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246 related items for PubMed ID: 8241181

  • 1. 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 07; 32(48):13254-61. PubMed ID: 8241181
    [Abstract] [Full Text] [Related]

  • 2. Identity of the axial ligand of the high-spin heme in cytochrome oxidase: spectroscopic characterization of mutants in the bo-type oxidase of Escherichia coli and the aa3-type oxidase of Rhodobacter sphaeroides.
    Calhoun MW, Thomas JW, Hill JJ, Hosler JP, Shapleigh JP, Tecklenburg MM, Ferguson-Miller S, Babcock GT, Alben JO, Gennis RB.
    Biochemistry; 1993 Oct 12; 32(40):10905-11. PubMed ID: 8399240
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  • 4. 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 19; 32(41):11173-80. PubMed ID: 8218180
    [Abstract] [Full Text] [Related]

  • 5. 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 24; 31(46):11435-40. PubMed ID: 1332759
    [Abstract] [Full Text] [Related]

  • 6. Site-directed mutagenesis of residues within helix VI in subunit I of the cytochrome bo3 ubiquinol oxidase from Escherichia coli suggests that tyrosine 288 may be a CuB ligand.
    Thomas JW, Calhoun MW, Lemieux LJ, Puustinen A, Wikström M, Alben JO, Gennis RB.
    Biochemistry; 1994 Nov 08; 33(44):13013-21. PubMed ID: 7947706
    [Abstract] [Full Text] [Related]

  • 7. 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 10; 37(6):1632-9. PubMed ID: 9484234
    [Abstract] [Full Text] [Related]

  • 8. 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 25; 267(3):2096-104. PubMed ID: 1309808
    [Abstract] [Full Text] [Related]

  • 9. 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 25; 122(2):422-9. PubMed ID: 9378723
    [Abstract] [Full Text] [Related]

  • 10. Determination of the ligands of the low spin heme of the cytochrome o ubiquinol oxidase complex using site-directed mutagenesis.
    Lemieux LJ, Calhoun MW, Thomas JW, Ingledew WJ, Gennis RB.
    J Biol Chem; 1992 Jan 25; 267(3):2105-13. PubMed ID: 1309809
    [Abstract] [Full Text] [Related]

  • 11. 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 09; 269(49):30861-8. PubMed ID: 7983018
    [Abstract] [Full Text] [Related]

  • 12. 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 22; 269(16):11912-20. PubMed ID: 8163490
    [Abstract] [Full Text] [Related]

  • 13. Spectroscopic and genetic evidence for two heme-Cu-containing oxidases in Rhodobacter sphaeroides.
    Shapleigh JP, Hill JJ, Alben JO, Gennis RB.
    J Bacteriol; 1992 Apr 22; 174(7):2338-43. PubMed ID: 1313003
    [Abstract] [Full Text] [Related]

  • 14. Time-resolved step-scan Fourier transform infrared spectroscopy of the CO adducts of bovine cytochrome c oxidase and of cytochrome bo(3) from Escherichia coli.
    Bailey JA, Tomson FL, Mecklenburg SL, MacDonald GM, Katsonouri A, Puustinen A, Gennis RB, Woodruff WH, Dyer RB.
    Biochemistry; 2002 Feb 26; 41(8):2675-83. PubMed ID: 11851414
    [Abstract] [Full Text] [Related]

  • 15. Strong-field and integral spin-ligand complexes of the cytochrome bo quinol oxidase in Escherichia coli membrane preparations.
    Calhoun MW, Gennis RB, Ingledew WJ, Salerno JC.
    Biochim Biophys Acta; 1994 May 18; 1206(1):143-54. PubMed ID: 8186244
    [Abstract] [Full Text] [Related]

  • 16. 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 16; 38(46):15150-6. PubMed ID: 10563797
    [Abstract] [Full Text] [Related]

  • 17. 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 17; 34(41):13491-501. PubMed ID: 7577938
    [Abstract] [Full Text] [Related]

  • 18. 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 24; 279(52):53980-7. PubMed ID: 15475358
    [Abstract] [Full Text] [Related]

  • 19. Polar residues in helix VIII of subunit I of cytochrome c oxidase influence the activity and the structure of the active site.
    Hosler JP, Shapleigh JP, Mitchell DM, Kim Y, Pressler MA, Georgiou C, Babcock GT, Alben JO, Ferguson-Miller S, Gennis RB.
    Biochemistry; 1996 Aug 20; 35(33):10776-83. PubMed ID: 8718868
    [Abstract] [Full Text] [Related]

  • 20. Location of heme axial ligands in the cytochrome d terminal oxidase complex of Escherichia coli determined by site-directed mutagenesis.
    Fang H, Lin RJ, Gennis RB.
    J Biol Chem; 1989 May 15; 264(14):8026-32. PubMed ID: 2656671
    [Abstract] [Full Text] [Related]

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