메뉴 건너뛰기




Volumn 12, Issue 4, 2004, Pages 703-715

X-ray structure determination of three mutants of the bacterial photosynthetic reaction centers from Rb. sphaeroides: Altered proton transfer pathways

Author keywords

[No Author keywords available]

Indexed keywords

1,4 BENZOQUINONE; CADMIUM; PROTON; WATER;

EID: 1842502604     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2004.03.001     Document Type: Article
Times cited : (38)

References (68)
  • 3
    • 0035807787 scopus 로고    scopus 로고
    • Identification of the proton pathway in bacterial reaction centers: Decrease of proton transfer rate by mutation of surface histidines at H126 and H128 and chemical rescue by imidazole identifies the initial proton donors
    • Ädelroth P., Paddock M.L., Tehrani A., Beatty J.T., Feher G., Okamura M.Y. Identification of the proton pathway in bacterial reaction centers. decrease of proton transfer rate by mutation of surface histidines at H126 and H128 and chemical rescue by imidazole identifies the initial proton donors Biochemistry. 40:2001;14538-14546.
    • (2001) Biochemistry , vol.40 , pp. 14538-14546
    • Ädelroth, P.1    Paddock, M.L.2    Tehrani, A.3    Beatty, J.T.4    Feher, G.5    Okamura, M.Y.6
  • 4
    • 0033614791 scopus 로고    scopus 로고
    • B in bacterial photosynthetic reaction centers
    • B in bacterial photosynthetic reaction centers Biochemistry. 38:1999;8253-8270.
    • (1999) Biochemistry , vol.38 , pp. 8253-8270
    • Alexov, E.G.1    Gunner, M.R.2
  • 6
    • 0027973329 scopus 로고
    • Crystallization of the reaction center from Rhodobacter sphaeroides in a new tetragonal form
    • Allen J.P. Crystallization of the reaction center from Rhodobacter sphaeroides in a new tetragonal form. Proteins. 20:1994;283-286.
    • (1994) Proteins , vol.20 , pp. 283-286
    • Allen, J.P.1
  • 10
    • 0005139633 scopus 로고
    • Proton transfer pathways in the reaction center of Rhodobacter sphaeroides: A computational study
    • J. Breton, & A. Vermeglio. New York: Plenum Press
    • Beroza P., Fredkin D.R., Okamura M.Y., Feher G. Proton transfer pathways in the reaction center of Rhodobacter sphaeroides. a computational study Breton J., Vermeglio A. The Photosynthetic Bacterial Reaction Center II. 1992;363-374 Plenum Press, New York.
    • (1992) The Photosynthetic Bacterial Reaction Center II , pp. 363-374
    • Beroza, P.1    Fredkin, D.R.2    Okamura, M.Y.3    Feher, G.4
  • 14
    • 0027176147 scopus 로고
    • New crystal form of the photosynthetic reaction centre from Rhodobacter sphaeroides of improved diffraction quality
    • Buchanan S.K., Fritzsch G., Ermler U., Michel H. New crystal form of the photosynthetic reaction centre from Rhodobacter sphaeroides of improved diffraction quality. J. Mol. Biol. 230:1993;1311-1314.
    • (1993) J. Mol. Biol. , vol.230 , pp. 1311-1314
    • Buchanan, S.K.1    Fritzsch, G.2    Ermler, U.3    Michel, H.4
  • 16
    • 0028103275 scopus 로고
    • The CCP4 (Collaborative Computational Project 4) suite: Programs for protein crystallography
    • CCP4 The CCP4 (Collaborative Computational Project 4) suite. programs for protein crystallography Acta Crystallogr. D. 50:1994;760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 17
    • 0037379781 scopus 로고    scopus 로고
    • Voltage-gated proton channels and other proton transfer pathways
    • Decoursey T.E. Voltage-gated proton channels and other proton transfer pathways. Physiol. Rev. 83:2003;475-579.
    • (2003) Physiol. Rev. , vol.83 , pp. 475-579
    • Decoursey, T.E.1
  • 18
    • 0028774335 scopus 로고
    • Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 Å resolution: Cofactors and protein-cofactor interactions
    • Ermler U., Fritzsch G., Buchanan S.K., Michel H. Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 Å resolution. cofactors and protein-cofactor interactions Structure. 2:1994;925-936.
    • (1994) Structure , vol.2 , pp. 925-936
    • Ermler, U.1    Fritzsch, G.2    Buchanan, S.K.3    Michel, H.4
  • 19
    • 0033119938 scopus 로고    scopus 로고
    • Further additions to MolScript version 1.4, including reading and contouring of electron-density maps
    • Esnouf R.M. Further additions to MolScript version 1.4, including reading and contouring of electron-density maps. Acta Crystallogr. D. 55:1999;938-940.
    • (1999) Acta Crystallogr. D. , vol.55 , pp. 938-940
    • Esnouf, R.M.1
  • 20
    • 0000058886 scopus 로고
    • Structure and function of bacterial photosynthetic reaction centers
    • Feher G., Allen J.P., Okamura M.Y., Rees D.C. Structure and function of bacterial photosynthetic reaction centers. Nature. 339:1989;111-116.
    • (1989) Nature , vol.339 , pp. 111-116
    • Feher, G.1    Allen, J.P.2    Okamura, M.Y.3    Rees, D.C.4
  • 21
    • 0036795645 scopus 로고    scopus 로고
    • Charge separation induces conformational changes in the photosynthetic reaction centre of purple bacteria
    • Fritzsch G., Koepke J., Diem R., Kuglstatter A., Baciou L. Charge separation induces conformational changes in the photosynthetic reaction centre of purple bacteria. Acta Crystallogr. D. 58:2002;1660-1663.
    • (2002) Acta Crystallogr. D , vol.58 , pp. 1660-1663
    • Fritzsch, G.1    Koepke, J.2    Diem, R.3    Kuglstatter, A.4    Baciou, L.5
  • 22
    • 0035852866 scopus 로고    scopus 로고
    • a shifts of key protonatable residues
    • a shifts of key protonatable residues. Biochemistry. 40:2001;1850-1860.
    • (2001) Biochemistry , vol.40 , pp. 1850-1860
    • Gerencser, L.1    Maroti, P.2
  • 24
    • 0000230806 scopus 로고
    • The reaction center protein from purple bacteria-structure and function
    • Gunner M.R. The reaction center protein from purple bacteria-structure and function. Curr. Top. Bioenerg. 16:1991;319-367.
    • (1991) Curr. Top. Bioenerg. , vol.16 , pp. 319-367
    • Gunner, M.R.1
  • 25
    • 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
  • 26
    • 0026731352 scopus 로고
    • In bacterial reaction centers protons can diffuse to the secondary quinone by alternative pathways
    • Hanson D.K., Baciou L., Tiede D.M., Nance S.L., Schiffer M., Sebban P. In bacterial reaction centers protons can diffuse to the secondary quinone by alternative pathways. Biochim. Biophys. Acta. 1102:1992;260-265.
    • (1992) Biochim. Biophys. Acta , vol.1102 , pp. 260-265
    • Hanson, D.K.1    Baciou, L.2    Tiede, D.M.3    Nance, S.L.4    Schiffer, M.5    Sebban, P.6
  • 29
    • 0031208887 scopus 로고    scopus 로고
    • Photophysics of photosynthesis. Structure and spectroscopy of reaction centers of purple bacteria
    • Hoff A.J., Deisenhofer J. Photophysics of photosynthesis. Structure and spectroscopy of reaction centers of purple bacteria. Phys. Rep. 287:1997;2-247.
    • (1997) Phys. Rep. , vol.287 , pp. 2-247
    • Hoff, A.J.1    Deisenhofer, J.2
  • 30
    • 0043095535 scopus 로고    scopus 로고
    • Lipidic cubic phase crystal structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.35 Å resolution
    • Katona G., Andreasson U., Landau E.M., Andreasson L.E., Neutze R. Lipidic cubic phase crystal structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.35 Å resolution. J. Mol. Biol. 331:2003;681-692.
    • (2003) J. Mol. Biol. , vol.331 , pp. 681-692
    • Katona, G.1    Andreasson, U.2    Landau, E.M.3    Andreasson, L.E.4    Neutze, R.5
  • 33
    • 0037064218 scopus 로고    scopus 로고
    • Wolinella succinogenes quinol: Fumarate reductase-2.2 Å resolution crystal structure and the E-pathway hypothesis of coupled transmembrane proton and electron transfer
    • Lancaster C.R. Wolinella succinogenes quinol. fumarate reductase-2.2 Å resolution crystal structure and the E-pathway hypothesis of coupled transmembrane proton and electron transfer Biochim. Biophys. Acta. 1565:2002;215-231.
    • (2002) Biochim. Biophys. Acta , vol.1565 , pp. 215-231
    • Lancaster, C.R.1
  • 34
    • 0030030176 scopus 로고    scopus 로고
    • Calculated coupling of electron and proton transfer in the photosynthetic reaction center of Rhodopseudomonas viridis
    • Lancaster C.R., Michel H., Honig B., Gunner M.R. Calculated coupling of electron and proton transfer in the photosynthetic reaction center of Rhodopseudomonas viridis. Biophys. J. 70:1996;2469-2492.
    • (1996) Biophys. J. , vol.70 , pp. 2469-2492
    • Lancaster, C.R.1    Michel, H.2    Honig, B.3    Gunner, M.R.4
  • 38
    • 0001099937 scopus 로고
    • Traitement statistique des erreurs dans la determination des structures cristallines
    • Luzzati P.V. Traitement statistique des erreurs dans la determination des structures cristallines. Acta Crystallog. 5:1952;802-810.
    • (1952) Acta Crystallog. , vol.5 , pp. 802-810
    • Luzzati, P.V.1
  • 39
    • 0028291259 scopus 로고
    • Proton conduction within the reaction centers of Rhodobacter capsulatus: The electrostatic role of the protein
    • Maroti P., Hanson D.K., Baciou L., Schiffer M., Sebban P. Proton conduction within the reaction centers of Rhodobacter capsulatus. the electrostatic role of the protein Proc. Natl. Acad. Sci. USA. 91:1994;5617-5621.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5617-5621
    • Maroti, P.1    Hanson, D.K.2    Baciou, L.3    Schiffer, M.4    Sebban, P.5
  • 41
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit: A versatile program for manipulating atomic coordinates and electron density
    • McRee D.E. XtalView/Xfit. a versatile program for manipulating atomic coordinates and electron density J. Struct. Biol. 125:1999;156-165.
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 42
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D photorealistic molecular graphics
    • Merritt E.A., Bacon J.D. Raster3D photorealistic molecular graphics. Methods Enzymol. 277:1997;505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, J.D.2
  • 43
    • 0032562166 scopus 로고    scopus 로고
    • In bacterial reaction centers, a key residue suppresses mutational blockage of two different proton transfer steps
    • Miksovska J., Valerio-Lepiniec M., Schiffer M., Hanson D.K., Sebban P. In bacterial reaction centers, a key residue suppresses mutational blockage of two different proton transfer steps. Biochemistry. 37:1998;2077-2083.
    • (1998) Biochemistry , vol.37 , pp. 2077-2083
    • Miksovska, J.1    Valerio-Lepiniec, M.2    Schiffer, M.3    Hanson, D.K.4    Sebban, P.5
  • 44
    • 0037716158 scopus 로고    scopus 로고
    • Understanding the mechanism of proton movement linked to oxygen reduction in cytochrome c oxidase: Lessons from other proteins
    • Mills D.A., Ferguson-Miller S. Understanding the mechanism of proton movement linked to oxygen reduction in cytochrome c oxidase. lessons from other proteins FEBS Lett. 545:2003;47-51.
    • (2003) FEBS Lett. , vol.545 , pp. 47-51
    • Mills, D.A.1    Ferguson-Miller, S.2
  • 47
    • 0002281681 scopus 로고
    • B in RCs
    • R.E. Blankenship, M.T. Madigan, & C.E. Bauer. Dordrecht, The Netherlands: Kluwer
    • B in RCs. Blankenship R.E., Madigan M.T., Bauer C.E. Anoxygenic Photosynthetic Bacteria. 1995;577-594 Kluwer, Dordrecht, The Netherlands.
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 577-594
    • Okamura, M.Y.1    Feher, G.2
  • 49
    • 0002733503 scopus 로고
    • Reaction centers from three herbicide resistant mutants of Rhodobacter sphaeroides 2.4.1: Sequence analysis and preliminary characterization
    • Paddock M.L., Rongey S.H., Abresch E.C., Feher G., Okamura M.Y. Reaction centers from three herbicide resistant mutants of Rhodobacter sphaeroides 2.4.1. sequence analysis and preliminary characterization Photosynth. Res. 17:1988;75-96.
    • (1988) Photosynth. Res. , vol.17 , pp. 75-96
    • Paddock, M.L.1    Rongey, S.H.2    Abresch, E.C.3    Feher, G.4    Okamura, M.Y.5
  • 50
    • 0024726467 scopus 로고
    • Pathway of proton transfer in bacterial reaction centers: Replacement of glutamic acid 212 in the L subunit by glutamine inhibits quinone (secondary acceptor) turnover
    • Paddock M.L., Rongey S.H., Feher G., Okamura M.Y. Pathway of proton transfer in bacterial reaction centers. replacement of glutamic acid 212 in the L subunit by glutamine inhibits quinone (secondary acceptor) turnover Proc. Natl. Acad. Sci. USA. 86:1989;6602-6606.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 6602-6606
    • Paddock, M.L.1    Rongey, S.H.2    Feher, G.3    Okamura, M.Y.4
  • 51
    • 0025134851 scopus 로고
    • Pathway of proton transfer in bacterial reaction centers: Replacement of serine-L223 by alanine inhibits electron and proton transfers associated with reduction of quinone to dihydroquinone
    • Paddock M.L., McPherson P.H., Feher G., Okamura M.Y. Pathway of proton transfer in bacterial reaction centers. replacement of serine-L223 by alanine inhibits electron and proton transfers associated with reduction of quinone to dihydroquinone Proc. Natl. Acad. Sci. USA. 87:1990;6803-6807.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6803-6807
    • Paddock, M.L.1    McPherson, P.H.2    Feher, G.3    Okamura, M.Y.4
  • 52
    • 0028009920 scopus 로고
    • Pathway of proton transfer in bacterial reaction centers: Role of aspartate-L213 in proton transfers associated with reduction of quinone to dihydroquinone
    • Paddock M.L., Rongey S.H., McPherson P.H., Juth A., Feher G., Okamura M.Y. Pathway of proton transfer in bacterial reaction centers. role of aspartate-L213 in proton transfers associated with reduction of quinone to dihydroquinone Biochemistry. 33:1994;734-745.
    • (1994) Biochemistry , vol.33 , pp. 734-745
    • Paddock, M.L.1    Rongey, S.H.2    McPherson, P.H.3    Juth, A.4    Feher, G.5    Okamura, M.Y.6
  • 58
    • 0037076542 scopus 로고    scopus 로고
    • The structure of a mutant photosynthetic reaction center shows unexpected changes in main chain orientations and quinone position
    • Pokkuluri P.R., Laible P.D., Deng Y.L., Wong T.N., Hanson D.K., Schiffer M. The structure of a mutant photosynthetic reaction center shows unexpected changes in main chain orientations and quinone position. Biochemistry. 41:2002;5998-6007.
    • (2002) Biochemistry , vol.41 , pp. 5998-6007
    • Pokkuluri, P.R.1    Laible, P.D.2    Deng, Y.L.3    Wong, T.N.4    Hanson, D.K.5    Schiffer, M.6
  • 59
    • 0032562210 scopus 로고    scopus 로고
    • Energetics of electron-transfer and protonation reactions of the quinones in the photosynthetic reaction center of Rhodopseudomonas viridis
    • Rabenstein B., Ullmann G.M., Knapp E.W. Energetics of electron-transfer and protonation reactions of the quinones in the photosynthetic reaction center of Rhodopseudomonas viridis. Biochemistry. 37:1998;2488-2495.
    • (1998) Biochemistry , vol.37 , pp. 2488-2495
    • Rabenstein, B.1    Ullmann, G.M.2    Knapp, E.W.3
  • 60
    • 0027405698 scopus 로고
    • Pathway of proton transfer in bacterial reaction centers: Second-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. second-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. USA. 90:1993;1325-1329.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1325-1329
    • Rongey, S.H.1    Paddock, M.L.2    Feher, G.3    Okamura, M.Y.4
  • 61
    • 0029007257 scopus 로고
    • Electrostatic dominoes: Long distance propagation of mutational effects in photosynthetic reaction centers of Rhodobacter capsulatus
    • Sebban P., Maroti P., Schiffer M., Hanson D.K. Electrostatic dominoes. long distance propagation of mutational effects in photosynthetic reaction centers of Rhodobacter capsulatus Biochemistry. 34:1995;8390-8397.
    • (1995) Biochemistry , vol.34 , pp. 8390-8397
    • Sebban, P.1    Maroti, P.2    Schiffer, M.3    Hanson, D.K.4
  • 62
    • 0344418714 scopus 로고    scopus 로고
    • Simulating proton translocations in proteins: Probing proton transfer pathways in the Rhodobacter sphaeroides reaction center
    • Sham Y.Y., Muegge I., Warshel A. Simulating proton translocations in proteins. Probing proton transfer pathways in the Rhodobacter sphaeroides reaction center Proteins. 36:1999;484-500.
    • (1999) Proteins , vol.36 , pp. 484-500
    • Sham, Y.Y.1    Muegge, I.2    Warshel, A.3
  • 63
    • 0034640335 scopus 로고    scopus 로고
    • Marcus rate theory applied to enzymatic proton transfer
    • Silverman D.N. Marcus rate theory applied to enzymatic proton transfer. Biochim. Biophys. Acta. 1458:2000;88-103.
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 88-103
    • Silverman, D.N.1
  • 64
    • 0030904273 scopus 로고    scopus 로고
    • Light-induced structural changes in photosynthetic reaction center: Implications for mechanism of electron-proton transfer
    • Stowell M.H., McPhillips T.M., Rees D.C., Soltis S.M., Abresch E., Feher G. Light-induced structural changes in photosynthetic reaction center. implications for mechanism of electron-proton transfer Science. 276:1997;812-816.
    • (1997) Science , vol.276 , pp. 812-816
    • Stowell, M.H.1    McPhillips, T.M.2    Rees, D.C.3    Soltis, S.M.4    Abresch, E.5    Feher, G.6
  • 65
    • 0025169243 scopus 로고
    • L213 in the proton transfer pathway to the secondary quinone of reaction centers from Rhodobacter sphaeroides
    • L213 in the proton transfer pathway to the secondary quinone of reaction centers from Rhodobacter sphaeroides. Biochim. Biophys. Acta. 1020:1990;107-111.
    • (1990) Biochim. Biophys. Acta , vol.1020 , pp. 107-111
    • Takahashi, E.1    Wraight, C.A.2
  • 67
    • 0029975953 scopus 로고    scopus 로고
    • Potentiation of proton transfer function by electrostatic interactions in photosynthetic reaction centers from Rhodobacter sphaeroides: First results from site-directed mutation of the H subunit
    • Takahashi E., Wraight C.A. Potentiation of proton transfer function by electrostatic interactions in photosynthetic reaction centers from Rhodobacter sphaeroides. First results from site-directed mutation of the H subunit Proc. Natl. Acad. Sci. USA. 93:1996;2640-2645.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2640-2645
    • Takahashi, E.1    Wraight, C.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.