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Journal Abstract Search

228 related items for PubMed ID: 8292013

  • 1.
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  • 2. Free flavins accelerate release of ferrous iron from iron storage proteins by both free flavin-dependent and -independent ferric reductases in Escherichia coli.
    Satoh J, Kimata S, Nakamoto S, Ishii T, Tanaka E, Yumoto S, Takeda K, Yoshimura E, Kanesaki Y, Ishige T, Tanaka K, Abe A, Kawasaki S, Niimura Y.
    J Gen Appl Microbiol; 2020 Jan 31; 65(6):308-315. PubMed ID: 31281172
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  • 3. Haem, flavin and oxygen interactions in Hmp, a flavohaemoglobin from Escherichia coli.
    Cooper CE, Ioannidis N, D'mello R, Poole RK.
    Biochem Soc Trans; 1994 Aug 31; 22(3):709-13. PubMed ID: 7821669
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  • 4. The haemoglobin-like protein (HMP) of Escherichia coli has ferrisiderophore reductase activity and its C-terminal domain shares homology with ferredoxin NADP+ reductases.
    Andrews SC, Shipley D, Keen JN, Findlay JB, Harrison PM, Guest JR.
    FEBS Lett; 1992 May 18; 302(3):247-52. PubMed ID: 1601132
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  • 5. Sulfite reductase of Escherichia coli is a ferrisiderophore reductase.
    Coves J, Eschenbrenner M, Fontecave M.
    Biochem Biophys Res Commun; 1993 May 14; 192(3):1403-8. PubMed ID: 8389549
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  • 11. Response of the NAD(P)H-oxidising flavohaemoglobin (Hmp) to prolonged oxidative stress and implications for its physiological role in Escherichia coli.
    Anjum MF, Ioannidis N, Poole RK.
    FEMS Microbiol Lett; 1998 Sep 15; 166(2):219-23. PubMed ID: 9770277
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  • 12. NAD(P)H:flavin oxidoreductase of Escherichia coli. A ferric iron reductase participating in the generation of the free radical of ribonucleotide reductase.
    Fontecave M, Eliasson R, Reichard P.
    J Biol Chem; 1987 Sep 05; 262(25):12325-31. PubMed ID: 3305505
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  • 13. Crystal structure of NAD(P)H:flavin oxidoreductase from Escherichia coli.
    Ingelman M, Ramaswamy S, Nivière V, Fontecave M, Eklund H.
    Biochemistry; 1999 Jun 01; 38(22):7040-9. PubMed ID: 10353815
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  • 14. The NAD(P)H:flavin oxidoreductase from Escherichia coli as a source of superoxide radicals.
    Gaudu P, Touati D, Nivière V, Fontecave M.
    J Biol Chem; 1994 Mar 18; 269(11):8182-8. PubMed ID: 8132544
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  • 15. Escherichia coli flavohaemoglobin (Hmp) with equistoichiometric FAD and haem contents has a low affinity for dioxygen in the absence or presence of nitric oxide.
    Mills CE, Sedelnikova S, Søballe B, Hughes MN, Poole RK.
    Biochem J; 2001 Jan 15; 353(Pt 2):207-13. PubMed ID: 11139382
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  • 16. NADPH-sulfite reductase from Escherichia coli. A flavin reductase participating in the generation of the free radical of ribonucleotide reductase.
    Covès J, Nivière V, Eschenbrenner M, Fontecave M.
    J Biol Chem; 1993 Sep 05; 268(25):18604-9. PubMed ID: 8360156
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  • 17. Nitric oxide reactivities of the two globins of the foodborne pathogen Campylobacter jejuni: roles in protection from nitrosative stress and analysis of potential reductants.
    Tinajero-Trejo M, Vreugdenhil A, Sedelnikova SE, Davidge KS, Poole RK.
    Nitric Oxide; 2013 Nov 01; 34():65-75. PubMed ID: 23764490
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  • 18. Ferric reductases or flavin reductases?
    Fontecave M, Covès J, Pierre JL.
    Biometals; 1994 Jan 01; 7(1):3-8. PubMed ID: 8118169
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  • 19. The oxygenated flavohaemoglobin from Escherichia coli: evidence from photodissociation and rapid-scan studies for two kinetic and spectral forms.
    Orii Y, Ioannidis N, Poole RK.
    Biochem Biophys Res Commun; 1992 Aug 31; 187(1):94-100. PubMed ID: 1325799
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  • 20. Reaction of the NAD(P)H:flavin oxidoreductase from Escherichia coli with NADPH and riboflavin: identification of intermediates.
    Nivière V, Vanoni MA, Zanetti G, Fontecave M.
    Biochemistry; 1998 Aug 25; 37(34):11879-87. PubMed ID: 9718311
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