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532 related items for PubMed ID: 10715119

  • 1. Mutations in the putative H-channel in the cytochrome c oxidase from Rhodobacter sphaeroides show that this channel is not important for proton conduction but reveal modulation of the properties of heme a.
    Lee HM, Das TK, Rousseau DL, Mills D, Ferguson-Miller S, Gennis RB.
    Biochemistry; 2000 Mar 21; 39(11):2989-96. PubMed ID: 10715119
    [Abstract] [Full Text] [Related]

  • 2. Comparative genomics and site-directed mutagenesis support the existence of only one input channel for protons in the C-family (cbb3 oxidase) of heme-copper oxygen reductases.
    Hemp J, Han H, Roh JH, Kaplan S, Martinez TJ, Gennis RB.
    Biochemistry; 2007 Sep 04; 46(35):9963-72. PubMed ID: 17676874
    [Abstract] [Full Text] [Related]

  • 3. Role of the conserved arginine pair in proton and electron transfer in cytochrome C oxidase.
    Qian J, Mills DA, Geren L, Wang K, Hoganson CW, Schmidt B, Hiser C, Babcock GT, Durham B, Millett F, Ferguson-Miller S.
    Biochemistry; 2004 May 18; 43(19):5748-56. PubMed ID: 15134449
    [Abstract] [Full Text] [Related]

  • 4. Water chain formation and possible proton pumping routes in Rhodobacter sphaeroides cytochrome c oxidase: a molecular dynamics comparison of the wild type and R481K mutant.
    Seibold SA, Mills DA, Ferguson-Miller S, Cukier RI.
    Biochemistry; 2005 Aug 09; 44(31):10475-85. PubMed ID: 16060656
    [Abstract] [Full Text] [Related]

  • 5. A mutation in subunit I of cytochrome oxidase from Rhodobacter sphaeroides results in an increase in steady-state activity but completely eliminates proton pumping.
    Pawate AS, Morgan J, Namslauer A, Mills D, Brzezinski P, Ferguson-Miller S, Gennis RB.
    Biochemistry; 2002 Nov 12; 41(45):13417-23. PubMed ID: 12416987
    [Abstract] [Full Text] [Related]

  • 6. Properties of Arg481 mutants of the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides suggest that neither R481 nor the nearby D-propionate of heme a3 is likely to be the proton loading site of the proton pump.
    Lee HJ, Ojemyr L, Vakkasoglu A, Brzezinski P, Gennis RB.
    Biochemistry; 2009 Aug 04; 48(30):7123-31. PubMed ID: 19575527
    [Abstract] [Full Text] [Related]

  • 7. Substitutions for glutamate 101 in subunit II of cytochrome c oxidase from Rhodobacter sphaeroides result in blocking the proton-conducting K-channel.
    Tomson FL, Morgan JE, Gu G, Barquera B, Vygodina TV, Gennis RB.
    Biochemistry; 2003 Feb 18; 42(6):1711-7. PubMed ID: 12578386
    [Abstract] [Full Text] [Related]

  • 8. 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]

  • 9. Decoupling mutations in the D-channel of the aa(3)-type cytochrome c oxidase from Rhodobacter sphaeroides suggest that a continuous hydrogen-bonded chain of waters is essential for proton pumping.
    Zhu J, Han H, Pawate A, Gennis RB.
    Biochemistry; 2010 Jun 01; 49(21):4476-82. PubMed ID: 20441187
    [Abstract] [Full Text] [Related]

  • 10. An arginine to lysine mutation in the vicinity of the heme propionates affects the redox potentials of the hemes and associated electron and proton transfer in cytochrome c oxidase.
    Mills DA, Geren L, Hiser C, Schmidt B, Durham B, Millett F, Ferguson-Miller S.
    Biochemistry; 2005 Aug 09; 44(31):10457-65. PubMed ID: 16060654
    [Abstract] [Full Text] [Related]

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  • 12. Mechanism of inhibition of electron transfer by amino acid replacement K362M in a proton channel of Rhodobacter sphaeroides cytochrome c oxidase.
    Vygodina TV, Pecoraro C, Mitchell D, Gennis R, Konstantinov AA.
    Biochemistry; 1998 Mar 03; 37(9):3053-61. PubMed ID: 9485458
    [Abstract] [Full Text] [Related]

  • 13. Role of the pathway through K(I-362) in proton transfer in cytochrome c oxidase from R. sphaeroides.
    Adelroth P, Gennis RB, Brzezinski P.
    Biochemistry; 1998 Feb 24; 37(8):2470-6. PubMed ID: 9485395
    [Abstract] [Full Text] [Related]

  • 14. Mutants of the CuA site in cytochrome c oxidase of Rhodobacter sphaeroides: I. Spectral and functional properties.
    Zhen Y, Schmidt B, Kang UG, Antholine W, Ferguson-Miller S.
    Biochemistry; 2002 Feb 19; 41(7):2288-97. PubMed ID: 11841221
    [Abstract] [Full Text] [Related]

  • 15. Site-directed mutagenesis of residues lining a putative proton transfer pathway in cytochrome c oxidase from Rhodobacter sphaeroides.
    Mitchell DM, Fetter JR, Mills DA, Adelroth P, Pressler MA, Kim Y, Aasa R, Brzezinski P, Malmström BG, Alben JO, Båbcock GT, Ferguson-Miller S, Gennis RB.
    Biochemistry; 1996 Oct 08; 35(40):13089-93. PubMed ID: 8855945
    [Abstract] [Full Text] [Related]

  • 16. Transmembrane charge separation during the ferryl-oxo -> oxidized transition in a nonpumping mutant of cytochrome c oxidase.
    Siletsky SA, Pawate AS, Weiss K, Gennis RB, Konstantinov AA.
    J Biol Chem; 2004 Dec 10; 279(50):52558-65. PubMed ID: 15385565
    [Abstract] [Full Text] [Related]

  • 17. Critical structural role of R481 in cytochrome c oxidase from Rhodobacter sphaeroides.
    Egawa T, Lee HJ, Gennis RB, Yeh SR, Rousseau DL.
    Biochim Biophys Acta; 2009 Oct 10; 1787(10):1272-5. PubMed ID: 19463779
    [Abstract] [Full Text] [Related]

  • 18. Differential effects of glutamate-286 mutations in the aa(3)-type cytochrome c oxidase from Rhodobacter sphaeroides and the cytochrome bo(3) ubiquinol oxidase from Escherichia coli.
    Egawa T, Ganesan K, Lin MT, Yu MA, Hosler JP, Yeh SR, Rousseau DL, Gennis RB.
    Biochim Biophys Acta; 2011 Oct 10; 1807(10):1342-8. PubMed ID: 21684251
    [Abstract] [Full Text] [Related]

  • 19. On the role of the K-proton transfer pathway in cytochrome c oxidase.
    Brändén M, Sigurdson H, Namslauer A, Gennis RB, Adelroth P, Brzezinski P.
    Proc Natl Acad Sci U S A; 2001 Apr 24; 98(9):5013-8. PubMed ID: 11296255
    [Abstract] [Full Text] [Related]

  • 20. Substitution of lysine-362 in a putative proton-conducting channel in the cytochrome c oxidase from Rhodobacter sphaeroides blocks turnover with O2 but not with H2O2.
    Zaslavsky D, Gennis RB.
    Biochemistry; 1998 Mar 03; 37(9):3062-7. PubMed ID: 9485459
    [Abstract] [Full Text] [Related]

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