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Journal Abstract Search
164 related items for PubMed ID: 8399242
1. Substitution of asparagine for aspartate-135 in subunit I of the cytochrome bo ubiquinol oxidase of Escherichia coli eliminates proton-pumping activity. Thomas JW, Puustinen A, Alben JO, Gennis RB, Wikström M. Biochemistry; 1993 Oct 12; 32(40):10923-8. PubMed ID: 8399242 [Abstract] [Full Text] [Related]
2. Proton transfer in cytochrome bo3 ubiquinol oxidase of Escherichia coli: second-site mutations in subunit I that restore proton pumping in the mutant Asp135-->Asn. Garcia-Horsman JA, Puustinen A, Gennis RB, Wikström M. Biochemistry; 1995 Apr 04; 34(13):4428-33. PubMed ID: 7703256 [Abstract] [Full Text] [Related]
3. 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]
4. 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]
5. Insight into the active-site structure and function of cytochrome oxidase by analysis of site-directed mutants of bacterial cytochrome aa3 and cytochrome bo. Hosler JP, Ferguson-Miller S, Calhoun MW, Thomas JW, Hill J, Lemieux L, Ma J, Georgiou C, Fetter J, Shapleigh J. J Bioenerg Biomembr; 1993 Apr 06; 25(2):121-36. PubMed ID: 8389745 [Abstract] [Full Text] [Related]
6. 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]
12. Direct evidence for the protonation of aspartate-75, proposed to be at a quinol binding site, upon reduction of cytochrome bo3 from Escherichia coli. Hellwig P, Barquera B, Gennis RB. Biochemistry; 2001 Jan 30; 40(4):1077-82. PubMed ID: 11170431 [Abstract] [Full Text] [Related]
13. 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]
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. 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 26; 126(5):934-9. PubMed ID: 10544288 [Abstract] [Full Text] [Related]
16. 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 26; 122(2):422-9. PubMed ID: 9378723 [Abstract] [Full Text] [Related]
17. 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]
18. 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]