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Journal Abstract Search

109 related items for PubMed ID: 8075079

  • 1. X-ray absorption studies on catechol 2,3-dioxygenase from Pseudomonas putida mt2.
    Bertini I, Briganti F, Mangani S, Nolting HF, Scozzafava A.
    Biochemistry; 1994 Sep 06; 33(35):10777-84. PubMed ID: 8075079
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  • 2. Substrate, substrate analogue, and inhibitor interactions with the ferrous active site of catechol 2,3-dioxygenase monitored through XAS studies.
    Bertini I, Briganti F, Mangani S, Nolting HF, Scozzafava A.
    FEBS Lett; 1994 Aug 22; 350(2-3):207-12. PubMed ID: 8070565
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  • 3. 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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  • 5. An archetypical extradiol-cleaving catecholic dioxygenase: the crystal structure of catechol 2,3-dioxygenase (metapyrocatechase) from Ppseudomonas putida mt-2.
    Kita A, Kita S, Fujisawa I, Inaka K, Ishida T, Horiike K, Nozaki M, Miki K.
    Structure; 1999 Jan 15; 7(1):25-34. PubMed ID: 10368270
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  • 6. Crystallization and preliminary X-ray diffraction studies of expressed Pseudomonas putida catechol 2,3-dioxygenase.
    Kita A, Kita S, Inaka K, Ishida T, Horiike K, Nozaki M, Miki K.
    J Biochem; 1997 Jul 15; 122(1):201-4. PubMed ID: 9276689
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  • 8. [17O]Water and nitric oxide binding by protocatechuate 4,5-dioxygenase and catechol 2,3-dioxygenase. Evidence for binding of exogenous ligands to the active site Fe2+ of extradiol dioxygenases.
    Arciero DM, Orville AM, Lipscomb JD.
    J Biol Chem; 1985 Nov 15; 260(26):14035-44. PubMed ID: 2997190
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  • 11. Tetrameric structure and cellular location of catechol 2,3-dioxygenase.
    Winkler J, Eltis LD, Dwyer DF, Rohde M.
    Arch Microbiol; 1995 Jan 15; 163(1):65-9. PubMed ID: 7710322
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  • 12. Crystal structure of 4-chlorocatechol 1,2-dioxygenase from the chlorophenol-utilizing gram-positive Rhodococcus opacus 1CP.
    Ferraroni M, Solyanikova IP, Kolomytseva MP, Scozzafava A, Golovleva L, Briganti F.
    J Biol Chem; 2004 Jun 25; 279(26):27646-55. PubMed ID: 15060064
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  • 13. Substrate specificity of catechol 2,3-dioxygenase encoded by TOL plasmid pWW0 of Pseudomonas putida and its relationship to cell growth.
    Cerdan P, Wasserfallen A, Rekik M, Timmis KN, Harayama S.
    J Bacteriol; 1994 Oct 25; 176(19):6074-81. PubMed ID: 7928969
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  • 14. XAS characterization of the active sites of novel intradiol ring-cleaving dioxygenases: hydroxyquinol and chlorocatechol dioxygenases.
    Briganti F, Mangani S, Pedocchi L, Scozzafava A, Golovleva LA, Jadan AP, Solyanikova IP.
    FEBS Lett; 1998 Aug 14; 433(1-2):58-62. PubMed ID: 9738933
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  • 15. Structure of catechol 2,3-dioxygenase gene encoded in chromosomal DNA of Pseudomonas putida KF715.
    Lee J, Oh J, Min KR, Kim CK, Min KH, Lee KS, Kim YC, Lim JY, Kim Y.
    Biochem Biophys Res Commun; 1996 Jul 25; 224(3):831-6. PubMed ID: 8713131
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  • 16. Quantitative structure/activity relationship for the rate of conversion of C4-substituted catechols by catechol-1,2-dioxygenase from Pseudomonas putida (arvilla) C1.
    Ridder L, Briganti F, Boersma MG, Boeren S, Vis EH, Scozzafava A, Veeger C, Rietjens IM.
    Eur J Biochem; 1998 Oct 01; 257(1):92-100. PubMed ID: 9799107
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  • 17. Inhibition of catechol 2,3-dioxygenase from Pseudomonas putida by 3-chlorocatechol.
    Klecka GM, Gibson DT.
    Appl Environ Microbiol; 1981 May 01; 41(5):1159-65. PubMed ID: 7259155
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  • 18. Ferredoxin-mediated reactivation of the chlorocatechol 2,3-dioxygenase from Pseudomonas putida GJ31.
    Tropel D, Meyer C, Armengaud J, Jouanneau Y.
    Arch Microbiol; 2002 Apr 01; 177(4):345-51. PubMed ID: 11889489
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  • 19. Novel iron(III) complexes of tripodal and linear tetradentate bis(phenolate) ligands: close relevance to intradiol-cleaving catechol dioxygenases.
    Velusamy M, Palaniandavar M, Gopalan RS, Kulkarni GU.
    Inorg Chem; 2003 Dec 15; 42(25):8283-93. PubMed ID: 14658880
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  • 20. Spectroscopic and electronic structure studies of 2,3-dihydroxybiphenyl 1,2-dioxygenase: O2 reactivity of the non-heme ferrous site in extradiol dioxygenases.
    Davis MI, Wasinger EC, Decker A, Pau MY, Vaillancourt FH, Bolin JT, Eltis LD, Hedman B, Hodgson KO, Solomon EI.
    J Am Chem Soc; 2003 Sep 17; 125(37):11214-27. PubMed ID: 16220940
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