227 related articles for article (PubMed ID: 16605245)
1. 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]
2. 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]
3. Conformational differences in Mycobacterium tuberculosis catalase-peroxidase KatG and its S315T mutant revealed by resonance Raman spectroscopy.
Kapetanaki S; Chouchane S; Girotto S; Yu S; Magliozzo RS; Schelvis JP
Biochemistry; 2003 Apr; 42(13):3835-45. PubMed ID: 12667074
[TBL] [Abstract][Full Text] [Related]
4. 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]
5. 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]
6. Kinetics of interconversion of ferrous enzymes, compound II and compound III, of wild-type synechocystis catalase-peroxidase and Y249F: proposal for the catalatic mechanism.
Jakopitsch C; Wanasinghe A; Jantschko W; Furtmüller PG; Obinger C
J Biol Chem; 2005 Mar; 280(10):9037-42. PubMed ID: 15637065
[TBL] [Abstract][Full Text] [Related]
7. Redox thermodynamics of the Fe(III)/Fe(II) couple of human myeloperoxidase in its high-spin and low-spin forms.
Battistuzzi G; Bellei M; Zederbauer M; Furtmüller PG; Sola M; Obinger C
Biochemistry; 2006 Oct; 45(42):12750-5. PubMed ID: 17042493
[TBL] [Abstract][Full Text] [Related]
8. 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]
9. 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]
10. 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]
11. Hydrogen peroxide oxidation by catalase-peroxidase follows a non-scrambling mechanism.
Vlasits J; Jakopitsch C; Schwanninger M; Holubar P; Obinger C
FEBS Lett; 2007 Jan; 581(2):320-4. PubMed ID: 17217949
[TBL] [Abstract][Full Text] [Related]
12. 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]
13. Two alternative substrate paths for compound I formation and reduction in catalase-peroxidase KatG from Burkholderia pseudomallei.
Deemagarn T; Wiseman B; Carpena X; Ivancich A; Fita I; Loewen PC
Proteins; 2007 Jan; 66(1):219-28. PubMed ID: 17063492
[TBL] [Abstract][Full Text] [Related]
14. 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]
15. Spectral and kinetic studies of the oxidation of monosubstituted phenols and anilines by recombinant Synechocystis catalase-peroxidase compound I.
Regelsberger G; Jakopitsch C; Engleder M; Rüker F; Peschek GA; Obinger C
Biochemistry; 1999 Aug; 38(32):10480-8. PubMed ID: 10441144
[TBL] [Abstract][Full Text] [Related]
16. Vital roles of an interhelical insertion in catalase-peroxidase bifunctionality.
Li Y; Goodwin DC
Biochem Biophys Res Commun; 2004 Jun; 318(4):970-6. PubMed ID: 15147967
[TBL] [Abstract][Full Text] [Related]
17. Redox thermodynamics of lactoperoxidase and eosinophil peroxidase.
Battistuzzi G; Bellei M; Vlasits J; Banerjee S; Furtmüller PG; Sola M; Obinger C
Arch Biochem Biophys; 2010 Feb; 494(1):72-7. PubMed ID: 19944669
[TBL] [Abstract][Full Text] [Related]
18. Impact of distal side water and residue 315 on ligand binding to ferric Mycobacterium tuberculosis catalase-peroxidase (KatG).
Ranguelova K; Suarez J; Metlitsky L; Yu S; Brejt SZ; Brejt SZ; Zhao L; Schelvis JP; Magliozzo RS
Biochemistry; 2008 Nov; 47(47):12583-92. PubMed ID: 18956888
[TBL] [Abstract][Full Text] [Related]
19. Influence of the protein matrix on intramolecular histidine ligation in ferric and ferrous hexacoordinate hemoglobins.
Halder P; Trent JT; Hargrove MS
Proteins; 2007 Jan; 66(1):172-82. PubMed ID: 17044063
[TBL] [Abstract][Full Text] [Related]
20. 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]
[Next] [New Search]