Výsledky vyhledávání - "Florian, Schmuckenschlager"

Role of the Main Access Channel of Catalase-Peroxidase in Catalysis

Autor: Christa Jakopitsch, Florian Schmuckenschlager, Giulietta Smulevich, Christian Obinger, Enrica Droghetti, Paul G. Furtmüller

Publikováno v: Journal of Biological Chemistry. 280:42411-42422

Catalase-peroxidases (KatG) are bifunctional heme peroxidases with an overwhelming catalatic activity. The structures show that the buried heme b is connected to the exterior of the enzyme by a main channel built up by KatG-specific loops named large

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e7b9952ce122d96943adec71666619d1
https://doi.org/10.1074/jbc.m508009200

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Influence of the Unusual Covalent Adduct on the Kinetics and Formation of Radical Intermediates in Synechocystis Catalase Peroxidase

Autor: Paul G. Furtmüller, Christa Jakopitsch, Christian Obinger, Gerald Pöltl, Florian Schmuckenschlager, Anuruddhika Wanasinghe, Florian Rüker, Anabella Ivancich

Publikováno v: Journal of Biological Chemistry. 279:46082-46095

Catalase-peroxidases (KatGs) are heme peroxidases with a catalatic activity comparable to monofunctional catalases. They contain an unusual covalent distal side adduct with the side chains of Trp122, Tyr249, and Met275 (Synechocysis KatG numbering).

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::350f938dc84c26c484319315c925a3d5
https://doi.org/10.1074/jbc.m408399200

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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

Autor: Christa, Jakopitsch, Anabella, Ivancich, Florian, Schmuckenschlager, Anuruddhika, Wanasinghe, Gerald, Pöltl, Paul Georg, Furtmüller, Florian, Rüker, Christian, Obinger

Publikováno v: The Journal of biological chemistry. 279(44)

Catalase-peroxidases (KatGs) are heme peroxidases with a catalatic activity comparable to monofunctional catalases. They contain an unusual covalent distal side adduct with the side chains of Trp(122), Tyr(249), and Met(275) (Synechocysis KatG number

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::27a1ce1d197b8055d0b52f0316af6693
https://pubmed.ncbi.nlm.nih.gov/15326163

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