메뉴 건너뛰기




Volumn 46, Issue 37, 2007, Pages 10461-10472

Structural responses to cavity-creating mutations in an integral membrane protein

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIOPHEOPHYTIN COFACTORS; CAVITY-CREATING MUTATIONS; INCUBATION; PROTEIN CRYSTALS;

EID: 34548686557     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701085w     Document Type: Article
Times cited : (11)

References (34)
  • 2
    • 0025276895 scopus 로고
    • Spectroscopic analysis of genetically-modified photosynthetic reaction centers
    • Coleman, W. J., and Youvan, D. C. (1990) Spectroscopic analysis of genetically-modified photosynthetic reaction centers, Annu. Rev. Biophys. Biophys. Chem. 19, 333-367.
    • (1990) Annu. Rev. Biophys. Biophys. Chem , vol.19 , pp. 333-367
    • Coleman, W.J.1    Youvan, D.C.2
  • 3
    • 0001337010 scopus 로고
    • The pathway, kinetics and thermodynamics of electron transfer in wild type and mutant bacterial reaction centers of purple nonsulfur bacteria
    • Blankenship, R. E, Madigan, M. T, and Bauer C. E, Eds, pp, Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Woodbury, N. W., and Allen, J. P. (1995) The pathway, kinetics and thermodynamics of electron transfer in wild type and mutant bacterial reaction centers of purple nonsulfur bacteria, in Anoxygenic Photosynthetic Bacteria (Blankenship, R. E., Madigan, M. T., and Bauer C. E., Eds.) pp 527-557, Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 527-557
    • Woodbury, N.W.1    Allen, J.P.2
  • 4
    • 0034577649 scopus 로고    scopus 로고
    • Reaction centres of purple bacteria
    • Scrutton, N. S, and Holzenburg, A, Eds, pp, Kluwer Academic/Plenum Publishers, New York
    • Van Brederode, M. E., and Jones, M. R. (2000) Reaction centres of purple bacteria, in Enzyme-Catalysed Electron and Radical Transfer (Scrutton, N. S., and Holzenburg, A., Eds.) pp 621-676, Kluwer Academic/Plenum Publishers, New York.
    • (2000) Enzyme-Catalysed Electron and Radical Transfer , pp. 621-676
    • Van Brederode, M.E.1    Jones, M.R.2
  • 5
    • 23844439587 scopus 로고    scopus 로고
    • Rewiring photosynthesis: Engineering wrong-way electron transfer in the purple bacterial reaction centre
    • Wakeham, M. C., and Jones, M. R. (2005) Rewiring photosynthesis: engineering wrong-way electron transfer in the purple bacterial reaction centre, Biochem. Soc. Trans. 33, 851-857.
    • (2005) Biochem. Soc. Trans , vol.33 , pp. 851-857
    • Wakeham, M.C.1    Jones, M.R.2
  • 7
    • 1242347393 scopus 로고    scopus 로고
    • Proton and electron transfer in the acceptor quinone complex of photosynthetic reaction centers from Rhodobacter sphaeroides
    • Wraight, C. A. (2004) Proton and electron transfer in the acceptor quinone complex of photosynthetic reaction centers from Rhodobacter sphaeroides, Front. Biosci. 9, 309-337.
    • (2004) Front. Biosci , vol.9 , pp. 309-337
    • Wraight, C.A.1
  • 8
    • 1642451819 scopus 로고    scopus 로고
    • Disruption of a specific molecular interaction with a bound lipid affects the thermal stability of the purple bacterial reaction center
    • Fyfe, P. K., Isaacs, N. W., Cogdell, R. J., and Jones, M. R. (2004) Disruption of a specific molecular interaction with a bound lipid affects the thermal stability of the purple bacterial reaction center, Biochim. Biophys. Acta 1608, 11-22.
    • (2004) Biochim. Biophys. Acta , vol.1608 , pp. 11-22
    • Fyfe, P.K.1    Isaacs, N.W.2    Cogdell, R.J.3    Jones, M.R.4
  • 9
    • 0034834616 scopus 로고    scopus 로고
    • Individual interactions influence the crystalline order for membrane proteins
    • Camara-Artigas, A., Magee, C. L., Williams, J. C., and Allen, J. P. (2001) Individual interactions influence the crystalline order for membrane proteins, Acta Crystallogr. D 57, 1281-1286.
    • (2001) Acta Crystallogr. D , vol.57 , pp. 1281-1286
    • Camara-Artigas, A.1    Magee, C.L.2    Williams, J.C.3    Allen, J.P.4
  • 10
    • 18844438921 scopus 로고    scopus 로고
    • Design of a redox-linked active metal site: Manganese bound to bacterial reaction centers at a site resembling that of photosystem II
    • Thielges, M., Uyeda, G., Camara-Artigas, A., Kalman, L., Williams, J. C., and Allen, J. P. (2005) Design of a redox-linked active metal site: Manganese bound to bacterial reaction centers at a site resembling that of photosystem II, Biochemistry 44, 7389-7394.
    • (2005) Biochemistry , vol.44 , pp. 7389-7394
    • Thielges, M.1    Uyeda, G.2    Camara-Artigas, A.3    Kalman, L.4    Williams, J.C.5    Allen, J.P.6
  • 11
    • 0002550620 scopus 로고
    • Reaction centers
    • Scheer, H, Ed, pp, CRC Press, Boca Raton, FL
    • Parson, W. W. (1991) Reaction centers, in Chlorophylls (Scheer, H., Ed.) pp 1153-1180, CRC Press, Boca Raton, FL.
    • (1991) Chlorophylls , pp. 1153-1180
    • Parson, W.W.1
  • 12
    • 0001124818 scopus 로고    scopus 로고
    • Photosynthetic bacterial reaction centers
    • Bendall, D. S, Ed, pp, BIOS Scientific Publishers, Oxford, U.K
    • Parson, W. W. (1996) Photosynthetic bacterial reaction centers, in Protein Electron Transfer (Bendall, D. S., Ed.) pp 125-160, BIOS Scientific Publishers, Oxford, U.K.
    • (1996) Protein Electron Transfer , pp. 125-160
    • Parson, W.W.1
  • 13
    • 0031208887 scopus 로고    scopus 로고
    • Photophysics of photosynthesis: Structure and spectroscopy of reaction centres of purple bacteria
    • Hoff, A. J., and Deisenhofer, J. (1997) Photophysics of photosynthesis: Structure and spectroscopy of reaction centres of purple bacteria, Phys. Rep.: Rev. Sect. Phys. Lett. 287, 2-247.
    • (1997) Phys. Rep.: Rev. Sect. Phys. Lett , vol.287 , pp. 2-247
    • Hoff, A.J.1    Deisenhofer, J.2
  • 14
    • 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., and Jones, M. R. (2000) Ubiquinone binding, ubiquinone exclusion, and detailed cofactor conformation in a mutant bacterial reaction center, Biochemistry 39, 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
  • 17
    • 1942502803 scopus 로고    scopus 로고
    • B site by A-branch or B-branch electron transfer in the reaction centre from Rhodobacter sphaeroides
    • B site by A-branch or B-branch electron transfer in the reaction centre from Rhodobacter sphaeroides, Biochemistry 43, 4755-4763.
    • (2004) Biochemistry , vol.43 , pp. 4755-4763
    • Wakeham, M.C.1    Nabedryk, E.2    Breton, J.3    Jones, M.R.4
  • 19
    • 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., and Jones, M. R. (1998) 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, 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
  • 20
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode, Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 21
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. (1994) AMoRe: an automated package for molecular replacement, Acta Crystallogr. A 50, 157-163.
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 22
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Refinement of macromolecular structures by the maximum-likelihood method, Acta Crystallogr. D 53, 240-255.
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 23
    • 18244409359 scopus 로고    scopus 로고
    • B) reduction by B-branch electron transfer in mutant bacterial reaction centers from Rhodobacter sphaeroides: Quantum efficiency and X-ray structure
    • B) reduction by B-branch electron transfer in mutant bacterial reaction centers from Rhodobacter sphaeroides: Quantum efficiency and X-ray structure, Biochemistry 44, 6920-6928.
    • (2005) Biochemistry , vol.44 , pp. 6920-6928
    • Paddock, M.L.1    Chang, C.2    Xu, Q.3    Abresch, E.C.4    Axelrod, H.L.5    Feher, G.6    Okamura, M.Y.7
  • 24
    • 25444501222 scopus 로고    scopus 로고
    • On the role of basic residues in adapting the purple bacterial reaction centre-LH1 photosystem for growth at elevated temperatures
    • Watson, A. J., Hughes, A. V., Fyfe, P. K., Wakeham, M. C., Holden-Dye, K., Heathcote, P., and Jones, M. R. (2005) On the role of basic residues in adapting the purple bacterial reaction centre-LH1 photosystem for growth at elevated temperatures, Photosynth. Res. 86, 81-100.
    • (2005) Photosynth. Res , vol.86 , pp. 81-100
    • Watson, A.J.1    Hughes, A.V.2    Fyfe, P.K.3    Wakeham, M.C.4    Holden-Dye, K.5    Heathcote, P.6    Jones, M.R.7
  • 25
    • 33744911339 scopus 로고    scopus 로고
    • Kinetic analysis of the thermal stability of the photosynthetic reaction centre from Rhodobacter sphaeroides
    • Hughes, A. V., Rees, P., Heathcote, P., and Jones, M. R. (2006) Kinetic analysis of the thermal stability of the photosynthetic reaction centre from Rhodobacter sphaeroides, Biophys. J. 90, 4155-4166.
    • (2006) Biophys. J , vol.90 , pp. 4155-4166
    • Hughes, A.V.1    Rees, P.2    Heathcote, P.3    Jones, M.R.4
  • 28
    • 0000178540 scopus 로고
    • Primary acceptor in bacterial photosynthesis - obligatory role of ubiquinone in photoactive reaction centers of Rhodopseudomonas spheroides
    • Okamura, M. Y., Isaacson, R. A., and Feher, G. (1975) Primary acceptor in bacterial photosynthesis - obligatory role of ubiquinone in photoactive reaction centers of Rhodopseudomonas spheroides, Proc. Natl. Acad. Sci. U.S.A. 72, 3491-3495.
    • (1975) Proc. Natl. Acad. Sci. U.S.A , vol.72 , pp. 3491-3495
    • Okamura, M.Y.1    Isaacson, R.A.2    Feher, G.3
  • 30
    • 0023048040 scopus 로고
    • Radical-pair energetics and decay mechanisms in reaction centers containing anthraquinones, naphthoquinones or benzoquinones in place of ubiquinone
    • Woodbury, N. W., Parson, W. W., Gunner, M. R., Prince, R. C., and Dutton, P. L. (1986) Radical-pair energetics and decay mechanisms in reaction centers containing anthraquinones, naphthoquinones or benzoquinones in place of ubiquinone, Biochim. Biophys. Acta 851, 6-22.
    • (1986) Biochim. Biophys. Acta , vol.851 , pp. 6-22
    • Woodbury, N.W.1    Parson, W.W.2    Gunner, M.R.3    Prince, R.C.4    Dutton, P.L.5
  • 31
    • 0027336755 scopus 로고
    • A site redox cofactor structure on equilibrium binding, in situ electrochemistry, and electron-transfer performance in the photosynthetic reaction center protein
    • A site redox cofactor structure on equilibrium binding, in situ electrochemistry, and electron-transfer performance in the photosynthetic reaction center protein, Biochemistry 32, 4769-4779.
    • (1993) Biochemistry , vol.32 , pp. 4769-4779
    • Warncke, K.1    Dutton, P.L.2
  • 32
    • 0000422036 scopus 로고
    • Bacterial reaction centers with modified tetrapyrrole chromophores
    • Deisenhofer, J, and Norris, J. R, Eds, Academic Press, San Diego, CA
    • Scheer, H., and Struck, A. (1993) Bacterial reaction centers with modified tetrapyrrole chromophores, in The Photosynthetic Reaction Center (Deisenhofer, J., and Norris, J. R., Eds.) Vol. 1, pp 157-192, Academic Press, San Diego, CA.
    • (1993) The Photosynthetic Reaction Center , vol.1 , pp. 157-192
    • Scheer, H.1    Struck, A.2
  • 33
    • 0000455514 scopus 로고
    • Bacterial reaction centers with modified tetrapyrrole chromophores
    • Blankenship, R. E, Madigan, M. T, and Bauer, C, Eds, pp, Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Scheer, H., and Hartwich, G. (1995) Bacterial reaction centers with modified tetrapyrrole chromophores, in Anoxygenic Photosynthetic Bacteria (Blankenship, R. E., Madigan, M. T., and Bauer, C., Eds.) pp 649-663, Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 649-663
    • Scheer, H.1    Hartwich, G.2
  • 34
    • 0033106268 scopus 로고    scopus 로고
    • Remarks about protein structure precision
    • Cruickshank, D. W. J. (1999) Remarks about protein structure precision, Acta Crystallogr. D 55, 583-601.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 583-601
    • Cruickshank, D.W.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.