Zobrazeno 1 - 10
of 69
pro vyhledávání: '"Stefan Hofbauer"'
Autor:
Tobias Schachinger, Ann- Holik, Gerald Schrenk, Herbert Gritsch, Stefan Hofbauer, Paul Furtmüller, Peter Turecek
Publikováno v:
Bio-Protocol, Vol 14, Iss 17 (2024)
Accurate quantification of von Willebrand factor ristocetin cofactor activity (VWF:RCo) is critical for the diagnosis and classification of von Willebrand disease, the most common hereditary and acquired bleeding disorder in humans. Moreover, it is i
Externí odkaz:
https://doaj.org/article/53832fb005264100a5d77328232d05fa
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 21, Iss , Pp 3933-3945 (2023)
The coproporphyrin dependent heme biosynthesis pathway is almost exclusively utilized by Gram-positive bacteria. This fact makes it a worthwhile topic for basic research, since a fundamental understanding of a metabolic pathway is necessary to transl
Externí odkaz:
https://doaj.org/article/ab02ec0ce2e047a6802aaf72e316ed4f
Publikováno v:
Biology, Vol 12, Iss 12, p 1527 (2023)
Coproporphyrinogen oxidase (CgoX) and protoporphyrinogen oxidase (PgoX) catalyze the oxidation of the flexible cyclic tetrapyrrole of porphyrinogen compounds into fully conjugated, planar macrocyclic porphyrin compounds during heme biosynthesis. Thes
Externí odkaz:
https://doaj.org/article/eff91766a6a64e459c2ac5fb67d6e5f1
Publikováno v:
Biomolecules, Vol 13, Iss 6, p 946 (2023)
Coproheme decarboxylases (ChdCs) are terminal enzymes of the coproporphyrin-dependent heme biosynthetic pathway. In this reaction, two propionate groups are cleaved from the redox-active iron-containing substrate, coproheme, to form vinyl groups of t
Externí odkaz:
https://doaj.org/article/d98dd22039d54f0aba0bed8c7716a430
Publikováno v:
Frontiers in Bioengineering and Biotechnology, Vol 9 (2022)
The oxidative decarboxylation of coproheme to form heme b by coproheme decarboxylase is a stereospecific two-step reaction. In the first step, the propionate at position two (p2) is cleaved off the pyrrole ring A to form a vinyl group at this positio
Externí odkaz:
https://doaj.org/article/ec3e5663ff704cae9beda2e92b60b1d7
Autor:
Federico Sebastiani, Chiara Baroni, Gaurav Patil, Andrea Dali, Maurizio Becucci, Stefan Hofbauer, Giulietta Smulevich
Publikováno v:
Biomolecules, Vol 13, Iss 2, p 235 (2023)
Monoderm bacteria accumulate heme b via the coproporphyrin-dependent biosynthesis pathway. In the final step, in the presence of two molecules of H2O2, the propionate groups of coproheme at positions 2 and 4 are decarboxylated to form vinyl groups by
Externí odkaz:
https://doaj.org/article/e289eb301f1b4da7b7af116ec4537c9b
Autor:
Montse Olivé, Martin Engvall, Gianina Ravenscroft, Macarena Cabrera-Serrano, Hong Jiao, Carlo Augusto Bortolotti, Marcello Pignataro, Matteo Lambrughi, Haibo Jiang, Alistair R. R. Forrest, Núria Benseny-Cases, Stefan Hofbauer, Christian Obinger, Gianantonio Battistuzzi, Marzia Bellei, Marco Borsari, Giulia Di Rocco, Helena M. Viola, Livia C. Hool, Josep Cladera, Kristina Lagerstedt-Robinson, Fengqing Xiang, Anna Wredenberg, Francesc Miralles, Juan José Baiges, Edoardo Malfatti, Norma B. Romero, Nathalie Streichenberger, Christophe Vial, Kristl G. Claeys, Chiara S. M. Straathof, An Goris, Christoph Freyer, Martin Lammens, Guillaume Bassez, Juha Kere, Paula Clemente, Thomas Sejersen, Bjarne Udd, Noemí Vidal, Isidre Ferrer, Lars Edström, Anna Wedell, Nigel G. Laing
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-14 (2019)
Myoglobin is a hemeprotein that reversibly binds oxygen and gives muscle its red color. Here, the authors report a genetic variant in the MB gene that associates with myoglobinopathy, an autosomal dominant progressive myopathy, and altered oxygen bin
Externí odkaz:
https://doaj.org/article/66b676bb69fb44be94c22654e712d730
Autor:
Federico Sebastiani, Chiara Niccoli, Hanna Michlits, Riccardo Risorti, Maurizio Becucci, Stefan Hofbauer, Giulietta Smulevich
Publikováno v:
Journal of Raman Spectroscopy. 53:890-901
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e90d5fbd76b85550150d305368bdc030
https://doi.org/10.1002/jrs.6326
https://doi.org/10.1002/jrs.6326
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c4075326a5761cc5a564bd7942257f79
https://doi.org/10.1002/pro.4534
https://doi.org/10.1002/pro.4534