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Journal Abstract Search

296 related items for PubMed ID: 15264822

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  • 6. Modeling the 2-His-1-carboxylate facial triad: iron-catecholato complexes as structural and functional models of the extradiol cleaving dioxygenases.
    Bruijnincx PC, Lutz M, Spek AL, Hagen WR, Weckhuysen BM, van Koten G, Gebbink RJ.
    J Am Chem Soc; 2007 Feb 28; 129(8):2275-86. PubMed ID: 17266307
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  • 7. Novel iron(III) complexes of sterically hindered 4N ligands: regioselectivity in biomimetic extradiol cleavage of catechols.
    Mayilmurugan R, Stoeckli-Evans H, Palaniandavar M.
    Inorg Chem; 2008 Aug 04; 47(15):6645-58. PubMed ID: 18597419
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  • 8. A functional model of extradiol-cleaving catechol dioxygenases: mimicking the 2-his-1-carboxylate facial triad.
    Paria S, Halder P, Paine TK.
    Inorg Chem; 2010 May 17; 49(10):4518-23. PubMed ID: 20392074
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  • 9. 4-nitrocatechol as a probe of a Mn(II)-dependent extradiol-cleaving catechol dioxygenase (MndD): comparison with relevant Fe(II) and Mn(II) model complexes.
    Reynolds MF, Costas M, Ito M, Jo DH, Tipton AA, Whiting AK, Que L.
    J Biol Inorg Chem; 2003 Feb 17; 8(3):263-72. PubMed ID: 12589562
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  • 10. Hybrid DFT study of the mechanism of quercetin 2,3-dioxygenase.
    Siegbahn PE.
    Inorg Chem; 2004 Sep 20; 43(19):5944-53. PubMed ID: 15360243
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  • 11. Iron(III) complexes of sterically hindered tetradentate monophenolate ligands as functional models for catechol 1,2-dioxygenases: the role of ligand stereoelectronic properties.
    Velusamy M, Mayilmurugan R, Palaniandavar M.
    Inorg Chem; 2004 Oct 04; 43(20):6284-93. PubMed ID: 15446874
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  • 12. Directed evolution of a non-heme-iron-dependent extradiol catechol dioxygenase: identification of mutants with intradiol oxidative cleavage activity.
    Schlosrich J, Eley KL, Crowley PJ, Bugg TD.
    Chembiochem; 2006 Dec 04; 7(12):1899-908. PubMed ID: 17051653
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  • 13. Catechol dioxygenases.
    Broderick JB.
    Essays Biochem; 1999 Dec 04; 34():173-89. PubMed ID: 10730195
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  • 14. Synthesis, structure, spectra and reactivity of iron(III) complexes of facially coordinating and sterically hindering 3N ligands as models for catechol dioxygenases.
    Sundaravel K, Dhanalakshmi T, Suresh E, Palaniandavar M.
    Dalton Trans; 2008 Dec 28; (48):7012-25. PubMed ID: 19050788
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  • 15. Molecular basis for the substrate selectivity of bicyclic and monocyclic extradiol dioxygenases.
    Vaillancourt FH, Fortin PD, Labbé G, Drouin NM, Karim Z, Agar NY, Eltis LD.
    Biochem Biophys Res Commun; 2005 Dec 09; 338(1):215-22. PubMed ID: 16165093
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  • 16. Unravelling the Molecular Origin of the Regiospecificity in Extradiol Catechol Dioxygenases.
    Christian GJ, Neese F, Ye S.
    Inorg Chem; 2016 Apr 18; 55(8):3853-64. PubMed ID: 27050565
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  • 17. X-ray absorption spectroscopic studies of the Fe(II) active site of catechol 2,3-dioxygenase. Implications for the extradiol cleavage mechanism.
    Shu L, Chiou YM, Orville AM, Miller MA, Lipscomb JD, Que L.
    Biochemistry; 1995 May 23; 34(20):6649-59. PubMed ID: 7756296
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  • 18. Iron(III) complexes of N2O and N3O donor ligands as functional models for catechol dioxygenase enzymes: ether oxygen coordination tunes the regioselectivity and reactivity.
    Sundaravel K, Suresh E, Saminathan K, Palaniandavar M.
    Dalton Trans; 2011 Aug 28; 40(32):8092-107. PubMed ID: 21766098
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  • 19. Intermediate in the O-O bond cleavage reaction of an extradiol dioxygenase.
    Kovaleva EG, Lipscomb JD.
    Biochemistry; 2008 Oct 28; 47(43):11168-70. PubMed ID: 18826259
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  • 20. Acid-base catalysis in the extradiol catechol dioxygenase reaction mechanism: site-directed mutagenesis of His-115 and His-179 in Escherichia coli 2,3-dihydroxyphenylpropionate 1,2-dioxygenase (MhpB).
    Mendel S, Arndt A, Bugg TD.
    Biochemistry; 2004 Oct 26; 43(42):13390-6. PubMed ID: 15491145
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