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114 related items for PubMed ID: 14527675

  • 1. Distal side tryptophan, tyrosine and methionine in catalase-peroxidases are covalently linked in solution.
    Jakopitsch C, Kolarich D, Petutschnig G, Furtmüller PG, Obinger C.
    FEBS Lett; 2003 Sep 25; 552(2-3):135-40. PubMed ID: 14527675
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  • 2. Manipulating the covalent link between distal side tryptophan, tyrosine, and methionine in catalase-peroxidases: an electronic absorption and resonance Raman study.
    Santoni E, Jakopitsch C, Obinger C, Smulevich G.
    Biopolymers; 2003 Sep 25; 74(1-2):46-50. PubMed ID: 15137092
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  • 4. The Met-Tyr-Trp cross-link in Mycobacterium tuberculosis catalase-peroxidase (KatG): autocatalytic formation and effect on enzyme catalysis and spectroscopic properties.
    Ghiladi RA, Knudsen GM, Medzihradszky KF, Ortiz de Montellano PR.
    J Biol Chem; 2005 Jun 17; 280(24):22651-63. PubMed ID: 15840564
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  • 6. Protein-based radicals in the catalase-peroxidase of synechocystis PCC6803: a multifrequency EPR investigation of wild-type and variants on the environment of the heme active site.
    Ivancich A, Jakopitsch C, Auer M, Un S, Obinger C.
    J Am Chem Soc; 2003 Nov 19; 125(46):14093-102. PubMed ID: 14611246
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  • 8. Total conversion of bifunctional catalase-peroxidase (KatG) to monofunctional peroxidase by exchange of a conserved distal side tyrosine.
    Jakopitsch C, Auer M, Ivancich A, Rüker F, Furtmüller PG, Obinger C.
    J Biol Chem; 2003 May 30; 278(22):20185-91. PubMed ID: 12649295
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  • 9. Distal site aspartate is essential in the catalase activity of catalase-peroxidases.
    Jakopitsch C, Auer M, Regelsberger G, Jantschko W, Furtmüller PG, Rüker F, Obinger C.
    Biochemistry; 2003 May 13; 42(18):5292-300. PubMed ID: 12731870
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  • 14. Redox thermodynamics of the ferric-ferrous couple of wild-type synechocystis KatG and KatG(Y249F).
    Bellei M, Jakopitsch C, Battistuzzi G, Sola M, Obinger C.
    Biochemistry; 2006 Apr 18; 45(15):4768-74. PubMed ID: 16605245
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  • 16. Theory Uncovers the Role of the Methionine-Tyrosine-Tryptophan Radical Adduct in the Catalase Reaction of KatGs: O2  Release Mediated by Proton-Coupled Electron Transfer.
    Wang B, Fita I, Rovira C.
    Chemistry; 2018 Apr 06; 24(20):5388-5395. PubMed ID: 29462509
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  • 18. Probing the structure and bifunctionality of catalase-peroxidase (KatG).
    Smulevich G, Jakopitsch C, Droghetti E, Obinger C.
    J Inorg Biochem; 2006 Apr 06; 100(4):568-85. PubMed ID: 16516299
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  • 19. Catalase-peroxidase from synechocystis is capable of chlorination and bromination reactions.
    Jakopitsch C, Regelsberger G, Furtmüller PG, Rüker F, Peschek GA, Obinger C.
    Biochem Biophys Res Commun; 2001 Sep 28; 287(3):682-7. PubMed ID: 11563849
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  • 20. The role of distal tryptophan in the bifunctional activity of catalase-peroxidases.
    Regelsberger G, Jakopitsch C, Furtmüller PG, Rueker F, Switala J, Loewen PC, Obinger C.
    Biochem Soc Trans; 2001 May 28; 29(Pt 2):99-105. PubMed ID: 11356135
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