Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Vera Pfanzagl"'
Publikováno v:
International Journal of Molecular Sciences, Vol 22, Iss 18, p 9849 (2021)
Dye-decolorizing peroxidases (DyPs) have gained interest for their ability to oxidize anthraquinone-derived dyes and lignin model compounds. Spectroscopic techniques, such as electron paramagnetic resonance and optical absorption spectroscopy, provid
Externí odkaz:
https://doaj.org/article/7780cd970c32497b8d2ff9721d0e5b11
Autor:
Daniel Schmidt, Nikolaus Falb, Ilenia Serra, Marzia Bellei, Vera Pfanzagl, Stefan Hofbauer, Sabine Van Doorslaer, Gianantonio Battistuzzi, Paul G. Furtmüller, Christian Obinger
Publikováno v:
Biochemistry
The heme enzyme chlorite dismutase (Cld) catalyzes the degradation of chlorite to chloride and dioxygen. Many questions about the molecular reaction mechanism of this iron protein have remained unanswered, including the electronic nature of the catal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a4a56b4a70142bbeae83ed7692ca7dc0
https://hdl.handle.net/11380/1294746
https://hdl.handle.net/11380/1294746
Autor:
Andrea Dali, Thomas Gabler, Federico Sebastiani, Alina Destinger, Paul Georg Furtmüller, Vera Pfanzagl, Maurizio Becucci, Giulietta Smulevich, Stefan Hofbauer
Publikováno v:
Protein Science. 32
Coproporphyrin ferrochelatases (CpfCs) are enzymes catalyzing the penultimate step in the coproporphyrin-dependent (CPD) heme biosynthesis pathway, which is mainly utilized by monoderm bacteria. Ferrochelatases insert ferrous iron into a porphyrin ma
Autor:
Urban Leitgeb, Paul G. Furtmüller, Stefan Hofbauer, Jose A. Brito, Christian Obinger, Vera Pfanzagl
Publikováno v:
The Journal of biological chemistry. 298(11)
The heme enzyme myeloperoxidase (MPO) is one of the key players in the neutrophil-mediated killing of invading pathogens as part of the innate immune system. MPO generates antimicrobial oxidants, which indiscriminately and effectively kill phagocytos
Autor:
Daniel Schmidt, Christian Obinger, Ilenia Serra, Sabine Van Doorslaer, Vera Pfanzagl, G. Mlynek, Paul G. Furtmüller, Stefan Hofbauer, Kristina Djinović-Carugo
Publikováno v:
Biochemistry
Biochemistry 60(8), 621-634 (2021). doi:10.1021/acs.biochem.0c00910
Biochemistry 60(8), 621-634 (2021). doi:10.1021/acs.biochem.0c00910
Biochemistry 60(8), 621 - 634 (2021). doi:10.1021/acs.biochem.0c00910
Chlorite dismutases (Clds) are heme b-containing oxidoreductases that can decompose chlorite to chloride and molecular oxygen. They are divided in two clades that differ in ol
Chlorite dismutases (Clds) are heme b-containing oxidoreductases that can decompose chlorite to chloride and molecular oxygen. They are divided in two clades that differ in ol
Autor:
Stefan Hofbauer, Vera Pfanzagl, Hanna Michlits, Kristina Djinović-Carugo, Daniel Schmidt, Thomas Gabler, John H. Beale, Christian Obinger
Publikováno v:
'Journal of Biological Chemistry ', vol: 295, pages: 13488-13501 (2020)
J Biol Chem
J Biol Chem
Since the advent of protein crystallography, atomic-level macromolecular structures have provided a basis to understand biological function. Enzymologists use detailed structural insights on ligand coordination, interatomic distances, and positioning
Autor:
Kristina Djinović-Carugo, Stefan Hofbauer, Christian Obinger, Bettina Lier, Paul G. Furtmüller, Vera Pfanzagl, Chris Oostenbrink, Hanna Michlits
Publikováno v:
ACS Catalysis
Coproheme decarboxylases (ChdCs) catalyze the final step in heme b biosynthesis of monoderm and some diderm bacteria. In this reaction, coproheme is converted to heme b via monovinyl monopropionate deuteroheme (MMD) in two consecutive decarboxylation
Autor:
Ilenia Serra, Daniel Schmidt, Vera Pfanzagl, Georg Mlynek, Stefan Hofbauer, Kristina Djinović-Carugo, Paul G. Furtmüller, Inés García-Rubio, Sabine Van Doorslaer, Christian Obinger
Publikováno v:
Journal of inorganic biochemistry
Chlorite dismutases (Clds) are heme b containing oxidoreductases able to decompose chlorite to chloride and molecular oxygen. This work analyses the impact of the distal, flexible and catalytic arginine on the binding of anionic angulate ligands like
Publikováno v:
Biochemistry
The catalytic activity of dye-decolorizing peroxidases (DyPs) toward bulky substrates, including anthraquinone dyes, phenolic lignin model compounds, or 2,2'-azino-bis(3-ethylbenzothia-zoline-6-sulfonic acid) (ABTS), is in strong contrast to their st
Autor:
Christian Obinger, Paul G. Furtmüller, Martina Paumann-Page, Stefan Hofbauer, Benjamin Sevcnikar, Vera Pfanzagl
Publikováno v:
Archives of biochemistry and biophysics. 681
Human peroxidasin 1 (hsPxd01) is a homotrimeric multidomain heme peroxidase embedded in the extracellular matrix. It catalyses the two-electron oxidation of bromide by hydrogen peroxide to hypobromous acid which mediates the formation of essential su