Jakopitsch C - Search Results

1

Active site structure and catalytic mechanisms of human peroxidases.

Furtmüller PG, Zederbauer M, Jantschko W, Helm J, Bogner M, Jakopitsch C, Obinger C. Furtmüller PG, et al. Among authors: jakopitsch c. Arch Biochem Biophys. 2006 Jan 15;445(2):199-213. doi: 10.1016/j.abb.2005.09.017. Epub 2005 Oct 26. Arch Biochem Biophys. 2006. PMID: 16288970 Review.

2

Redox intermediates of plant and mammalian peroxidases: a comparative transient-kinetic study of their reactivity toward indole derivatives.

Jantschko W, Furtmüller PG, Allegra M, Livrea MA, Jakopitsch C, Regelsberger G, Obinger C. Jantschko W, et al. Among authors: jakopitsch c. Arch Biochem Biophys. 2002 Feb 1;398(1):12-22. doi: 10.1006/abbi.2001.2674. Arch Biochem Biophys. 2002. PMID: 11811944

3

Reaction of lactoperoxidase compound I with halides and thiocyanate.

Furtmüller PG, Jantschko W, Regelsberger G, Jakopitsch C, Arnhold J, Obinger C. Furtmüller PG, et al. Among authors: jakopitsch c. Biochemistry. 2002 Oct 1;41(39):11895-900. doi: 10.1021/bi026326x. Biochemistry. 2002. PMID: 12269834

4

The catalytic role of the distal site asparagine-histidine couple in catalase-peroxidases.

Jakopitsch C, Auer M, Regelsberger G, Jantschko W, Furtmüller PG, Rüker F, Obinger C. Jakopitsch C, et al. Eur J Biochem. 2003 Mar;270(5):1006-13. doi: 10.1046/j.1432-1033.2003.03476.x. Eur J Biochem. 2003. PMID: 12603334 Free article.

5

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. Jakopitsch C, et al. Biochemistry. 2003 May 13;42(18):5292-300. doi: 10.1021/bi026944d. Biochemistry. 2003. PMID: 12731870

6

Kinetics of oxygen binding to ferrous myeloperoxidase.

Jantschko W, Furtmüller PG, Zederbauer M, Jakopitsch C, Obinger C. Jantschko W, et al. Among authors: jakopitsch c. Arch Biochem Biophys. 2004 Jun 1;426(1):91-7. doi: 10.1016/j.abb.2004.03.019. Arch Biochem Biophys. 2004. PMID: 15130787

7

Reaction of ferrous lactoperoxidase with hydrogen peroxide and dioxygen: an anaerobic stopped-flow study.

Jantschko W, Furtmüller PG, Zederbauer M, Neugschwandtner K, Jakopitsch C, Obinger C. Jantschko W, et al. Among authors: jakopitsch c. Arch Biochem Biophys. 2005 Feb 1;434(1):51-9. doi: 10.1016/j.abb.2004.10.014. Arch Biochem Biophys. 2005. PMID: 15629108

8

Exploitation of the unusual thermodynamic properties of human myeloperoxidase in inhibitor design.

Jantschko W, Furtmüller PG, Zederbauer M, Neugschwandtner K, Lehner I, Jakopitsch C, Arnhold J, Obinger C. Jantschko W, et al. Among authors: jakopitsch c. Biochem Pharmacol. 2005 Apr 15;69(8):1149-57. doi: 10.1016/j.bcp.2005.02.006. Biochem Pharmacol. 2005. PMID: 15794935

9

Role of the covalent glutamic acid 242-heme linkage in the formation and reactivity of redox intermediates of human myeloperoxidase.

Zederbauer M, Jantschko W, Neugschwandtner K, Jakopitsch C, Moguilevsky N, Obinger C, Furtmüller PG. Zederbauer M, et al. Among authors: jakopitsch c. Biochemistry. 2005 May 3;44(17):6482-91. doi: 10.1021/bi0501737. Biochemistry. 2005. PMID: 15850382

10

Role of the main access channel of catalase-peroxidase in catalysis.

Jakopitsch C, Droghetti E, Schmuckenschlager F, Furtmüller PG, Smulevich G, Obinger C. Jakopitsch C, et al. J Biol Chem. 2005 Dec 23;280(51):42411-22. doi: 10.1074/jbc.M508009200. Epub 2005 Oct 22. J Biol Chem. 2005. PMID: 16244360 Free article.

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