Výsledky vyhledávání - "Walter Jantschko"

Active site structure and catalytic mechanisms of human peroxidases

Autor: Christa Jakopitsch, Christian Obinger, Paul G. Furtmüller, Jutta Helm, Walter Jantschko, Martin Bogner, Martina Zederbauer

Publikováno v: Archives of Biochemistry and Biophysics. 445:199-213

Myeloperoxidase (MPO), eosinophil peroxidase, lactoperoxidase, and thyroid peroxidase are heme-containing oxidoreductases (EC 1.7.1.11), which bind ligands and/or undergo a series of redox reactions. Though sharing functional and structural homology,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::22bd967646e2ddb5b684c84d74df8576
https://doi.org/10.1016/j.abb.2005.09.017

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Standard reduction potentials of all couples of the peroxidase cycle of lactoperoxidase

Autor: Martina Zederbauer, Jürgen Arnhold, Christa Jakopitsch, Walter Jantschko, Paul G. Furtmüller, Christian Obinger

Publikováno v: Journal of Inorganic Biochemistry. 99:1220-1229

Lactoperoxidase (LPO) is found in mucosal surfaces and exocrine secretions including milk, tears and saliva and has physiological significance in antimicrobial defense. Its predominant physiological role is to convert hydrogen peroxide and thiocyanat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::60666bbf5a8e341e7c8ef5f509bf1c37
https://doi.org/10.1016/j.jinorgbio.2005.02.021

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Role of the Covalent Glutamic Acid 242−Heme Linkage in the Formation and Reactivity of Redox Intermediates of Human Myeloperoxidase

Autor: Paul G. Furtmüller, Martina Zederbauer, Karin Neugschwandtner, Christian Obinger, Christa Jakopitsch, Walter Jantschko, Nicole Moguilevsky

Publikováno v: Biochemistry. 44:6482-6491

In human myeloperoxidase the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu242 and Asp94 and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between

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https://doi.org/10.1021/bi0501737

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Kinetics of Interconversion of Ferrous Enzymes, Compound II and Compound III, of Wild-type Synechocystis Catalase-peroxidase and Y249F

Autor: Christa Jakopitsch, Walter Jantschko, Paul G. Furtmüller, Anuruddhika Wanasinghe, Christian Obinger

Publikováno v: Journal of Biological Chemistry. 280:9037-9042

With the exception of catalase-peroxidases, heme peroxidases show no significant ability to oxidize hydrogen peroxide and are trapped and inactivated in the compound III form by H2O2 in the absence of one-electron donors. Interestingly, some KatG var

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https://doi.org/10.1074/jbc.m413317200

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Purification and Physical-Chemical Characterization of the Three Hydroperoxidases from the Symbiotic Bacterium Sinorhizobium meliloti

Autor: Pierre Frendo, Rosa Pia Ferrari, Enzo Laurenti, Walter Jantschko, Silvia Ardissone, and Alain Puppo, Christian Obinger

Publikováno v: Biochemistry. 43:12692-12699

Three genes encoding heme hydroperoxidases (katA, katB, and katC) have been identified in the soil bacterium Sinorhizobium meliloti. The recombinant proteins were overexpressed in Escherichia coli and purified in order toachieve a spectral and kineti

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https://doi.org/10.1021/bi048836s

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Distal Site Aspartate Is Essential in the Catalase Activity of Catalase-Peroxidases

Autor: Günther Regelsberger, Florian Rüker, Paul G. Furtmüller, Walter Jantschko, Christian Obinger, Markus Auer, Christa Jakopitsch

Publikováno v: Biochemistry. 42:5292-5300

Structural and biochemical characterization of aspartate 152 at the distal heme side of catalase-peroxidase (KatG) from Synechocystis PCC 6803 reveals an important functional role for this residue. In the wild-type protein, the side chain carboxyl gr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4ad3b25097fb93e53c1f253212c9f2e6
https://doi.org/10.1021/bi026944d

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

Autor: Paul G. Furtmüller, Florian Rüker, Günther Regelsberger, Walter Jantschko, Christian Obinger, Christa Jakopitsch, Markus Auer

Publikováno v: European Journal of Biochemistry. 270:1006-1013

Catalase-peroxidases (KatGs) are unique in exhibiting an overwhelming catalase activity and a peroxidase activity of broad specificity. Similar to other peroxidases the distal histidine in KatGs forms a hydrogen bond with an adjacent conserved aspara

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https://doi.org/10.1046/j.1432-1033.2003.03476.x

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Reaction of Lactoperoxidase Compound I with Halides and Thiocyanate

Autor: Christa Jakopitsch, Günther Regelsberger, Christian Obinger, Paul G. Furtmüller, Walter Jantschko, Jürgen Arnhold

Publikováno v: Biochemistry. 41:11895-11900

Lactoperoxidase (LPO) is found in mucosal surfaces and exocrine secretions, including milk, tears, and saliva, and has physiological significance in antimicrobial defense which involves (pseudo-) halide oxidation. This study for the first time presen

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https://doi.org/10.1021/bi026326x

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A transient kinetic study on the reactivity of recombinant unprocessed monomeric myeloperoxidase

Autor: Günther Regelsberger, Nicole Moguilevsky, Christa Jakopitsch, Paul G. Furtmüller, Walter Jantschko, Christian Obinger

Publikováno v: FEBS Letters. 503:147-150

Spectral and kinetic features of the redox intermediates of human recombinant unprocessed monomeric myeloperoxidase (recMPO), purified from an engineered Chinese hamster ovary cell line, were studied by the multi-mixing stopped-flow technique. Both t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2bc2c91d3130f19a6a593ce748789268
https://doi.org/10.1016/s0014-5793(01)02725-9

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The reactivity of myeloperoxidase compound I formed with hypochlorous acid

Autor: Ursula Burner, Günther Regelsberger, Paul G. Furtmüller, Christian Obinger, Walter Jantschko

Publikováno v: Redox Report. 5:173-178

The reaction of human myeloperoxidase (MPO) with hypochlorous acid (HOCl) was investigated by conventional stopped-flow spectroscopy at pH 5, 7, and 9. In the reaction of MPO with HOCl, compound I is formed. Its formation is strongly dependent on pH.

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https://doi.org/10.1179/135100000101535717

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