Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Dominic Pühringer"'
Autor:
Benjamin Salzer, Irene Schaffner, Kristina Djinović-Carugo, Michael W. Traxlmayr, Annika De Sousa Linhares, Wolfgang Holter, Manfred Lehner, Peter Steinberger, Nicole J. Yang, Christian Obinger, Charlotte U. Zajc, Markus Dobersberger, G. Mlynek, Dominic Pühringer
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Significance Molecular ON-switches are important tools in chemical biology, enabling protein–protein interactions to be regulated by small molecules. However, currently available ON-switches that induce conditional heterodimerization are suboptimal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e7f8213a9d6b594eef65dc5a3b709dc
http://europepmc.org/articles/PMC7334647
http://europepmc.org/articles/PMC7334647
Autor:
Leighton Coates, Giulietta Smulevich, Stefan Hofbauer, Irene Schaffner, Gianantonio Battistuzzi, Kristina Djinović-Carugo, Nicola Flego, Paul G. Furtmüller, Georg Mlynek, Marzia Bellei, Julian Libiseller-Egger, Christian Obinger, Dominic Pühringer
Publikováno v:
'ACS Catalysis ', vol: 7, pages: 7962-7976 (2017)
ACS Catalysis
ACS Catalysis
The heme enzyme chlorite dismutase (Cld) catalyzes the degradation of chlorite to chloride and dioxygen. Although structure and steady-state kinetics of Clds have been elucidated, many questions remain (e.g., the mechanism of chlorite cleavage and th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2cd536ce6d7bcf33db70cfc9439c0ff4
https://epn-library.esrf.fr/flora/jsp/index_view_direct_anonymous.jsp?record=doc:PUB_ESRF:48367
https://epn-library.esrf.fr/flora/jsp/index_view_direct_anonymous.jsp?record=doc:PUB_ESRF:48367
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::0feae02dad4e40fadb46cd0ea6b08093
https://pubmed.ncbi.nlm.nih.gov/31423350
https://pubmed.ncbi.nlm.nih.gov/31423350
Autor:
Dominic Pühringer
Publikováno v:
Acta Crystallographica Section A Foundations and Advances. 75:e118-e118
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::93a3b180997399dd346daedec7356b55
https://doi.org/10.1107/s2053273319094385
https://doi.org/10.1107/s2053273319094385
Autor:
Stefan, Hofbauer, Georg, Mlynek, Lisa, Milazzo, Dominic, Pühringer, Daniel, Maresch, Irene, Schaffner, Paul G, Furtmüller, Giulietta, Smulevich, Kristina, Djinović-Carugo, Christian, Obinger
Publikováno v:
The Febs Journal
Heme biosynthesis in Gram‐positive bacteria follows a recently described coproporphyrin‐dependent pathway with HemQ catalyzing the decarboxylation of coproheme to heme b. Here we present the first crystal structure of a HemQ (homopentameric copro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::2e47d7862a7ec958c01c3101278ed1f0
https://pubmed.ncbi.nlm.nih.gov/27758026
https://pubmed.ncbi.nlm.nih.gov/27758026