Výsledky vyhledávání - "Vera Pfanzagl"

Compound I formation and reactivity in dimeric chlorite dismutase – Impact of pH and the dynamics of the catalytic arginine

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

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Active site architecture of coproporphyrin ferrochelatase with its physiological substrate coproporphyrin III : Propionate interactions and porphyrin core deformation

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c4075326a5761cc5a564bd7942257f79
https://doi.org/10.1002/pro.4534

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The staphylococcal inhibitory protein SPIN binds to human myeloperoxidase with picomolar affinity but only dampens halide oxidation

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e819b5e81488c71696fb2052a7d901a3
https://pubmed.ncbi.nlm.nih.gov/36150500

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Arresting the Catalytic Arginine in Chlorite Dismutases: Impact on Heme Coordination, Thermal Stability, and Catalysis

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
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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f1c972d165fbcdf339d8c7ed0de6395a
https://doi.org/10.1021/acs.biochem.0c00910

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X-ray–induced photoreduction of heme metal centers rapidly induces active-site perturbations in a protein-independent manner

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

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d256d58f187fcc1a4496c7ce2a0a32c7
https://doi.org/10.1074/jbc.ra120.014087

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Actinobacterial Coproheme Decarboxylases Use Histidine as a Distal Base to Promote Compound I Formation

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::99703bb7c5f29da94288a765c8118bba
https://doi.org/10.1021/acscatal.0c00411

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Impact of the dynamics of the catalytic arginine on nitrite and chlorite binding by dimeric chlorite dismutase

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3bdadd3a8e6ba2843e719e63f7feaac7
https://pubmed.ncbi.nlm.nih.gov/34922158

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On the Track of Long-Range Electron Transfer in B-Type Dye-Decolorizing Peroxidases: Identification of a Tyrosyl Radical by Computational Prediction and Electron Paramagnetic Resonance Spectroscopy

Autor: Kevin Nys, Paul G. Furtmüller, Vera Pfanzagl, Christian Obinger, Sabine Van Doorslaer

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::61c6fa0fedaee6eea72e014feca960ac
https://pubmed.ncbi.nlm.nih.gov/33784066

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Reaction of human peroxidasin 1 compound I and compound II with one-electron donors

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::00441000b7dd50b35007ba13255cb8a8
https://pubmed.ncbi.nlm.nih.gov/31953133

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In Vitro Heme Coordination of a Dye-Decolorizing Peroxidase—The Interplay of Key Amino Acids, pH, Buffer and Glycerol

Autor: Vera Pfanzagl, Christian Obinger, Sabine Van Doorslaer, Kevin Nys, Jeroen Roefs

Publikováno v: International Journal of Molecular Sciences
Volume 22
Issue 18
International journal of molecular sciences
International Journal of Molecular Sciences, Vol 22, Iss 9849, 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://explore.openaire.eu/search/publication?articleId=doi_dedup___::1bac1ddfb239b5f30d2f7ca775a43ef5
https://doi.org/10.3390/ijms22189849

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