Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Anuruddhika, Wanasinghe"'
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5f1879e44dc1b63b0ff55bab8d2e1211
https://doi.org/10.1074/jbc.m413317200
https://doi.org/10.1074/jbc.m413317200
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
https://doi.org/10.1074/jbc.m408399200
Autor:
Christa, Jakopitsch, Anuruddhika, Wanasinghe, Walter, Jantschko, Paul G, Furtmüller, Christian, Obinger
Publikováno v:
The Journal of biological chemistry. 280(10)
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ab2cbaf52356d979de2ed35564b6ea6b
https://pubmed.ncbi.nlm.nih.gov/15637065
https://pubmed.ncbi.nlm.nih.gov/15637065
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
https://pubmed.ncbi.nlm.nih.gov/15326163