BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

270 related articles for article (PubMed ID: 9378723)

  • 1. Substitutions of charged amino acid residues conserved in subunit I perturb the redox metal centers of the Escherichia coli bo-type ubiquinol oxidase.
    Kawasaki M; Mogi T; Anraku Y
    J Biochem; 1997 Aug; 122(2):422-9. PubMed ID: 9378723
    [TBL] [Abstract][Full Text] [Related]  

  • 2. Substitutions of conserved aromatic amino acid residues in subunit I perturb the metal centers of the Escherichia coli bo-type ubiquinol oxidase.
    Mogi T; Minagawa J; Hirano T; Sato-Watanabe M; Tsubaki M; Uno T; Hori H; Nakamura H; Nishimura Y; Anraku Y
    Biochemistry; 1998 Feb; 37(6):1632-9. PubMed ID: 9484234
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Effects of subunit I mutations on redox-linked conformational changes of the Escherichia coli bo-type ubiquinol oxidase revealed by Fourier-transform infrared spectroscopy.
    Yamazaki Y; Kandori H; Mogi T
    J Biochem; 1999 Jul; 126(1):194-9. PubMed ID: 10393339
    [TBL] [Abstract][Full Text] [Related]  

  • 4. Identification of heme and copper ligands in subunit I of the cytochrome bo complex in Escherichia coli.
    Minagawa J; Mogi T; Gennis RB; Anraku Y
    J Biol Chem; 1992 Jan; 267(3):2096-104. PubMed ID: 1309808
    [TBL] [Abstract][Full Text] [Related]  

  • 5. Molecular structure of redox metal centers of the cytochrome bo complex from Escherichia coli. Spectroscopic characterizations of the subunit I histidine mutant oxidases.
    Tsubaki M; Mogi T; Hori H; Hirota S; Ogura T; Kitagawa T; Anraku Y
    J Biol Chem; 1994 Dec; 269(49):30861-8. PubMed ID: 7983018
    [TBL] [Abstract][Full Text] [Related]  

  • 6. Assignment and functional roles of the cyoABCDE gene products required for the Escherichia coli bo-type quinol oxidase.
    Nakamura H; Saiki K; Mogi T; Anraku Y
    J Biochem; 1997 Aug; 122(2):415-21. PubMed ID: 9378722
    [TBL] [Abstract][Full Text] [Related]  

  • 7. Resonance Raman and Fourier transform infrared studies on the subunit I histidine mutants of the cytochrome bo complex in Escherichia coli. Molecular structure of redox metal centers.
    Uno T; Mogi T; Tsubaki M; Nishimura Y; Anraku Y
    J Biol Chem; 1994 Apr; 269(16):11912-20. PubMed ID: 8163490
    [TBL] [Abstract][Full Text] [Related]  

  • 8. Identification of the functional domains in heme O synthase. Site-directed mutagenesis studies on the cyoE gene of the cytochrome bo operon in Escherichia coli.
    Saiki K; Mogi T; Hori H; Tsubaki M; Anraku Y
    J Biol Chem; 1993 Dec; 268(36):26927-34. PubMed ID: 8262927
    [TBL] [Abstract][Full Text] [Related]  

  • 9. Glutamate-89 in subunit II of cytochrome bo3 from Escherichia coli is required for the function of the heme-copper oxidase.
    Ma J; Tsatsos PH; Zaslavsky D; Barquera B; Thomas JW; Katsonouri A; Puustinen A; Wikström M; Brzezinski P; Alben JO; Gennis RB
    Biochemistry; 1999 Nov; 38(46):15150-6. PubMed ID: 10563797
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Site-directed mutagenesis of highly conserved residues in helix VIII of subunit I of the cytochrome bo ubiquinol oxidase from Escherichia coli: an amphipathic transmembrane helix that may be important in conveying protons to the binuclear center.
    Thomas JW; Lemieux LJ; Alben JO; Gennis RB
    Biochemistry; 1993 Oct; 32(41):11173-80. PubMed ID: 8218180
    [TBL] [Abstract][Full Text] [Related]  

  • 11. Spectroscopic characterization of mutants supports the assignment of histidine-419 as the axial ligand of heme o in the binuclear center of the cytochrome bo ubiquinol oxidase from Escherichia coli.
    Calhoun MW; Lemieux LJ; Thomas JW; Hill JJ; Goswitz VC; Alben JO; Gennis RB
    Biochemistry; 1993 Dec; 32(48):13254-61. PubMed ID: 8241181
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Molecular structure of a heme-copper redox center of the Escherichia coli ubiquinol oxidase: evidence and model.
    Mogi T; Nakamura H; Anraku Y
    J Biochem; 1994 Sep; 116(3):471-7. PubMed ID: 7852262
    [TBL] [Abstract][Full Text] [Related]  

  • 13. A novel chloride-binding site modulates the heme-copper binuclear center of the Escherichia coli bo-type ubiquinol oxidase.
    Hirano T; Mogi T; Tsubaki M; Hori H; Orii Y; Anraku Y
    J Biochem; 1997 Aug; 122(2):430-7. PubMed ID: 9378724
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Arginine 391 in subunit I of the cytochrome bd quinol oxidase from Escherichia coli stabilizes the reduced form of the hemes and is essential for quinol oxidase activity.
    Zhang J; Hellwig P; Osborne JP; Gennis RB
    J Biol Chem; 2004 Dec; 279(52):53980-7. PubMed ID: 15475358
    [TBL] [Abstract][Full Text] [Related]  

  • 15. Site-directed mutation of the highly conserved region near the Q-loop of the cytochrome bd quinol oxidase from Escherichia coli specifically perturbs heme b595.
    Zhang J; Hellwig P; Osborne JP; Huang HW; Moënne-Loccoz P; Konstantinov AA; Gennis RB
    Biochemistry; 2001 Jul; 40(29):8548-56. PubMed ID: 11456494
    [TBL] [Abstract][Full Text] [Related]  

  • 16. Glutamate 107 in subunit I of the cytochrome bd quinol oxidase from Escherichia coli is protonated and near the heme d/heme b595 binuclear center.
    Yang K; Zhang J; Vakkasoglu AS; Hielscher R; Osborne JP; Hemp J; Miyoshi H; Hellwig P; Gennis RB
    Biochemistry; 2007 Mar; 46(11):3270-8. PubMed ID: 17305364
    [TBL] [Abstract][Full Text] [Related]  

  • 17. Structure of the heme-copper binuclear center of the cytochrome bo complex of Escherichia coli: EPR and Fourier transform infrared spectroscopic studies.
    Tsubaki M; Mogi T; Anraku Y; Hori H
    Biochemistry; 1993 Jun; 32(23):6065-72. PubMed ID: 8389588
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Demonstration by FTIR that the bo-type ubiquinol oxidase of Escherichia coli contains a heme-copper binuclear center similar to that in cytochrome c oxidase and that proper assembly of the binuclear center requires the cyoE gene product.
    Hill J; Goswitz VC; Calhoun M; Garcia-Horsman JA; Lemieux L; Alben JO; Gennis RB
    Biochemistry; 1992 Nov; 31(46):11435-40. PubMed ID: 1332759
    [TBL] [Abstract][Full Text] [Related]  

  • 19. Site-directed mutants of the cytochrome bo ubiquinol oxidase of Escherichia coli: amino acid substitutions for two histidines that are putative CuB ligands.
    Calhoun MW; Hill JJ; Lemieux LJ; Ingledew WJ; Alben JO; Gennis RB
    Biochemistry; 1993 Nov; 32(43):11524-9. PubMed ID: 8218219
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Methionine-393 is an axial ligand of the heme b558 component of the cytochrome bd ubiquinol oxidase from Escherichia coli.
    Kaysser TM; Ghaim JB; Georgiou C; Gennis RB
    Biochemistry; 1995 Oct; 34(41):13491-501. PubMed ID: 7577938
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 14.