BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

557 related articles for article (PubMed ID: 9305957)

  • 1. Conserved nonliganding residues of the Rhodobacter capsulatus Rieske iron-sulfur protein of the bc1 complex are essential for protein structure, properties of the [2Fe-2S] cluster, and communication with the quinone pool.
    Liebl U; Sled V; Brasseur G; Ohnishi T; Daldal F
    Biochemistry; 1997 Sep; 36(39):11675-84. PubMed ID: 9305957
    [TBL] [Abstract][Full Text] [Related]  

  • 2. The amino-terminal portion of the Rieske iron-sulfur protein contributes to the ubihydroquinone oxidation site catalysis of the Rhodobacter capsulatus bc1 complex.
    Brasseur G; Sled V; Liebl U; Ohnishi T; Daldal F
    Biochemistry; 1997 Sep; 36(39):11685-96. PubMed ID: 9305958
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Potential ligands to the [2Fe-2S] Rieske cluster of the cytochrome bc1 complex of Rhodobacter capsulatus probed by site-directed mutagenesis.
    Davidson E; Ohnishi T; Atta-Asafo-Adjei E; Daldal F
    Biochemistry; 1992 Apr; 31(13):3342-51. PubMed ID: 1313292
    [TBL] [Abstract][Full Text] [Related]  

  • 4. Cytochrome bc1 complex [2Fe-2S] cluster and its interaction with ubiquinone and ubihydroquinone at the Qo site: a double-occupancy Qo site model.
    Ding H; Robertson DE; Daldal F; Dutton PL
    Biochemistry; 1992 Mar; 31(12):3144-58. PubMed ID: 1313287
    [TBL] [Abstract][Full Text] [Related]  

  • 5. 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 RJ; Doan PE; Gassner GT; Macke TJ; Case DA; Ohnishi T; Fee JA; Ballou DP; Hoffman BM
    Biochemistry; 1996 Jun; 35(24):7834-45. PubMed ID: 8672484
    [TBL] [Abstract][Full Text] [Related]  

  • 6. Isolation and characterization of a two-subunit cytochrome b-c1 subcomplex from Rhodobacter capsulatus and reconstitution of its ubihydroquinone oxidation (Qo) site with purified Fe-S protein subunit.
    Valkova-Valchanova MB; Saribas AS; Gibney BR; Dutton PL; Daldal F
    Biochemistry; 1998 Nov; 37(46):16242-51. PubMed ID: 9819216
    [TBL] [Abstract][Full Text] [Related]  

  • 7. Mutational analysis of residues forming hydrogen bonds in the Rieske [2Fe-2S] cluster of the cytochrome bc1 complex in Paracoccus denitrificans.
    Schröter T; Hatzfeld OM; Gemeinhardt S; Korn M; Friedrich T; Ludwig B; Link TA
    Eur J Biochem; 1998 Jul; 255(1):100-6. PubMed ID: 9692907
    [TBL] [Abstract][Full Text] [Related]  

  • 8. Rhodobacter capsulatus mutants lacking the Rieske FeS protein form a stable cytochrome bc1 subcomplex with an intact quinone reduction site.
    Davidson E; Ohnishi T; Tokito M; Daldal F
    Biochemistry; 1992 Apr; 31(13):3351-8. PubMed ID: 1313293
    [TBL] [Abstract][Full Text] [Related]  

  • 9. Structure of a water soluble fragment of the 'Rieske' iron-sulfur protein of the bovine heart mitochondrial cytochrome bc1 complex determined by MAD phasing at 1.5 A resolution.
    Iwata S; Saynovits M; Link TA; Michel H
    Structure; 1996 May; 4(5):567-79. PubMed ID: 8736555
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Interactions between the cytochrome b, cytochrome c1, and Fe-S protein subunits at the ubihydroquinone oxidation site of the bc1 complex of Rhodobacter capsulatus.
    Saribaş AS; Valkova-Valchanova M; Tokito MK; Zhang Z; Berry EA; Daldal F
    Biochemistry; 1998 Jun; 37(22):8105-14. PubMed ID: 9609705
    [TBL] [Abstract][Full Text] [Related]  

  • 11. The raised midpoint potential of the [2Fe2S] cluster of cytochrome bc1 is mediated by both the Qo site occupants and the head domain position of the Fe-S protein subunit.
    Cooley JW; Roberts AG; Bowman MK; Kramer DM; Daldal F
    Biochemistry; 2004 Mar; 43(8):2217-27. PubMed ID: 14979718
    [TBL] [Abstract][Full Text] [Related]  

  • 12. 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.
    Merbitz-Zahradnik T; Zwicker K; Nett JH; Link TA; Trumpower BL
    Biochemistry; 2003 Nov; 42(46):13637-45. PubMed ID: 14622010
    [TBL] [Abstract][Full Text] [Related]  

  • 13. The [2Fe-2S] cluster E(m) as an indicator of the iron-sulfur subunit position in the ubihydroquinone oxidation site of the cytochrome bc1 complex.
    Darrouzet E; Valkova-Valchanova M; Daldal F
    J Biol Chem; 2002 Feb; 277(5):3464-70. PubMed ID: 11707448
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Plasmon waveguide resonance spectroscopic evidence for differential binding of oxidized and reduced Rhodobacter capsulatus cytochrome c2 to the cytochrome bc1 complex mediated by the conformation of the Rieske iron-sulfur protein.
    Devanathan S; Salamon Z; Tollin G; Fitch JC; Meyer TE; Berry EA; Cusanovich MA
    Biochemistry; 2007 Jun; 46(24):7138-45. PubMed ID: 17516628
    [TBL] [Abstract][Full Text] [Related]  

  • 15. Functional flexibility of electron flow between quinol oxidation Q
    Borek A; Ekiert R; Osyczka A
    Biochim Biophys Acta Bioenerg; 2018 Sep; 1859(9):754-761. PubMed ID: 29705394
    [TBL] [Abstract][Full Text] [Related]  

  • 16. Effect of H bond removal and changes in the position of the iron-sulphur head domain on the spin-lattice relaxation properties of the [2Fe-2S](2+) Rieske cluster in cytochrome bc(1).
    Sarewicz M; Dutka M; Pietras R; Borek A; Osyczka A
    Phys Chem Chem Phys; 2015 Oct; 17(38):25297-308. PubMed ID: 26355649
    [TBL] [Abstract][Full Text] [Related]  

  • 17. Binding dynamics at the quinone reduction (Qi) site influence the equilibrium interactions of the iron sulfur protein and hydroquinone oxidation (Qo) site of the cytochrome bc1 complex.
    Cooley JW; Ohnishi T; Daldal F
    Biochemistry; 2005 Aug; 44(31):10520-32. PubMed ID: 16060661
    [TBL] [Abstract][Full Text] [Related]  

  • 18. The iron-sulfur cluster of the Rieske iron-sulfur protein functions as a proton-exiting gate in the cytochrome bc(1) complex.
    Gurung B; Yu L; Xia D; Yu CA
    J Biol Chem; 2005 Jul; 280(26):24895-902. PubMed ID: 15878858
    [TBL] [Abstract][Full Text] [Related]  

  • 19. Substitutions at position 146 of cytochrome b affect drastically the properties of heme bL and the Qo site of Rhodobacter capsulatus cytochrome bc1 complex.
    Saribaş AS; Ding H; Dutton PL; Daldal F
    Biochim Biophys Acta; 1997 Mar; 1319(1):99-108. PubMed ID: 9107318
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Site-directed mutations of conserved residues of the Rieske iron-sulfur subunit of the cytochrome bc1 complex of Rhodobacter sphaeroides blocking or impairing quinol oxidation.
    Van Doren SR; Gennis RB; Barquera B; Crofts AR
    Biochemistry; 1993 Aug; 32(32):8083-91. PubMed ID: 8394124
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 28.