H.1    Paddock, M.L.2    Feher, G.3    Okamura, M.Y.4
  • 39
    • 0029090142 scopus 로고
    • Proline in a transmembrane helix compensates for cavities in the photosynthetic reaction-center
    • Schiffer M., Ainsworth C.F., Deng Y.-L., Johnson G., Pascoe F.H., Hanson D.K. Proline in a transmembrane helix compensates for cavities in the photosynthetic reaction-center. J. Mol. Biol. 252:1995;472-482.
    • (1995) J. Mol. Biol. , vol.252 , pp. 472-482
    • Schiffer, M.1    Ainsworth, C.F.2    Deng, Y.-L.3    Johnson, G.4    Pascoe, F.H.5    Hanson, D.K.6
  • 41
    • 0031828333 scopus 로고    scopus 로고
    • Symmetry-related mutants in the quinone binding sites of the bacterial reaction center - The effects of changes in charge distribution
    • Hanson D.K., Schiffer M. Symmetry-related mutants in the quinone binding sites of the bacterial reaction center - the effects of changes in charge distribution. Photosynth. Res. 55:1998;275-280.
    • (1998) Photosynth. Res. , vol.55 , pp. 275-280
    • Hanson, D.K.1    Schiffer, M.2
  • 43
    • 0033524437 scopus 로고    scopus 로고
    • Mutations in the environment of the primary quinone facilitate proton delivery to the secondary quinone in bacterial photosynthetic reaction centers
    • Valerio-Lepiniec M., Miksovska J., Schiffer M., Hanson D.K., Sebban P. Mutations in the environment of the primary quinone facilitate proton delivery to the secondary quinone in bacterial photosynthetic reaction centers. Biochemistry. 38:1999;390-398.
    • (1999) Biochemistry , vol.38 , pp. 390-398
    • Valerio-Lepiniec, M.1    Miksovska, J.2    Schiffer, M.3    Hanson, D.K.4    Sebban, P.5
  • 45
    • 0002460215 scopus 로고
    • The evolution of chlorophylls
    • H. Scheer. Boston: CRC Press
    • Larkum A.W.D. The evolution of chlorophylls. Scheer H. Chlorophylls. 1991;367-383 CRC Press, Boston.
    • (1991) Chlorophylls , pp. 367-383
    • Larkum, A.W.D.1
  • 46
    • 0030848989 scopus 로고    scopus 로고
    • On the origin of photosynthesis as inferred from sequence analysis
    • Mulkidjanian A.Y., Junge W. On the origin of photosynthesis as inferred from sequence analysis. Photosynth. Res. 51:1997;27-42.
    • (1997) Photosynth. Res. , vol.51 , pp. 27-42
    • Mulkidjanian, A.Y.1    Junge, W.2
  • 47
    • 0035923418 scopus 로고    scopus 로고
    • Blue light drives B-side electron transfer in bacterial photosynthetic reaction centers
    • Lin S., Katilius E., Haffa A.L.M., Taguchi A.K.W., Woodbury N.W. Blue light drives B-side electron transfer in bacterial photosynthetic reaction centers. Biochemistry. 40:2001;13767-13773.
    • (2001) Biochemistry , vol.40 , pp. 13767-13773
    • Lin, S.1    Katilius, E.2    Haffa, A.L.M.3    Taguchi, A.K.W.4    Woodbury, N.W.5
  • 49
    • 0028131660 scopus 로고
    • Evolution of photosynthetic reaction centers and light-harvesting chlorophyll proteins
    • Meyer T.E. Evolution of photosynthetic reaction centers and light-harvesting chlorophyll proteins. Biosystems. 33:1994;167-175.
    • (1994) Biosystems , vol.33 , pp. 167-175
    • Meyer, T.E.1
  • 50
    • 0036414764 scopus 로고    scopus 로고
    • A cytochrome b origin of photosynthetic reaction centers: An evolutionary link between respiration and photosynthesis
    • Xiong J., Bauer C.E. A cytochrome b origin of photosynthetic reaction centers: an evolutionary link between respiration and photosynthesis. J. Mol. Biol. 322:2002;1025-1037.
    • (2002) J. Mol. Biol. , vol.322 , pp. 1025-1037
    • Xiong, J.1    Bauer, C.E.2
  • 51
    • 0035969974 scopus 로고    scopus 로고
    • Protein control of the redox potential of the primary quinone acceptor in reaction centers from Rhodobacter sphaeroides
    • Takahashi E., Wells T.A., Wraight C.A. Protein control of the redox potential of the primary quinone acceptor in reaction centers from Rhodobacter sphaeroides. Biochemistry. 40:2001;1020-1028.
    • (2001) Biochemistry , vol.40 , pp. 1020-1028
    • Takahashi, E.1    Wells, T.A.2    Wraight, C.A.3
  • 52
    • 0037446648 scopus 로고    scopus 로고
    • A) binding site of bacterial photosynthetic reaction centers: Mutations at residue M265 probed by FTIR spectroscopy
    • A) binding site of bacterial photosynthetic reaction centers: mutations at residue M265 probed by FTIR spectroscopy. Biochemistry. 42:2003;4064-4074.
    • (2003) Biochemistry , vol.42 , pp. 4064-4074
    • Wells, T.A.1    Takahashi, E.2    Wraight, C.A.3
  • 53
    • 0026244229 scopus 로고
    • MOLSCRIPT - A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT - a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:1991;946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 54
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt E.A., Bacon D.J. Raster3D: photorealistic molecular graphics. Methods Enzymol. 277:1997;505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 55
    • 84893482610 scopus 로고
    • A solution for the best rotation to relate two sets of vectors
    • Kabsch W. A solution for the best rotation to relate two sets of vectors. Acta Crystallogr., A. 32:1976;922-923.
    • (1976) Acta Crystallogr., A , vol.32 , pp. 922-923
    • Kabsch, W.1


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