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193 related items for PubMed ID: 33705279

  • 1. Terminal Oxidase Cytochrome bd Protects Bacteria Against Hydrogen Sulfide Toxicity.
    Borisov VB, Forte E.
    Biochemistry (Mosc); 2021 Jan; 86(1):22-32. PubMed ID: 33705279
    [Abstract] [Full Text] [Related]

  • 2. The cytochrome bd oxidase of Escherichia coli prevents respiratory inhibition by endogenous and exogenous hydrogen sulfide.
    Korshunov S, Imlay KR, Imlay JA.
    Mol Microbiol; 2016 Jul; 101(1):62-77. PubMed ID: 26991114
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  • 3. The Terminal Oxidase Cytochrome bd Promotes Sulfide-resistant Bacterial Respiration and Growth.
    Forte E, Borisov VB, Falabella M, Colaço HG, Tinajero-Trejo M, Poole RK, Vicente JB, Sarti P, Giuffrè A.
    Sci Rep; 2016 Mar 31; 6():23788. PubMed ID: 27030302
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  • 4. Cytochrome bd-I in Escherichia coli is less sensitive than cytochromes bd-II or bo'' to inhibition by the carbon monoxide-releasing molecule, CORM-3: N-acetylcysteine reduces CO-RM uptake and inhibition of respiration.
    Jesse HE, Nye TL, McLean S, Green J, Mann BE, Poole RK.
    Biochim Biophys Acta; 2013 Sep 31; 1834(9):1693-703. PubMed ID: 23624261
    [Abstract] [Full Text] [Related]

  • 5. The terminal oxidase cytochrome bd-I confers carbon monoxide resistance to Escherichia coli cells.
    Nastasi MR, Borisov VB, Forte E.
    J Inorg Biochem; 2023 Oct 31; 247():112341. PubMed ID: 37515940
    [Abstract] [Full Text] [Related]

  • 6. Cytochrome bd confers nitric oxide resistance to Escherichia coli.
    Mason MG, Shepherd M, Nicholls P, Dobbin PS, Dodsworth KS, Poole RK, Cooper CE.
    Nat Chem Biol; 2009 Feb 31; 5(2):94-6. PubMed ID: 19109594
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  • 8. Impact of Hydrogen Sulfide on Mitochondrial and Bacterial Bioenergetics.
    Borisov VB, Forte E.
    Int J Mol Sci; 2021 Nov 24; 22(23):. PubMed ID: 34884491
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  • 10. Oxygen as Acceptor.
    Borisov VB, Verkhovsky MI.
    EcoSal Plus; 2015 Nov 24; 6(2):. PubMed ID: 26734697
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  • 11. Mechanistic and structural diversity between cytochrome bd isoforms of Escherichia coli.
    Grund TN, Radloff M, Wu D, Goojani HG, Witte LF, Jösting W, Buschmann S, Müller H, Elamri I, Welsch S, Schwalbe H, Michel H, Bald D, Safarian S.
    Proc Natl Acad Sci U S A; 2021 Dec 14; 118(50):. PubMed ID: 34873041
    [Abstract] [Full Text] [Related]

  • 12. 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
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  • 14. The carboxy-terminal insert in the Q-loop is needed for functionality of Escherichia coli cytochrome bd-I.
    Goojani HG, Konings J, Hakvoort H, Hong S, Gennis RB, Sakamoto J, Lill H, Bald D.
    Biochim Biophys Acta Bioenerg; 2020 Jun 01; 1861(5-6):148175. PubMed ID: 32061652
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  • 17. Respiration of Escherichia coli can be fully uncoupled via the nonelectrogenic terminal cytochrome bd-II oxidase.
    Bekker M, de Vries S, Ter Beek A, Hellingwerf KJ, de Mattos MJ.
    J Bacteriol; 2009 Sep 01; 191(17):5510-7. PubMed ID: 19542282
    [Abstract] [Full Text] [Related]

  • 18. The cytochrome bd quinol oxidase in Escherichia coli has an extremely high oxygen affinity and two oxygen-binding haems: implications for regulation of activity in vivo by oxygen inhibition.
    D'mello R, Hill S, Poole RK.
    Microbiology (Reading); 1996 Apr 01; 142 ( Pt 4)():755-763. PubMed ID: 8936304
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  • 19. Electrocatalytic evidence of the diversity of the oxygen reaction in the bacterial bd oxidase from different organisms.
    Nikolaev A, Safarian S, Thesseling A, Wohlwend D, Friedrich T, Michel H, Kusumoto T, Sakamoto J, Melin F, Hellwig P.
    Biochim Biophys Acta Bioenerg; 2021 Aug 01; 1862(8):148436. PubMed ID: 33940039
    [Abstract] [Full Text] [Related]

  • 20. The long Q-loop of Escherichia coli cytochrome bd oxidase is required for assembly and structural integrity.
    Theßeling A, Burschel S, Wohlwend D, Friedrich T.
    FEBS Lett; 2020 May 01; 594(10):1577-1585. PubMed ID: 32002997
    [Abstract] [Full Text] [Related]

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