메뉴 건너뛰기




Volumn 100, Issue 4, 1997, Pages 852-862

The cytochrome b6f complex. Novel aspects

Author keywords

Cytochrome f; Membrane proteins; Plastocyanin; Proton translocation; Rieske iron sulfur protein

Indexed keywords


EID: 0030826096     PISSN: 00319317     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1399-3054.1997.1000411.x     Document Type: Article
Times cited : (17)

References (54)
  • 1
    • 0040499666 scopus 로고
    • 6/f-complex and PSI-complex from the cyanobacterium Synechocystis PCC6803
    • N. Murata, ed., Kluwer, Dordrecht. ISBN 0-7923-2073-5.
    • 6/f-complex and PSI-complex from the cyanobacterium Synechocystis PCC6803. - In Research in Photosynthesis (N. Murata, ed.), Vol. I, pp. 629-632. Kluwer, Dordrecht. ISBN 0-7923-2073-5.
    • (1992) Research in Photosynthesis , vol.1 , pp. 629-632
    • Bald, D.1    Kruip, J.2    Boekema, E.J.3    Rogner, M.4
  • 2
    • 0028807043 scopus 로고
    • The deletion of petG in Chlamydomonas reinhardtii disrupts the Cyt bf complex
    • Berthold, D., Schmidt, C. L. & Malkin, R. 1995. The deletion of petG in Chlamydomonas reinhardtii disrupts the Cyt bf complex. - J. Biol. Chem. 270: 29293-29298.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29293-29298
    • Berthold, D.1    Schmidt, C.L.2    Malkin, R.3
  • 4
    • 0025767748 scopus 로고
    • Nucleotide sequences of the continuous and the separated petA, petB, and petD chloroplast genes in C. reinhardtii
    • Büschlen, S., Choquet, Y., Kuras, R. & Wollman, F. A. 1991. Nucleotide sequences of the continuous and the separated petA, petB, and petD chloroplast genes in C. reinhardtii. - FEBS Lett. 284: 257-262.
    • (1991) FEBS Lett. , vol.284 , pp. 257-262
    • Büschlen, S.1    Choquet, Y.2    Kuras, R.3    Wollman, F.A.4
  • 6
    • 0018118041 scopus 로고
    • Circular dichroic analysis of protein conformation: Inclusion of the β-turns
    • Chang, C. T., Wu, C.-S. C. & Yang, J. T. 1978. Circular dichroic analysis of protein conformation: Inclusion of the β-turns. - Anal. Biochem. 91: 13-31.
    • (1978) Anal. Biochem. , vol.91 , pp. 13-31
    • Chang, C.T.1    Wu, C.-S.C.2    Yang, J.T.3
  • 10
    • 0002320878 scopus 로고
    • Catalytic sites for reduction and oxidation of quinones
    • S. Papa, B. Chance and L. Ernster, eds, Plenum Press, New York, NY. ISBN 0-306-42693-5
    • Crofts, A. R., Robinson, H., Andrews, K., van Doren, S. & Berry, E. 1987. Catalytic sites for reduction and oxidation of quinones. - In Cytochrome Systems: Molecular Biology and Bioenergetics (S. Papa, B. Chance and L. Ernster, eds), pp. 617-624. Plenum Press, New York, NY. ISBN 0-306-42693-5.
    • (1987) Cytochrome Systems: Molecular Biology and Bioenergetics , pp. 617-624
    • Crofts, A.R.1    Robinson, H.2    Andrews, K.3    Van Doren, S.4    Berry, E.5
  • 11
    • 0005384356 scopus 로고
    • The Nobel lecture: The photosynthetic reaction center from the purple bacterium Rhodopseudomonas viridis
    • Deisenhofer, J. & Michel, H. 1989. The Nobel lecture: The photosynthetic reaction center from the purple bacterium Rhodopseudomonas viridis. - EMBO J. 8: 2149-2170.
    • (1989) EMBO J. , vol.8 , pp. 2149-2170
    • Deisenhofer, J.1    Michel, H.2
  • 12
    • 0028338910 scopus 로고
    • Characterization of the gene of the chloroplast Rieske iron-sulfur protein in Chlamydomonas reinhardtii. Indications for an uncleaved lumen targeting sequence
    • de Vitry, C. 1994. Characterization of the gene of the chloroplast Rieske iron-sulfur protein in Chlamydomonas reinhardtii. Indications for an uncleaved lumen targeting sequence. - J. Biol. Chem. 269: 7603.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7603
    • De Vitry, C.1
  • 14
    • 0028774335 scopus 로고
    • Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 Å resolution: Cofactors and protein-cofactor interactions
    • Ermler, U. G., Fritsch, S. K., Buchanan, S. K. & Michel, H. 1994. Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 Å resolution: Cofactors and protein-cofactor interactions. - Structure 2: 925-936.
    • (1994) Structure , vol.2 , pp. 925-936
    • Ermler, U.G.1    Fritsch, S.K.2    Buchanan, S.K.3    Michel, H.4
  • 15
    • 0026503527 scopus 로고
    • Organization and structure of plastome psbF, psbL, petG and ORF712 genes in Chlamydomonas reinhardtii
    • Fong, S. E. & Surzycki, S. J. 1992. Organization and structure of plastome psbF, psbL, petG and ORF712 genes in Chlamydomonas reinhardtii. - Curr. Genet. 21: 527-530.
    • (1992) Curr. Genet. , vol.21 , pp. 527-530
    • Fong, S.E.1    Surzycki, S.J.2
  • 18
    • 0000121207 scopus 로고
    • Cytochrome f: Structure, function, and biosynthesis
    • Gray, J. C. 1992. Cytochrome f: Structure, function, and biosynthesis. - Photosynth. Res. 34: 359-374.
    • (1992) Photosynth. Res. , vol.34 , pp. 359-374
    • Gray, J.C.1
  • 19
    • 0026691440 scopus 로고
    • The biosynthesis of membrane and soluble c-type cytochromes of C. reinhardtii is dependent upon multiple, common gene products
    • Howe, G. & Merchant, S. 1992. The biosynthesis of membrane and soluble c-type cytochromes of C. reinhardtii is dependent upon multiple, common gene products. - EMBO J. 11: 2789-2801.
    • (1992) EMBO J. , vol.11 , pp. 2789-2801
    • Howe, G.1    Merchant, S.2
  • 24
    • 0002500644 scopus 로고
    • Photosynthetic capacity, osmotic response and solute content of leaves and chloroplasts from Spinacia oleracea under salt stress
    • Kaiser, W. M., Weber, H. & Sauer, M. 1983. Photosynthetic capacity, osmotic response and solute content of leaves and chloroplasts from Spinacia oleracea under salt stress. - Z. Pflanzenphysiol. 113: 15-27.
    • (1983) Z. Pflanzenphysiol. , vol.113 , pp. 15-27
    • Kaiser, W.M.1    Weber, H.2    Sauer, M.3
  • 25
    • 0029995705 scopus 로고    scopus 로고
    • The role of acidic residues of plastocyanin in its interaction with Cyt f
    • Kannt, A., Young, S. & Bendall, D. S. 1996. The role of acidic residues of plastocyanin in its interaction with Cyt f. - Biochim. Biophys. Acta 1277: 115-126.
    • (1996) Biochim. Biophys. Acta , vol.1277 , pp. 115-126
    • Kannt, A.1    Young, S.2    Bendall, D.S.3
  • 27
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. - J. Appl. Crystallogr. 24: 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 28
    • 0028147508 scopus 로고
    • Atomic model of plant light-harvesting complex by electron crystallography
    • Kühlbrandt, W., Wang, D. N. & Fujiyoshi, Y. 1994. Atomic model of plant light-harvesting complex by electron crystallography. - Nature 367: 614-621.
    • (1994) Nature , vol.367 , pp. 614-621
    • Kühlbrandt, W.1    Wang, D.N.2    Fujiyoshi, Y.3
  • 29
    • 0026086866 scopus 로고
    • Restricted diffusion in photosynthetic membranes
    • Lavergne, J. & Joliot, P. 1991. Restricted diffusion in photosynthetic membranes. - Trends Biochem. Sci. 16: 129-134.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 129-134
    • Lavergne, J.1    Joliot, P.2
  • 32
    • 0023656828 scopus 로고
    • Variable selection method improves the prediction of protein secondary structure from circular dichroism
    • Manavalan, P. & Johnson, W. C. Jr. 1987. Variable selection method improves the prediction of protein secondary structure from circular dichroism. - Anal. Biochem. 167: 76-85.
    • (1987) Anal. Biochem. , vol.167 , pp. 76-85
    • Manavalan, P.1    Johnson Jr., W.C.2
  • 33
    • 0028773015 scopus 로고
    • Crystal structure of chloroplast Cyt f reveals a novel Cyt fold and unexpected heme ligation
    • Martinez, S. E., Huang, D., Szczepaniak, A., Cramer, W. A. & Smith, J. L. 1994. Crystal structure of chloroplast Cyt f reveals a novel Cyt fold and unexpected heme ligation. - Structure 2: 95-105.
    • (1994) Structure , vol.2 , pp. 95-105
    • Martinez, S.E.1    Huang, D.2    Szczepaniak, A.3    Cramer, W.A.4    Smith, J.L.5
  • 34
    • 0029897140 scopus 로고    scopus 로고
    • The heme redox center of chloroplast Cyt f is linked to a buried five-water chain
    • _, Huang, D., Ponomarev, M., Cramer, W. A. & Smith, J. L. 1996. The heme redox center of chloroplast Cyt f is linked to a buried five-water chain. - Protein Sci. 5: 1081-1092.
    • (1996) Protein Sci. , vol.5 , pp. 1081-1092
    • Huang, D.1    Ponomarev, M.2    Cramer, W.A.3    Smith, J.L.4
  • 35
    • 0002857939 scopus 로고
    • Structural analysis and expression during dark-light transitions of a gene for Cyt f in Chlamydomonas reinhardtii
    • Matsumoto, T., Matsuo, M. & Matsuda, Y. 1991. Structural analysis and expression during dark-light transitions of a gene for Cyt f in Chlamydomonas reinhardtii. - Plant Cell Physiol. 32: 863-872.
    • (1991) Plant Cell Physiol. , vol.32 , pp. 863-872
    • Matsumoto, T.1    Matsuo, M.2    Matsuda, Y.3
  • 36
    • 0027319734 scopus 로고
    • Transient kinetics of electron transfer from a variety of c-type cytochromes to plastocyanin
    • Meyer, T. E., Zhao, Z. G., Cusanovich, M. A. & Tollin, G. 1993. Transient kinetics of electron transfer from a variety of c-type cytochromes to plastocyanin. - Biochemistry 32: 4552-4559.
    • (1993) Biochemistry , vol.32 , pp. 4552-4559
    • Meyer, T.E.1    Zhao, Z.G.2    Cusanovich, M.A.3    Tollin, G.4
  • 39
    • 0020803933 scopus 로고
    • 1 ATP synthetase complexes into phospholipid and galactolipid liposomes
    • 1 ATP synthetase complexes into phospholipid and galactolipid liposomes. - J. Cell Biol. 97: 301-310.
    • (1983) J. Cell Biol. , vol.97 , pp. 301-310
    • Mörschel, E.1    Staehelin, A.2
  • 42
    • 0030011088 scopus 로고    scopus 로고
    • + translocation along the single-file water chain in the gramicidin A channel
    • + translocation along the single-file water chain in the gramicidin A channel. - Biophys. J. 71: 19-39.
    • (1996) Biophys. J. , vol.71 , pp. 19-39
    • Pomes, R.1    Roux, B.2
  • 43
    • 0027340169 scopus 로고
    • 1.5 Å Crystal structure of plastocyanin from the green alga, C. reinhardtii
    • Redinbo, M., Cascio, D., Choukair, M. K., Rice, D., Merchant, S. & Yeates, T. O. 1993. 1.5 Å Crystal structure of plastocyanin from the green alga, C. reinhardtii. - Biochemistry 32: 10560-10567.
    • (1993) Biochemistry , vol.32 , pp. 10560-10567
    • Redinbo, M.1    Cascio, D.2    Choukair, M.K.3    Rice, D.4    Merchant, S.5    Yeates, T.O.6
  • 44
    • 0025780587 scopus 로고
    • The interactions of duroquinol, DBMIB, and NQNO with the chloroplast Cyt bf complex
    • Rich, P. R., Madgwick, S. A. & Moss, D. A. 1991. The interactions of duroquinol, DBMIB, and NQNO with the chloroplast Cyt bf complex. - Biochim. Biophys. Acta 1058: 312-328.
    • (1991) Biochim. Biophys. Acta , vol.1058 , pp. 312-328
    • Rich, P.R.1    Madgwick, S.A.2    Moss, D.A.3
  • 45
    • 0030446029 scopus 로고    scopus 로고
    • Effect of the interdomain basic region of Cyt f on its redox reactions in vivo
    • Soriano, G., Ponomarev, M., Tae, G.-S. & Cramer, W. A. 1996. Effect of the interdomain basic region of Cyt f on its redox reactions in vivo. - Biochemistry 35: 14590-14598.
    • (1996) Biochemistry , vol.35 , pp. 14590-14598
    • Soriano, G.1    Ponomarev, M.2    Tae, G.-S.3    Cramer, W.A.4
  • 48
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matrix choice
    • Thompson, J. D., Higgins, D. G. & Gibson, T. J. 1994. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matrix choice.- Nucleic Acids Res. 22: 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 49
    • 0030607121 scopus 로고    scopus 로고
    • Some characteristics of Cyt f in the cyanobacterium Phormidium laminosum: Its sequence and charge properties in the reaction with plastocyanin
    • Wagner, M. J., Packer, J. C. L., Howe, C. J. & Bendall, D. S. 1996. Some characteristics of Cyt f in the cyanobacterium Phormidium laminosum: Its sequence and charge properties in the reaction with plastocyanin. - Biochim. Biophys. Acta 1276: 246-252.
    • (1996) Biochim. Biophys. Acta , vol.1276 , pp. 246-252
    • Wagner, M.J.1    Packer, J.C.L.2    Howe, C.J.3    Bendall, D.S.4
  • 50
    • 0006800575 scopus 로고
    • Mobile electron carriers in thylakoids
    • Photosynthesis III (L. A. Staehelin and C. J. Arntzen, eds), Springer-Verlag, Berlin. ISBN 3-540-16140-6
    • Whitmarsh, J. 1986. Mobile electron carriers in thylakoids. - In Encyclopedia of Plant Physiology, New Series. Vol. 19, Photosynthesis III (L. A. Staehelin and C. J. Arntzen, eds), pp. 508-527. Springer-Verlag, Berlin. ISBN 3-540-16140-6.
    • (1986) Encyclopedia of Plant Physiology, New Series. , vol.19 , pp. 508-527
    • Whitmarsh, J.1
  • 52
    • 0000748066 scopus 로고
    • Epistatic effects in thylakoid protein synthesis: The example of Cyt f
    • P. Mathis, ed., Kluwer, Dordrecht. ISBN 0-7923-3862-6
    • Wollman, F. A., Kuras, R. & Choquet, Y. 1995. Epistatic effects in thylakoid protein synthesis: The example of Cyt f. - In Proceedings of the Xth International Congress on Photosynthesis (P. Mathis, ed.), pp. 737-742. Kluwer, Dordrecht. ISBN 0-7923-3862-6.
    • (1995) Proceedings of the Xth International Congress on Photosynthesis , pp. 737-742
    • Wollman, F.A.1    Kuras, R.2    Choquet, Y.3
  • 54
    • 0029962504 scopus 로고    scopus 로고
    • Characterization and crystallization of the lumen-side domain of the chloroplast Rieske iron-sulfur protein
    • Zhang, H., Carrell, C. J., Huang, D., Sled, V., Ohnishi, T., Smith, J. L. & Cramer, W. A. 1996. Characterization and crystallization of the lumen-side domain of the chloroplast Rieske iron-sulfur protein. - J. Biol. Chem. 271: 31360-31366.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31360-31366
    • Zhang, H.1    Carrell, C.J.2    Huang, D.3    Sled, V.4    Ohnishi, T.5    Smith, J.L.6    Cramer, W.A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.