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121 related items for PubMed ID: 8663126
1. Probing a role of subunit IV of the Escherichia coli bo-type ubiquinol oxidase by deletion and cross-linking analyses. Saiki K, Nakamura H, Mogi T, Anraku Y. J Biol Chem; 1996 Jun 28; 271(26):15336-40. PubMed ID: 8663126 [Abstract] [Full Text] [Related]
2. Exploring subunit-subunit interactions in the Escherichia coli bo-type ubiquinol oxidase by extragenic suppressor mutation analysis. Saiki K, Mogi T, Tsubaki M, Hori H, Anraku Y. J Biol Chem; 1997 Jun 06; 272(23):14721-6. PubMed ID: 9169436 [Abstract] [Full Text] [Related]
3. 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]
4. 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 [Abstract] [Full Text] [Related]
5. 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]
6. 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]
7. 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]
8. 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]
9. 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 02; 32(43):11524-9. PubMed ID: 8218219 [Abstract] [Full Text] [Related]
10. Defining the structural domain of subunit II of the heme-copper terminal oxidase using chimeric enzymes constructed from the Escherichia coli bo-type ubiquinol oxidase and the thermophilic Bacillus caa(3)-type cytochrome c oxidase. Sakamoto K, Mogi T, Noguchi S, Sone N. J Biochem; 1999 Nov 02; 126(5):934-9. PubMed ID: 10544288 [Abstract] [Full Text] [Related]
11. Modified, large-scale purification of the cytochrome o complex (bo-type oxidase) of Escherichia coli yields a two heme/one copper terminal oxidase with high specific activity. Minghetti KC, Goswitz VC, Gabriel NE, Hill JJ, Barassi CA, Georgiou CD, Chan SI, Gennis RB. Biochemistry; 1992 Aug 04; 31(30):6917-24. PubMed ID: 1322173 [Abstract] [Full Text] [Related]
12. Genetic fusion of subunits I, II, and III of the cytochrome bo ubiquinol oxidase from Escherichia coli results in a fully assembled and active enzyme. Ma J, Lemieux L, Gennis RB. Biochemistry; 1993 Aug 03; 32(30):7692-7. PubMed ID: 8394111 [Abstract] [Full Text] [Related]
14. Infrared and EPR studies on cyanide binding to the heme-copper binuclear center of cytochrome bo-type ubiquinol oxidase from Escherichia coli. Release of a CuB-cyano complex in the partially reduced state. Tsubaki M, Mogi T, Hori H, Sato-Watanabe M, Anraku Y. J Biol Chem; 1996 Feb 23; 271(8):4017-22. PubMed ID: 8626734 [Abstract] [Full Text] [Related]
15. Isolation and characterizations of quinone analogue-resistant mutants of bo-type ubiquinol oxidase from Escherichia coli. Sato-Watanabe M, Mogi T, Sakamoto K, Miyoshi H, Anraku Y. Biochemistry; 1998 Sep 15; 37(37):12744-52. PubMed ID: 9737851 [Abstract] [Full Text] [Related]
17. 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]
19. 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 08; 122(2):422-9. PubMed ID: 9378723 [Abstract] [Full Text] [Related]
20. 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] Page: [Next] [New Search]