메뉴 건너뛰기




Volumn 43, Issue 2, 2004, Pages 430-436

Orientation of the g-Tensor Axes of the Rieske Subunit in the Cytochrome bc1 Complex

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONS; DIMERS; PROTEINS; SINGLE CRYSTALS;

EID: 0346463130     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi034620z     Document Type: Article
Times cited : (23)

References (36)
  • 2
    • 0016754421 scopus 로고
    • The protonmotive Q cycle: A general formulation
    • Mitchell, P. (1975) The protonmotive Q cycle: A general formulation, FEBS Lett. 59, 137-139.
    • (1975) FEBS Lett. , vol.59 , pp. 137-139
    • Mitchell, P.1
  • 3
    • 0000026361 scopus 로고
    • The mechanism of the ubiquinol:cytochrome c oxidoreductases of mitochondria and of Rhodopseudomonas sphaeroides
    • (Martonosi, A. N., Ed.), Plenum Publishing Corp., New York
    • Crofts, A. R. (1985) The mechanism of the ubiquinol:cytochrome c oxidoreductases of mitochondria and of Rhodopseudomonas sphaeroides, in The Enzymes of Biological Membranes (Martonosi, A. N., Ed.) pp 347-382, Plenum Publishing Corp., New York.
    • (1985) The Enzymes of Biological Membranes , pp. 347-382
    • Crofts, A.R.1
  • 4
    • 0002658350 scopus 로고
    • How rapid are the internal reactions of the ubiquinol: Cytochrome c2 oxidoreductase?
    • Crofts, A. R., and Wang, Z. (1989) How rapid are the internal reactions of the ubiquinol: cytochrome c2 oxidoreductase? Photosynth. Res. 22, 69-87.
    • (1989) Photosynth. Res. , vol.22 , pp. 69-87
    • Crofts, A.R.1    Wang, Z.2
  • 6
    • 0028277764 scopus 로고
    • The protonmotive Q cycle in mitochondria and bacteria
    • Brandt, U., and Trumpower, B. (1994) The protonmotive Q cycle in mitochondria and bacteria, Crit. Rev. Biochem. Mol. Biol. 29, 165-197.
    • (1994) Crit. Rev. Biochem. Mol. Biol. , vol.29 , pp. 165-197
    • Brandt, U.1    Trumpower, B.2
  • 10
    • 0034687656 scopus 로고    scopus 로고
    • The proton to electron stoichiometry of steady-state photosynthesis in living plants: A proton-pumping Q cycle is continuously engaged
    • Sacksteder, C. A., Kanazawa, A., Jacoby, M. E., and Kramer, D. M. (2000) The proton to electron stoichiometry of steady-state photosynthesis in living plants: A proton-pumping Q cycle is continuously engaged, Proc. Natl. Acad. Sci. U.S.A. 97, 14283-14288.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 14283-14288
    • Sacksteder, C.A.1    Kanazawa, A.2    Jacoby, M.E.3    Kramer, D.M.4
  • 13
    • 0014199259 scopus 로고
    • On the composition and structural organization of complex 3 of the mitochondrial electron transfer chain
    • Baum, H., Silman, H. I., Rieske, H. S., and Lipton, S. H. (1967) On the composition and structural organization of complex 3 of the mitochondrial electron transfer chain, J. Biol. Chem. 242, 4876-4887.
    • (1967) J. Biol. Chem. , vol.242 , pp. 4876-4887
    • Baum, H.1    Silman, H.I.2    Rieske, H.S.3    Lipton, S.H.4
  • 15
    • 0030001519 scopus 로고    scopus 로고
    • 1 complex by proton-gated charge transfer
    • 1 complex by proton-gated charge transfer, FEBS Lett. 387, 1-6.
    • (1996) FEBS Lett. , vol.387 , pp. 1-6
    • Brandt, U.1
  • 24
    • 0032457470 scopus 로고    scopus 로고
    • Diversity of cytochrome bc complexes: Example of the Rieske protein in green sulfur bacteria
    • Brugna, M., Albouy, D., and Nitschke, W. (1998) Diversity of cytochrome bc complexes: example of the Rieske protein in green sulfur bacteria, J. Bacteriol. 180, 3719-3723.
    • (1998) J. Bacteriol. , vol.180 , pp. 3719-3723
    • Brugna, M.1    Albouy, D.2    Nitschke, W.3
  • 25
    • 0032587408 scopus 로고    scopus 로고
    • o-site inhibitor DBMIB favours the proximal position of the chloroplast Rieske protein and induces a pK-shift of the redox-linked proton
    • o-site inhibitor DBMIB favours the proximal position of the chloroplast Rieske protein and induces a pK-shift of the redox-linked proton, FEBS Lett. 450, 245-250.
    • (1999) FEBS Lett. , vol.450 , pp. 245-250
    • Schoepp, B.1    Brugna, M.2    Riedel, A.3    Nitschke, W.4    Kramer, D.M.5
  • 26
    • 0033546142 scopus 로고    scopus 로고
    • Redox components of cytochrome bc-type enzymes in acidophilic prokaryotes. II. The Rieske protein of phylogenetically distant acidophilic organisms
    • Brugna, M., Nitschke, W., Asso, M., Guigliarelli, B., Lemesle-Meunier, D., and Schmidt, C. (1999) Redox components of cytochrome bc-type enzymes in acidophilic prokaryotes. II. The Rieske protein of phylogenetically distant acidophilic organisms, J. Biol. Chem. 274, 16766-16772.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16766-16772
    • Brugna, M.1    Nitschke, W.2    Asso, M.3    Guigliarelli, B.4    Lemesle-Meunier, D.5    Schmidt, C.6
  • 28
    • 0021970338 scopus 로고
    • A ligand-field model to describe a new class of 2Fe-2S clusters in proteins and their synthetic analogues
    • Bertrand, P., Guigliarelli, B., Gayda, J.-P., Beardwood, P., and Gibson, J. F. (1985) A ligand-field model to describe a new class of 2Fe-2S clusters in proteins and their synthetic analogues, Biochim. Biophys. Acta 831, 261-266.
    • (1985) Biochim. Biophys. Acta , vol.831 , pp. 261-266
    • Bertrand, P.1    Guigliarelli, B.2    Gayda, J.-P.3    Beardwood, P.4    Gibson, J.F.5
  • 29
    • 0029999657 scopus 로고    scopus 로고
    • Active site structure of Rieske-type proteins: Electron nuclear double resonance studies of isotopically labeled phthalate dioxygenase from Pseudomonas cepacia and Rieske protein from Rhodobacter capsulatus and molecular modeling studies of a Rieske center
    • Gurbiel, R. J., Doan, P. E., Gassner, G. T., Macke, T. J., Case, D. A., Ohnishi, T., Fee, J. A., Ballou, D. P., and Hoffman, B. M. (1996) Active site structure of Rieske-type proteins: electron nuclear double resonance studies of isotopically labeled phthalate dioxygenase from Pseudomonas cepacia and Rieske protein from Rhodobacter capsulatus and molecular modeling studies of a Rieske center, Biochemistry 35, 7834-7845.
    • (1996) Biochemistry , vol.35 , pp. 7834-7845
    • Gurbiel, R.J.1    Doan, P.E.2    Gassner, G.T.3    Macke, T.J.4    Case, D.A.5    Ohnishi, T.6    Fee, J.A.7    Ballou, D.P.8    Hoffman, B.M.9
  • 30
    • 84985816702 scopus 로고
    • Crystal point group symmetry and microscopic tensor properties in magnetic resonance spectroscopy
    • Weil, J. A., Buch, T., and Clapp, J. E. (1973) Crystal point group symmetry and microscopic tensor properties in magnetic resonance spectroscopy, Adv. Magn. Reson. 6, 183-257.
    • (1973) Adv. Magn. Reson. , vol.6 , pp. 183-257
    • Weil, J.A.1    Buch, T.2    Clapp, J.E.3
  • 31
    • 0023690621 scopus 로고
    • Studies on the effect of stigmatellin derivatives on cytochrome b and the Rieske iron-sulfur cluster of cytochrome c reductase from bovine heart mitochondria
    • Ohnishi, T., Brandt, U., and von Jagow, G. (1988) Studies on the effect of stigmatellin derivatives on cytochrome b and the Rieske iron-sulfur cluster of cytochrome c reductase from bovine heart mitochondria, Eur. J. Biochem. 176, 385-389.
    • (1988) Eur. J. Biochem. , vol.176 , pp. 385-389
    • Ohnishi, T.1    Brandt, U.2    Von Jagow, G.3
  • 32
    • 0021759095 scopus 로고
    • Purification and characterization of the Rieske iron sulfur protein from Thermus thermophilus: Evidence for a 2 Iron 2 Sulfur cluster having noncysteine ligands
    • Fee, J. A., Findling, K. L., Yoshida, T., Hille, R., Tarr, G. E., Hearshen, D. O., Dunham, W. R., Day, E. P., Kent, T. A., and Münck, E. (1984) Purification and characterization of the Rieske iron sulfur protein from Thermus thermophilus: Evidence for a 2 Iron 2 Sulfur cluster having noncysteine ligands, J. Biol. Chem. 259, 124-133.
    • (1984) J. Biol. Chem. , vol.259 , pp. 124-133
    • Fee, J.A.1    Findling, K.L.2    Yoshida, T.3    Hille, R.4    Tarr, G.E.5    Hearshen, D.O.6    Dunham, W.R.7    Day, E.P.8    Kent, T.A.9    Münck, E.10
  • 33
    • 0008876318 scopus 로고
    • An analysis of g-strain in the electron-paramagnetic-resonance of 2 [2Fe-2S] ferredoxins: Evidence for a protein rigidity model
    • Hearshen, D. O., Hagen, W. R., Sands, R. H., Grande, H. J., Crespi, H. L., Gunsalus, I. C., and Dunham, W. R. (1986) An analysis of g-strain in the electron-paramagnetic-resonance of 2 [2Fe-2S] ferredoxins: evidence for a protein rigidity model, J. Magn. Reson. 69, 440-459.
    • (1986) J. Magn. Reson. , vol.69 , pp. 440-459
    • Hearshen, D.O.1    Hagen, W.R.2    Sands, R.H.3    Grande, H.J.4    Crespi, H.L.5    Gunsalus, I.C.6    Dunham, W.R.7
  • 35
    • 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., and Smith, J. L. (1997) Biological identity and diversity in photosynthesis and respiration: structure of the lumen-side domain of the chloroplast Rieske protein, Structure 5, 1613-1625.
    • (1997) Structure , vol.5 , pp. 1613-1625
    • Carrell, C.J.1    Zhang, H.2    Cramer, W.A.3    Smith, J.L.4
  • 36
    • 0036301443 scopus 로고    scopus 로고
    • The structure of the soluble domain of an archaeal Rieske iron-sulfur protein at 1.1 Å resolution
    • Bonisch, H., Schmidt, C. L., Schafer, G., and Ladenstein, R. (2002) The structure of the soluble domain of an archaeal Rieske iron-sulfur protein at 1. 1 Å resolution, J. Mol. Biol. 319, 791-805.
    • (2002) J. Mol. Biol. , vol.319 , pp. 791-805
    • Bonisch, H.1    Schmidt, C.L.2    Schafer, G.3    Ladenstein, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.