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432 related items for PubMed ID: 17305364

  • 1. 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 20; 46(11):3270-8. PubMed ID: 17305364
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  • 2. Glutamates 99 and 107 in transmembrane helix III of subunit I of cytochrome bd are critical for binding of the heme b595-d binuclear center and enzyme activity.
    Mogi T, Endou S, Akimoto S, Morimoto-Tadokoro M, Miyoshi H.
    Biochemistry; 2006 Dec 26; 45(51):15785-92. PubMed ID: 17176101
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  • 3. Glutamate 107 in subunit I of cytochrome bd from Escherichia coli is part of a transmembrane intraprotein pathway conducting protons from the cytoplasm to the heme b595/heme d active site.
    Borisov VB, Belevich I, Bloch DA, Mogi T, Verkhovsky MI.
    Biochemistry; 2008 Jul 29; 47(30):7907-14. PubMed ID: 18597483
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  • 4. Functional importance of Glutamate-445 and Glutamate-99 in proton-coupled electron transfer during oxygen reduction by cytochrome bd from Escherichia coli.
    Murali R, Gennis RB.
    Biochim Biophys Acta Bioenerg; 2018 Aug 29; 1859(8):577-590. PubMed ID: 29719208
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  • 6. 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 24; 40(29):8548-56. PubMed ID: 11456494
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  • 7. Probing the haem d-binding site in cytochrome bd quinol oxidase by site-directed mutagenesis.
    Mogi T.
    J Biochem; 2009 Jun 24; 145(6):763-70. PubMed ID: 19254926
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  • 9. Fourier-transform infrared studies on conformation changes in bd-type ubiquinol oxidase from Escherichia coli upon photoreduction of the redox metal centers.
    Yamazaki Y, Kandori H, Mogi T.
    J Biochem; 1999 Jun 24; 125(6):1131-6. PubMed ID: 10348916
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  • 10. Sequence analysis of cytochrome bd oxidase suggests a revised topology for subunit I.
    Osborne JP, Gennis RB.
    Biochim Biophys Acta; 1999 Jan 27; 1410(1):32-50. PubMed ID: 10076013
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  • 11. Probing the ubiquinol-binding site in cytochrome bd by site-directed mutagenesis.
    Mogi T, Akimoto S, Endou S, Watanabe-Nakayama T, Mizuochi-Asai E, Miyoshi H.
    Biochemistry; 2006 Jun 27; 45(25):7924-30. PubMed ID: 16784245
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  • 12. Spectroscopic evidence for a heme-heme binuclear center in the cytochrome bd ubiquinol oxidase from Escherichia coli.
    Hill JJ, Alben JO, Gennis RB.
    Proc Natl Acad Sci U S A; 1993 Jun 15; 90(12):5863-7. PubMed ID: 8516338
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  • 16. 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
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  • 18. Heme-heme and heme-ligand interactions in the di-heme oxygen-reducing site of cytochrome bd from Escherichia coli revealed by nanosecond absorption spectroscopy.
    Rappaport F, Zhang J, Vos MH, Gennis RB, Borisov VB.
    Biochim Biophys Acta; 2010 Sep 17; 1797(9):1657-64. PubMed ID: 20529691
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  • 19. Strong excitonic interactions in the oxygen-reducing site of bd-type oxidase: the Fe-to-Fe distance between hemes d and b595 is 10 A.
    Arutyunyan AM, Borisov VB, Novoderezhkin VI, Ghaim J, Zhang J, Gennis RB, Konstantinov AA.
    Biochemistry; 2008 Feb 12; 47(6):1752-9. PubMed ID: 18205406
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