117 related articles for article (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; 552(2-3):135-40. PubMed ID: 14527675
[TBL] [Abstract][Full Text] [Related]
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; 2004 May-Jun 5; 74(1-2):46-50. PubMed ID: 15137092
[TBL] [Abstract][Full Text] [Related]
3. Role of the Met-Tyr-Trp cross-link in Mycobacterium tuberculosis catalase-peroxidase (KatG) as revealed by KatG(M255I).
Ghiladi RA; Medzihradszky KF; Ortiz de Montellano PR
Biochemistry; 2005 Nov; 44(46):15093-105. PubMed ID: 16285713
[TBL] [Abstract][Full Text] [Related]
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; 280(24):22651-63. PubMed ID: 15840564
[TBL] [Abstract][Full Text] [Related]
5. Influence of the unusual covalent adduct on the kinetics and formation of radical intermediates in synechocystis catalase peroxidase: a stopped-flow and EPR characterization of the MET275, TYR249, and ARG439 variants.
Jakopitsch C; Ivancich A; Schmuckenschlager F; Wanasinghe A; Pöltl G; Furtmüller PG; Rüker F; Obinger C
J Biol Chem; 2004 Oct; 279(44):46082-95. PubMed ID: 15326163
[TBL] [Abstract][Full Text] [Related]
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; 125(46):14093-102. PubMed ID: 14611246
[TBL] [Abstract][Full Text] [Related]
7. New insights into the heme cavity structure of catalase-peroxidase: a spectroscopic approach to the recombinant synechocystis enzyme and selected distal cavity mutants.
Heering HA; Indiani C; Regelsberger G; Jakopitsch C; Obinger C; Smulevich G
Biochemistry; 2002 Jul; 41(29):9237-47. PubMed ID: 12119039
[TBL] [Abstract][Full Text] [Related]
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; 278(22):20185-91. PubMed ID: 12649295
[TBL] [Abstract][Full Text] [Related]
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; 42(18):5292-300. PubMed ID: 12731870
[TBL] [Abstract][Full Text] [Related]
10. Comparison between catalase-peroxidase and cytochrome c peroxidase. The role of the hydrogen-bond networks for protein stability and catalysis.
Santoni E; Jakopitsch C; Obinger C; Smulevich G
Biochemistry; 2004 May; 43(19):5792-802. PubMed ID: 15134453
[TBL] [Abstract][Full Text] [Related]
11. Modification of the active site of Mycobacterium tuberculosis KatG after disruption of the Met-Tyr-Trp cross-linked adduct.
Kapetanaki SM; Zhao X; Yu S; Magliozzo RS; Schelvis JP
J Inorg Biochem; 2007 Mar; 101(3):422-33. PubMed ID: 17188362
[TBL] [Abstract][Full Text] [Related]
12. Probing hydrogen peroxide oxidation kinetics of wild-type Synechocystis catalase-peroxidase (KatG) and selected variants.
Vlasits J; Furtmüller PG; Jakopitsch C; Zamocky M; Obinger C
Biochim Biophys Acta; 2010 Apr; 1804(4):799-805. PubMed ID: 20026288
[TBL] [Abstract][Full Text] [Related]
13. Disruption of the H-bond network in the main access channel of catalase-peroxidase modulates enthalpy and entropy of Fe(III) reduction.
Vlasits J; Bellei M; Jakopitsch C; De Rienzo F; Furtmüller PG; Zamocky M; Sola M; Battistuzzi G; Obinger C
J Inorg Biochem; 2010 Jun; 104(6):648-56. PubMed ID: 20347488
[TBL] [Abstract][Full Text] [Related]
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; 45(15):4768-74. PubMed ID: 16605245
[TBL] [Abstract][Full Text] [Related]
15. Identification of Trp106 as the tryptophanyl radical intermediate in Synechocystis PCC6803 catalase-peroxidase by multifrequency Electron Paramagnetic Resonance spectroscopy.
Jakopitsch C; Obinger C; Un S; Ivancich A
J Inorg Biochem; 2006 May; 100(5-6):1091-9. PubMed ID: 16574230
[TBL] [Abstract][Full Text] [Related]
16. Theory Uncovers the Role of the Methionine-Tyrosine-Tryptophan Radical Adduct in the Catalase Reaction of KatGs: O
Wang B; Fita I; Rovira C
Chemistry; 2018 Apr; 24(20):5388-5395. PubMed ID: 29462509
[TBL] [Abstract][Full Text] [Related]
17. The molecular peculiarities of catalase-peroxidases.
Zámocký M; Regelsberger G; Jakopitsch C; Obinger C
FEBS Lett; 2001 Mar; 492(3):177-82. PubMed ID: 11257490
[TBL] [Abstract][Full Text] [Related]
18. Probing the structure and bifunctionality of catalase-peroxidase (KatG).
Smulevich G; Jakopitsch C; Droghetti E; Obinger C
J Inorg Biochem; 2006 Apr; 100(4):568-85. PubMed ID: 16516299
[TBL] [Abstract][Full Text] [Related]
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; 287(3):682-7. PubMed ID: 11563849
[TBL] [Abstract][Full Text] [Related]
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; 29(Pt 2):99-105. PubMed ID: 11356135
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
