These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

205 related articles for article (PubMed ID: 10858292)

  • 1. 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 bc(1) complex.
    Guergova-Kuras M; Kuras R; Ugulava N; Hadad I; Crofts AR
    Biochemistry; 2000 Jun; 39(25):7436-44. PubMed ID: 10858292
    [TBL] [Abstract][Full Text] [Related]  

  • 2. 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]  

  • 3. Proton-coupled electron transfer at the Qo-site of the bc1 complex controls the rate of ubihydroquinone oxidation.
    Crofts AR
    Biochim Biophys Acta; 2004 Apr; 1655(1-3):77-92. PubMed ID: 15100020
    [TBL] [Abstract][Full Text] [Related]  

  • 4. CD-monitored redox titration of the Rieske Fe-S protein of Rhodobacter sphaeroides: pH dependence of the midpoint potential in isolated bc1 complex and in membranes.
    Ugulava NB; Crofts AR
    FEBS Lett; 1998 Dec; 440(3):409-13. PubMed ID: 9872412
    [TBL] [Abstract][Full Text] [Related]  

  • 5. Modulation of the midpoint potential of the [2Fe-2S] Rieske iron sulfur center by Qo occupants in the bc1 complex.
    Shinkarev VP; Kolling DR; Miller TJ; Crofts AR
    Biochemistry; 2002 Dec; 41(48):14372-82. PubMed ID: 12450404
    [TBL] [Abstract][Full Text] [Related]  

  • 6. Modifications of protein environment of the [2Fe-2S] cluster of the bc1 complex: effects on the biophysical properties of the rieske iron-sulfur protein and on the kinetics of the complex.
    Lhee S; Kolling DR; Nair SK; Dikanov SA; Crofts AR
    J Biol Chem; 2010 Mar; 285(12):9233-48. PubMed ID: 20023300
    [TBL] [Abstract][Full Text] [Related]  

  • 7. 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]  

  • 8. Flexibility of the neck region of the rieske iron-sulfur protein is functionally important in the cytochrome bc1 complex.
    Tian H; Yu L; Mather MW; Yu CA
    J Biol Chem; 1998 Oct; 273(43):27953-9. PubMed ID: 9774409
    [TBL] [Abstract][Full Text] [Related]  

  • 9. Pathways for proton release during ubihydroquinone oxidation by the bc(1) complex.
    Crofts AR; Hong S; Ugulava N; Barquera B; Gennis R; Guergova-Kuras M; Berry EA
    Proc Natl Acad Sci U S A; 1999 Aug; 96(18):10021-6. PubMed ID: 10468555
    [TBL] [Abstract][Full Text] [Related]  

  • 10. The extra fragment of the iron-sulfur protein (residues 96-107) of Rhodobacter sphaeroides cytochrome bc1 complex is required for protein stability.
    Xiao K; Liu X; Yu CA; Yu L
    Biochemistry; 2004 Feb; 43(6):1488-95. PubMed ID: 14769025
    [TBL] [Abstract][Full Text] [Related]  

  • 11. Formation of engineered intersubunit disulfide bond in cytochrome bc1 complex disrupts electron transfer activity in the complex.
    Ma HW; Yang S; Yu L; Yu CA
    Biochim Biophys Acta; 2008 Mar; 1777(3):317-26. PubMed ID: 18258178
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Mitochondrial disease-related mutations at the cytochrome b-iron-sulfur protein (ISP) interface: Molecular effects on the large-scale motion of ISP and superoxide generation studied in Rhodobacter capsulatus cytochrome bc1.
    Ekiert R; Borek A; Kuleta P; Czernek J; Osyczka A
    Biochim Biophys Acta; 2016 Aug; 1857(8):1102-1110. PubMed ID: 27032290
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Negatively charged residues and hydrogen bonds tune the ligand histidine pKa values of Rieske iron-sulfur proteins.
    Klingen AR; Ullmann GM
    Biochemistry; 2004 Oct; 43(39):12383-9. PubMed ID: 15449929
    [TBL] [Abstract][Full Text] [Related]  

  • 14. 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]  

  • 15. Tight binding of inhibitors to bovine bc1 complex is independent of the Rieske protein redox state. Consequences for semiquinone stabilization in the quinol oxidation site.
    Covián R; Pardo JP; Moreno-Sánchez R
    J Biol Chem; 2002 Dec; 277(50):48449-55. PubMed ID: 12364330
    [TBL] [Abstract][Full Text] [Related]  

  • 16. Proton-coupled electron transfer at the Q(o) site: what type of mechanism can account for the high activation barrier?
    Crofts AR; Guergova-Kuras M; Kuras R; Ugulava N; Li J; Hong S
    Biochim Biophys Acta; 2000 Aug; 1459(2-3):456-66. PubMed ID: 11004463
    [TBL] [Abstract][Full Text] [Related]  

  • 17. 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]  

  • 18. 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]  

  • 19. Confirmation of the involvement of protein domain movement during the catalytic cycle of the cytochrome bc1 complex by the formation of an intersubunit disulfide bond between cytochrome b and the iron-sulfur protein.
    Xiao K; Yu L; Yu CA
    J Biol Chem; 2000 Dec; 275(49):38597-604. PubMed ID: 10978350
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Physicochemical aspects of the movement of the rieske iron sulfur protein during quinol oxidation by the bc(1) complex from mitochondria and photosynthetic bacteria.
    Crofts AR; Hong S; Zhang Z; Berry EA
    Biochemistry; 1999 Nov; 38(48):15827-39. PubMed ID: 10625447
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 11.