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Volumn 42, Issue 46, 2003, Pages 13637-13645

Elimination of the Disulfide Bridge in the Rieske Iron-Sulfur Protein Allows Assembly of the [2Fe-2S] Cluster into the Rieske Protein but Damages the Ubiquinol Oxidation Site in the Cytochrome bc1 Complex

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL BONDS; ELECTRONIC STRUCTURE; IRON COMPOUNDS; OXIDATION; YEAST;

EID: 0344391926     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi035344r     Document Type: Article
Times cited : (36)

References (27)
  • 1
    • 0442331120 scopus 로고    scopus 로고
    • The structures of Rieske and Rieske-type proteins
    • Link, T. A. (1999) The structures of Rieske and Rieske-type proteins, Adv. Inorg. Chem. 47, 83-157.
    • (1999) Adv. Inorg. Chem. , vol.47 , pp. 83-157
    • Link, T.A.1
  • 2
    • 0037180385 scopus 로고    scopus 로고
    • Breaking and re-forming the disulfide bond at the high-potential, respiratory-type Rieske [2Fe-2S] center of Thermus thermophilus: Characterization of the sulfhydryl state by protein-film voltammetry
    • Zu, Y., Fee, J. A., and Hirst, J. (2002) Breaking and re-forming the disulfide bond at the high-potential, respiratory-type Rieske [2Fe-2S] center of Thermus thermophilus: Characterization of the sulfhydryl state by protein-film voltammetry, Biochemistry 41, 14054-14065.
    • (2002) Biochemistry , vol.41 , pp. 14054-14065
    • Zu, Y.1    Fee, J.A.2    Hirst, J.3
  • 3
    • 0030868605 scopus 로고    scopus 로고
    • Iron-sulfur clusters: Nature's modular, multipurpose structures
    • Beinert, H., Holm, R. H., and Münck, E. (1997) Iron-sulfur clusters: Nature's modular, multipurpose structures, Science 277, 653-659.
    • (1997) Science , vol.277 , pp. 653-659
    • Beinert, H.1    Holm, R.H.2    Münck, E.3
  • 4
    • 0034480510 scopus 로고    scopus 로고
    • A cluster exposed: Structure of the Rieske ferredoxin from biphenyl dioxygenase and the redox properties of Rieske Fe-S proteins
    • Colbert, C. L., Couture, M. M.-J., Eltis, L. D., and Bolin, J. T. (2000) A cluster exposed: Structure of the Rieske ferredoxin from biphenyl dioxygenase and the redox properties of Rieske Fe-S proteins, Structure 8, 1267-1278.
    • (2000) Structure , vol.8 , pp. 1267-1278
    • Colbert, C.L.1    Couture, M.M.-J.2    Eltis, L.D.3    Bolin, J.T.4
  • 5
    • 0032502711 scopus 로고    scopus 로고
    • Alteration of the midpoint potential and catalytic activity of the Rieske iron-sulfur protein by changes of amino acids forming hydrogen bonds to the iron-sulfur cluster
    • Denke, E., Merbitz-Zahradnik, T., Hatzfeld, O. M., Snyder, C., Link, T. A., and Trumpower, B. L. (1998) Alteration of the midpoint potential and catalytic activity of the Rieske iron-sulfur protein by changes of amino acids forming hydrogen bonds to the iron-sulfur cluster, J. Biol. Chem. 273, 9085-9093.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9085-9093
    • Denke, E.1    Merbitz-Zahradnik, T.2    Hatzfeld, O.M.3    Snyder, C.4    Link, T.A.5    Trumpower, B.L.6
  • 7
    • 0034720770 scopus 로고    scopus 로고
    • Specific mutagenesis of the Rieske iron-sulfur protein in Rhodobacter sphaeroides shows that both the thermodynamic gradient and the pK of the oxidized form determine the rate of quinol oxidation by the bcl be, complex
    • Guergova-Kuras, M., Kuras, R., Ugulava, N., Hadad, I., and Crofts, A. R. (2000) Specific mutagenesis of the Rieske iron-sulfur protein in Rhodobacter sphaeroides shows that both the thermodynamic gradient and the pK of the oxidized form determine the rate of quinol oxidation by the bcl be, complex, Biochemistry 39, 7436-7444.
    • (2000) Biochemistry , vol.39 , pp. 7436-7444
    • Guergova-Kuras, M.1    Kuras, R.2    Ugulava, N.3    Hadad, I.4    Crofts, A.R.5
  • 11
    • 0024515576 scopus 로고
    • Mutational analysis of the mitochondrial Rieske iron-sulfur protein of Saccharomyces cerevisiae I. Construction of a RIP1 deletion strain and isolation of temperature sensitive mutants
    • Beckmann, J. D., Ljungdahl, P. O., and Trumpower, B. L. (1989) Mutational analysis of the mitochondrial Rieske iron-sulfur protein of Saccharomyces cerevisiae I. Construction of a RIP1 deletion strain and isolation of temperature sensitive mutants, J. Biol. Chem. 264, 3713-3722.
    • (1989) J. Biol. Chem. , vol.264 , pp. 3713-3722
    • Beckmann, J.D.1    Ljungdahl, P.O.2    Trumpower, B.L.3
  • 14
    • 0032321683 scopus 로고    scopus 로고
    • 1 complexes containing site-directed mutants of the Rieske iron-sulfur protein
    • 1 complexes containing site-directed mutants of the Rieske iron-sulfur protein, Biochim. Biophys. Acta 1365, 125-134.
    • (1998) Biochim. Biophys. Acta , vol.1365 , pp. 125-134
    • Snyder, C.1    Trumpower, B.L.2
  • 15
    • 0029864555 scopus 로고    scopus 로고
    • Dissociation of import of the Rieske iron-sulfur protein into Saccharomyces cerevisiae mitochondria from proteolytic processing of the presequence
    • Nett, J. H., and Trumpower, B. L. (1996) Dissociation of import of the Rieske iron-sulfur protein into Saccharomyces cerevisiae mitochondria from proteolytic processing of the presequence, J. Biol. Chem. 271, 26713-26716.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26713-26716
    • Nett, J.H.1    Trumpower, B.L.2
  • 16
    • 0027191299 scopus 로고
    • Steady-state kinetics of ubiquinol cytochrome c reductase in Saccharomyces cerevisiae mitochondria: Effects of fluidity changes obtained by different growth temperatures
    • Cavazzoni, M., Svobodova, J., Desantis, A., Fato, R., and Lenaz, G. (1993) Steady-state kinetics of ubiquinol cytochrome c reductase in Saccharomyces cerevisiae mitochondria: Effects of fluidity changes obtained by different growth temperatures, Arch. Biochem. Biophys. 303, 246-254.
    • (1993) Arch. Biochem. Biophys. , vol.303 , pp. 246-254
    • Cavazzoni, M.1    Svobodova, J.2    Desantis, A.3    Fato, R.4    Lenaz, G.5
  • 18
    • 0025884019 scopus 로고
    • 1 Complex of Iron-Sulfur Protein Lacking the Iron-Sulfur Cluster
    • 1 Complex of Iron-Sulfur Protein Lacking the Iron-Sulfur Cluster, J. Biol. Chem. 266, 22485-22492.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22485-22492
    • Graham, L.1    Trumpower, B.L.2
  • 19
    • 0033515655 scopus 로고    scopus 로고
    • 1 complex of Saccharomyces cerevisiae
    • 1 complex of Saccharomyces cerevisiae, J. Biol. Chem. 274, 9253-9257.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9253-9257
    • Nett, J.1    Trumpower, B.L.2
  • 21
    • 0015911233 scopus 로고
    • The mechanism of action of the respiratory inhibitor, antimycin
    • Slater, E. C. (1973) The mechanism of action of the respiratory inhibitor, antimycin, Biochim. Biophys. Acta 301, 129-154.
    • (1973) Biochim. Biophys. Acta , vol.301 , pp. 129-154
    • Slater, E.C.1
  • 22
    • 0023109105 scopus 로고
    • The circular-dichroic properties of the Rieske iron-sulfur protein in the mitochondrial ubiquinol: Cytochrome c reductase
    • Degli-Esposti, M., Ballester, F., Solaini, G., and Lenaz, G (1987) The circular-dichroic properties of the Rieske iron-sulfur protein in the mitochondrial ubiquinol: cytochrome c reductase, Biochem. J. 241, 285-290.
    • (1987) Biochem. J. , vol.241 , pp. 285-290
    • Degli-Esposti, M.1    Ballester, F.2    Solaini, G.3    Lenaz, G.4
  • 23
    • 0034660152 scopus 로고    scopus 로고
    • 1 complex from the yeast Saccharomyces cerevisiae cocrystallized with an antibody Fv fragment
    • 1 complex from the yeast Saccharomyces cerevisiae cocrystallized with an antibody Fv fragment, Structure 8, 669-684.
    • (2000) Structure , vol.8 , pp. 669-684
    • Hunte, C.1    Koepke, J.2    Lange, C.3    Rossmanith, T.4    Michel, H.5
  • 25
    • 0016213178 scopus 로고
    • On the interpretation of electron paramagnetic resonance spectra of binuclear iron-sulfur proteins
    • Blumberg, W. E., and Peisach, J. (1974) On the interpretation of electron paramagnetic resonance spectra of binuclear iron-sulfur proteins, Arch. Biochem. Biophys. 162, 502-512.
    • (1974) Arch. Biochem. Biophys. , vol.162 , pp. 502-512
    • Blumberg, W.E.1    Peisach, J.2


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