Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Hanna Michlits"'
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
Publikováno v:
Biomolecules; Volume 13; Issue 6; Pages: 946
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
Autor:
Federico Sebastiani, Chiara Niccoli, Hanna Michlits, Riccardo Risorti, Maurizio Becucci, Stefan Hofbauer, Giulietta Smulevich
Publikováno v:
Journal of Raman Spectroscopy. 53:890-901
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:
Federico Sebastiani, Riccardo Risorti, Chiara Niccoli, Hanna Michlits, Maurizio Becucci, Stefan Hofbauer, Giulietta Smulevich
Coproheme decarboxylases (ChdCs) are utilized by monoderm bacteria to produce heme b by a stepwise oxidative decarboxylation of the 2- and 4-propionate groups of iron coproporphyrin III (coproheme) to vinyl groups. This work compares the effect of he
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7453acd2ea93c715af47efe189014b7a
http://hdl.handle.net/2158/1254141
http://hdl.handle.net/2158/1254141
Autor:
Federico, Sebastiani, Chiara, Niccoli, Hanna, Michlits, Riccardo, Risorti, Maurizio, Becucci, Stefan, Hofbauer, Giulietta, Smulevich
Publikováno v:
Journal of Raman spectroscopy : JRS. 53(5)
The actinobacterial coproheme decarboxylase from
Autor:
Christian Obinger, Giulietta Smulevich, Stefan Hofbauer, Chris Oostenbrink, Hanna Michlits, Federico Sebastiani, Bettina Lier, Paul G. Furtmüller, Maurizio Becucci
Publikováno v:
Biophys J
Monoderm bacteria utilize coproheme decarboxylases (ChdCs) to generate heme b by a stepwise decarboxylation of two propionate groups of iron coproporphyrin III (coproheme), forming two vinyl groups. This work focuses on actinobacterial ChdC from Cory
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::45768df218b9e8f6d5d5a0c52169b650
http://hdl.handle.net/2158/1243069
http://hdl.handle.net/2158/1243069
Autor:
Lisa, Milazzo, Thomas, Gabler, Dominic, Pühringer, Zuzana, Jandova, Daniel, Maresch, Hanna, Michlits, Vera, Pfanzagl, Kristina, Djinović-Carugo, Chris, Oostenbrink, Paul G, Furtmüller, Christian, Obinger, Giulietta, Smulevich, Stefan, Hofbauer
Publikováno v:
ACS Catalysis
Coproheme decarboxylase (ChdC) catalyzes the last step in the heme biosynthesis pathway of monoderm bacteria with coproheme acting both as redox cofactor and substrate. Hydrogen peroxide mediates the stepwise decarboxylation of propionates 2 and 4 of