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Volumn 426, Issue 6965, 2003, Pages 413-418

An atypical haem in the cytochrome b6f complex

Author keywords

[No Author keywords available]

Indexed keywords

ALGAE; AMINO ACIDS; BACTERIA; BIOLOGICAL MEMBRANES; CHLOROPHYLL; ELECTRON TRANSITIONS; OXYGEN; PHOTOSYNTHESIS; PROTONS;

EID: 0344497439     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature02155     Document Type: Article
Times cited : (535)

References (51)
  • 1
    • 0017148721 scopus 로고
    • Possible molecular mechanisms of the protomotive function of cytochrome systems
    • Mitchell, P. Possible molecular mechanisms of the protomotive function of cytochrome systems. J. Theor. Biol. 62, 327-367 (1976).
    • (1976) J. Theor. Biol. , vol.62 , pp. 327-367
    • Mitchell, P.1
  • 2
    • 48749143707 scopus 로고
    • The electrochemical domain of photosynthesis
    • Crofts, A. & Wraight, C. A. The electrochemical domain of photosynthesis. Biochim. Biophys. Acta 726, 149-185 (1983).
    • (1983) Biochim. Biophys. Acta , vol.726 , pp. 149-185
    • Crofts, A.1    Wraight, C.A.2
  • 3
    • 0032477715 scopus 로고    scopus 로고
    • The plastid ndh genes code for an NADH-specific dehydrogenase: Isolation of a complex I analogue from pea thylakoid membranes
    • Sazanov, L. A., Burrows, P. A. & Nixon, P. J. The plastid ndh genes code for an NADH-specific dehydrogenase: isolation of a complex I analogue from pea thylakoid membranes. Proc. Natl Acad. Sci. USA 95, 1319-1324 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 1319-1324
    • Sazanov, L.A.1    Burrows, P.A.2    Nixon, P.J.3
  • 5
    • 0002565747 scopus 로고
    • 6 in an algal mutant lacking photosystem I centers
    • 6 in an algal mutant lacking photosystem I centers. Biochim. Biophys. Acta 725, 25-33 (1983).
    • (1983) Biochim. Biophys. Acta , vol.725 , pp. 25-33
    • Lavergne, J.1
  • 6
    • 0001695270 scopus 로고
    • The low potential electron transfer chain in cytochrome b/f complex
    • Joliot, P. & Joliot, A. The low potential electron transfer chain in cytochrome b/f complex. Biochim. Biophys. Acta 933, 319-333 (1988).
    • (1988) Biochim. Biophys. Acta , vol.933 , pp. 319-333
    • Joliot, P.1    Joliot, A.2
  • 7
    • 0037423885 scopus 로고    scopus 로고
    • Role of chloroplast protein kinase Stt7 in LHCII phosphorylation and state transition in Chlamydomonas
    • Depege, N., Bellafiore, S. & Rochaix, J.-D. Role of chloroplast protein kinase Stt7 in LHCII phosphorylation and state transition in Chlamydomonas. Science 299, 1572-1575 (2003).
    • (2003) Science , vol.299 , pp. 1572-1575
    • Depege, N.1    Bellafiore, S.2    Rochaix, J.-D.3
  • 8
    • 0035898532 scopus 로고    scopus 로고
    • State transitions reveal the dynamics and flexibility of the photosynthetic apparatus
    • Wollman, F.-A. State transitions reveal the dynamics and flexibility of the photosynthetic apparatus. EMBO J. 20, 3623-3630 (2001).
    • (2001) EMBO J. , vol.20 , pp. 3623-3630
    • Wollman, F.-A.1
  • 9
    • 0032555219 scopus 로고    scopus 로고
    • In vivo analysis of the effect of dicyclohexylcarbodiimide on electron and proton transfers in cytochrome bf complex of Chlorella sorokiniana
    • Joliot, P. & Joliot, A. In vivo analysis of the effect of dicyclohexylcarbodiimide on electron and proton transfers in cytochrome bf complex of Chlorella sorokiniana. Biochemistry 37, 10404-10410 (1998).
    • (1998) Biochemistry , vol.37 , pp. 10404-10410
    • Joliot, P.1    Joliot, A.2
  • 10
    • 0030824327 scopus 로고    scopus 로고
    • 6f complex
    • 6f complex. J. Biol. Chem. 272, 21901-21908 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 21901-21908
    • Pierre, Y.1
  • 11
    • 0030867866 scopus 로고    scopus 로고
    • 1 complex from bovine heart mitochondria
    • 1 complex from bovine heart mitochondria. Science 277, 60-66 (1997).
    • (1997) Science , vol.277 , pp. 60-66
    • Xia, D.1
  • 12
    • 0032537117 scopus 로고    scopus 로고
    • 1
    • 1. Nature 392, 677-684 (1998).
    • (1998) Nature , vol.392 , pp. 677-684
    • Zhang, Z.1
  • 13
    • 0032479524 scopus 로고    scopus 로고
    • 1 complex
    • 1 complex. Science 281, 64-71 (1998).
    • (1998) Science , vol.281 , pp. 64-71
    • Iwata, S.1
  • 19
    • 0028773015 scopus 로고
    • Crystal structure of chloroplast cytochrome freveals a novel cytochrome fold and unexpected heme ligation
    • Martinez, S. E., Huang, D., Szczepaniak, A., Cramer, W. A. & Smith, J. L. Crystal structure of chloroplast cytochrome freveals a novel cytochrome fold and unexpected heme ligation. Structure 2, 95-105 (1994).
    • (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
  • 21
    • 0031574021 scopus 로고    scopus 로고
    • Biological identity and diversity in photosynthesis and respiration: Structure of the lumen-side domain of the chloroplast Rieske protein
    • Carrell, C. J., Zhang, H., Cramer, W. A. & Smith, J. L. Biological identity and diversity in photosynthesis and respiration: structure of the lumen-side domain of the chloroplast Rieske protein. Structure 5, 1613-1625 (1997).
    • (1997) Structure , vol.5 , pp. 1613-1625
    • Carrell, C.J.1    Zhang, H.2    Cramer, W.A.3    Smith, J.L.4
  • 23
    • 0033556297 scopus 로고    scopus 로고
    • 6f complex of oxygenic photosynthesis protects against oxygen damage
    • 6f complex of oxygenic photosynthesis protects against oxygen damage. J. Biol. Chem. 274, 1581-1587 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 1581-1587
    • Zhang, H.1    Huang, D.2    Cramer, W.A.3
  • 25
    • 0031863230 scopus 로고    scopus 로고
    • 6f of Synechocystis PCC6803
    • 6f of Synechocystis PCC6803. Biophys. J. 75, 389-398 (1998).
    • (1998) Biophys. J. , vol.75 , pp. 389-398
    • Peterman, E.J.1
  • 26
    • 0037657832 scopus 로고    scopus 로고
    • Role of charges on cytochrome f from the cyanobacterium Phormidium laminosum in its interaction with plastocyanin
    • Hart, S. E., Schlarb-Ridley, B. G., Delon, C., Bendall, D. S. J. & Howe, C. J. Role of charges on cytochrome f from the cyanobacterium Phormidium laminosum in its interaction with plastocyanin. Biochemistry 42, 4829-4836 (2003).
    • (2003) Biochemistry , vol.42 , pp. 4829-4836
    • Hart, S.E.1    Schlarb-Ridley, B.G.2    Delon, C.3    Bendall, D.S.J.4    Howe, C.J.5
  • 27
    • 0038118626 scopus 로고    scopus 로고
    • Cytochrome f translation in Chlamydomonas chloroplast is autoregulated by its carboxyl-terminal domain
    • Choquet, Y., Zito, F., Wostrikoff, K. & Wollman, F.-A. Cytochrome f translation in Chlamydomonas chloroplast is autoregulated by its carboxyl-terminal domain. Plant Cell 15, 1443-1454 (2003).
    • (2003) Plant Cell , vol.15 , pp. 1443-1454
    • Choquet, Y.1    Zito, F.2    Wostrikoff, K.3    Wollman, F.-A.4
  • 30
    • 0037062618 scopus 로고    scopus 로고
    • 6f, as evidenced by the pH dependence of electron transfer in whole cells of Chlamydomonas reinhardtii
    • 6f, as evidenced by the pH dependence of electron transfer in whole cells of Chlamydomonas reinhardtii. Biochemistry 41, 7475-7482 (2002).
    • (2002) Biochemistry , vol.41 , pp. 7475-7482
    • Finazzi, G.1
  • 31
    • 0024959362 scopus 로고
    • 1 of Euglena gracilis mitochondrial complex 111
    • 1 of Euglena gracilis mitochondrial complex 111. Eur. J. Biochem. 178, 649-656 (1989).
    • (1989) Eur. J. Biochem. , vol.178 , pp. 649-656
    • Mukai, K.1
  • 32
    • 0023653927 scopus 로고
    • Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra
    • Berry, E. A. & Trumpower, B. L. Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra. Anal. Biochem. 161, 1-15 (1987).
    • (1987) Anal. Biochem. , vol.161 , pp. 1-15
    • Berry, E.A.1    Trumpower, B.L.2
  • 33
    • 0019585529 scopus 로고
    • 6 complex of five polypeptides with plastoquinol-plastocyanin-oxidoreductase activity from spinach chloroplasts
    • 6 complex of five polypeptides with plastoquinol-plastocyanin-oxidoreductase activity from spinach chloroplasts. Eur. J. Biochem. 117, 591-595 (1981).
    • (1981) Eur. J. Biochem. , vol.117 , pp. 591-595
    • Hurt, E.1    Hauska, G.2
  • 36
    • 0033535930 scopus 로고    scopus 로고
    • Assignment of the heme axial ligand(s) for the ferric myoglobin (H93G) and heme oxygenase (H25A) cavity mutants as oxygen donors using magnetic circular dichroism
    • Pond, A. E. et al. Assignment of the heme axial ligand(s) for the ferric myoglobin (H93G) and heme oxygenase (H25A) cavity mutants as oxygen donors using magnetic circular dichroism. Biochemistry 38, 7601-7608 (1999).
    • (1999) Biochemistry , vol.38 , pp. 7601-7608
    • Pond, A.E.1
  • 37
    • 0035814811 scopus 로고    scopus 로고
    • Replacement of the axial histidine ligand with imidazole in cytochrome c peroxidase. 2. Effects on heme coordination and function
    • Hirst, J. et al. Replacement of the axial histidine ligand with imidazole in cytochrome c peroxidase. 2. Effects on heme coordination and function. Biochemistry 40, 1274-1283 (2001).
    • (2001) Biochemistry , vol.40 , pp. 1274-1283
    • Hirst, J.1
  • 40
    • 0032502756 scopus 로고    scopus 로고
    • Studies of the cytochrome subunits of menaquinone: Cytochrome c reductase (bc complex) of Bacillus subtilis. Evidence for the covalent attachment of heme to the cytochrome b subunit
    • Yu, J. & Le Brun, N. E. Studies of the cytochrome subunits of menaquinone: cytochrome c reductase (bc complex) of Bacillus subtilis. Evidence for the covalent attachment of heme to the cytochrome b subunit. J. Biol. Chem. 273, 8860-8866 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 8860-8866
    • Yu, J.1    Le Brun, N.E.2
  • 41
    • 0034697992 scopus 로고    scopus 로고
    • Early evolution of cytochrome bc complexes
    • Schütz, M. et al. Early evolution of cytochrome bc complexes. J. Mol. Biol. 300, 663-675 (2000).
    • (2000) J. Mol. Biol. , vol.300 , pp. 663-675
    • Schütz, M.1
  • 42
    • 0027241479 scopus 로고
    • The chloroplast cytochrome bc complex: A critical focus on function
    • Hope, A. B. The chloroplast cytochrome bc complex: a critical focus on function. Biochim. Biophys. Acta 1143, 1-22 (1993).
    • (1993) Biochim. Biophys. Acta , vol.1143 , pp. 1-22
    • Hope, A.B.1
  • 43
    • 0242494128 scopus 로고    scopus 로고
    • 6f complex of oxygenic photosynthesis: Tuning the cavity
    • 2 October (doi:10.1126/science. 1090165)
    • 6f complex of oxygenic photosynthesis: Tuning the cavity. Science, 2 October 2003 (doi:10.1126/science.1090165).
    • (2003) Science
    • Kurisu, G.1    Zhang, H.2    Smith, J.L.3    Cramer, W.A.4
  • 44
    • 0021679693 scopus 로고
    • Antibiotica aus gleitende Bakterien XIII:Stigmatellin A und B-zwei neue Antibiotika aus Stigmatella aurantiaca (Myxobacterales)
    • Höffle, G., Kunze, B., Zorzin, C. & Reichenbach, H. Antibiotica aus gleitende Bakterien XIII:Stigmatellin A und B-zwei neue Antibiotika aus Stigmatella aurantiaca (Myxobacterales). Liebigs Annal. Chem. 12, 1883-1904 (1984).
    • (1984) Liebigs Annal. Chem. , vol.12 , pp. 1883-1904
    • Höffle, G.1    Kunze, B.2    Zorzin, C.3    Reichenbach, H.4
  • 45
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • The CCP4 suite: Programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 46
    • 0034622581 scopus 로고    scopus 로고
    • Interruption of the internal water chain of cytochrome f impairs photosynthetic function
    • Sainz, G. et al. Interruption of the internal water chain of cytochrome f impairs photosynthetic function. Biochemistry 39, 9164-9173 (2000).
    • (2000) Biochemistry , vol.39 , pp. 9164-9173
    • Sainz, G.1
  • 47
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 48
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brünger, A. T. et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brünger, A.T.1
  • 49
    • 0026244229 scopus 로고
    • A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 50
    • 0030815133 scopus 로고    scopus 로고
    • Raster 3D photorealistic molecular graphics
    • Merritt, E. & Bacon, D. Raster3D photorealistic molecular graphics. Methods Enzymol. 277, 505-524 (1997).
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.1    Bacon, D.2
  • 51
    • 85006166266 scopus 로고
    • Protonation and chloroplast membrane structure
    • Murakami, S. & Packer, L. Protonation and chloroplast membrane structure. J. Cell Biol. 47, 332-351 (1970).
    • (1970) J. Cell Biol. , vol.47 , pp. 332-351
    • Murakami, S.1    Packer, L.2


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