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Journal Abstract Search

155 related items for PubMed ID: 11017198

  • 1. A switch in heme axial ligation prepares Paracoccus pantotrophus cytochrome cd1 for catalysis.
    Allen JW, Watmough NJ, Ferguson SJ.
    Nat Struct Biol; 2000 Oct; 7(10):885-8. PubMed ID: 11017198
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  • 3. Paracoccus pantotrophus NapC can reductively activate cytochrome cd1 nitrite reductase.
    Zajicek RS, Allen JW, Cartron ML, Richardson DJ, Ferguson SJ.
    FEBS Lett; 2004 May 07; 565(1-3):48-52. PubMed ID: 15135051
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  • 4. Probing the unusual oxidation/reduction behavior of Paracoccus pantotrophus cytochrome cd1 nitrite reductase by replacing a switchable methionine heme iron ligand with histidine.
    Zajicek RS, Cartron ML, Ferguson SJ.
    Biochemistry; 2006 Sep 19; 45(37):11208-16. PubMed ID: 16964982
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  • 6. Two enzymes with a common function but different heme ligands in the forms as isolated. Optical and magnetic properties of the heme groups in the oxidized forms of nitrite reductase, cytochrome cd1, from Pseudomonas stutzeri and Thiosphaera pantotropha.
    Cheesman MR, Ferguson SJ, Moir JW, Richardson DJ, Zumft WG, Thomson AJ.
    Biochemistry; 1997 Dec 23; 36(51):16267-76. PubMed ID: 9405061
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  • 8. Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme.
    Williams PA, Fülöp V, Garman EF, Saunders NF, Ferguson SJ, Hajdu J.
    Nature; 1997 Sep 25; 389(6649):406-12. PubMed ID: 9311786
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  • 9. Activation of the cytochrome cd1 nitrite reductase from Paracoccus pantotrophus. Reaction of oxidized enzyme with substrate drives a ligand switch at heme c.
    van Wonderen JH, Knight C, Oganesyan VS, George SJ, Zumft WG, Cheesman MR.
    J Biol Chem; 2007 Sep 21; 282(38):28207-15. PubMed ID: 17623666
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  • 10. Quantum mechanical interpretation of nitrite reduction by cytochrome cd1 nitrite reductase from Paracoccus pantotrophus.
    Ranghino G, Scorza E, Sjögren T, Williams PA, Ricci M, Hajdu J.
    Biochemistry; 2000 Sep 12; 39(36):10958-66. PubMed ID: 10998232
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  • 11. Time-resolved infrared spectroscopy reveals a stable ferric heme-NO intermediate in the reaction of Paracoccus pantotrophus cytochrome cd1 nitrite reductase with nitrite.
    George SJ, Allen JW, Ferguson SJ, Thorneley RN.
    J Biol Chem; 2000 Oct 27; 275(43):33231-7. PubMed ID: 10922371
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  • 13. Heme ligation and conformational plasticity in the isolated c domain of cytochrome cd1 nitrite reductase.
    Steensma E, Gordon E, Oster LM, Ferguson SJ, Hajdu J.
    J Biol Chem; 2001 Feb 23; 276(8):5846-55. PubMed ID: 11035020
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  • 14. Observation of fast release of NO from ferrous d₁ haem allows formulation of a unified reaction mechanism for cytochrome cd₁ nitrite reductases.
    Rinaldo S, Sam KA, Castiglione N, Stelitano V, Arcovito A, Brunori M, Allen JW, Ferguson SJ, Cutruzzolà F.
    Biochem J; 2011 Apr 01; 435(1):217-25. PubMed ID: 21244362
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  • 16. The Structure of an alternative form of Paracoccus pantotrophus cytochrome cd(1) nitrite reductase.
    Sjögren T, Hajdu J.
    J Biol Chem; 2001 Aug 03; 276(31):29450-5. PubMed ID: 11373294
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  • 20. Unexpected dependence on pH of NO release from Paracoccus pantotrophus cytochrome cd1.
    Sam KA, Tolland JD, Fairhurst SA, Higham CW, Lowe DJ, Thorneley RN, Allen JW, Ferguson SJ.
    Biochem Biophys Res Commun; 2008 Jul 11; 371(4):719-23. PubMed ID: 18471989
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