Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Axel Sündermann"'
Autor:
Axel Sündermann, Chris Oostenbrink
Publikováno v:
Protein Science. 22:1183-1195
Cytochrome P450 reductase (CYPOR) undergoes a large conformational change to allow for an electron transfer to a redox partner to take place. After an internal electron transfer over its cofactors, it opens up to facilitate the interaction and electr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e83baad67c1db18083a4599e0d4ea238
https://doi.org/10.1002/pro.2307
https://doi.org/10.1002/pro.2307
Autor:
Axel, Sündermann, Roland, Solc, Daniel, Tunega, Georg, Haberhauer, Martin H, Gerzabek, Chris, Oostenbrink
Publikováno v:
Journal of molecular graphicsmodelling. 62
Humic substances are ubiquitous in the environment and have manifold functions. While their composition is well known, information on the chemical structure and three-dimensional conformation is scarce. Here we describe the Vienna Soil-Organic-Matter
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e555cc562719aba4347eb18e5695546e
https://pubmed.ncbi.nlm.nih.gov/26521208
https://pubmed.ncbi.nlm.nih.gov/26521208
Autor:
Christian Obinger, Andrea Nicolussi, Katharina F. Pirker, Paul G. Furtmüller, Christa Jakopitsch, Marcel Zamocky, Bernhard Gasselhuber, Chris Oostenbrink, Michael M. H. Graf, Ignacio Fita, Stefan Hofbauer, Axel Sündermann, Xavi Carpena
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
instname
Bernhard Gasselhuber et al.
© 2015 American Chemical Society. Recently, it was demonstrated that bifunctional catalase-peroxidases (KatGs) are found not only in archaea and bacteria but also in lower eukaryotes. Structural studies and prelimina
© 2015 American Chemical Society. Recently, it was demonstrated that bifunctional catalase-peroxidases (KatGs) are found not only in archaea and bacteria but also in lower eukaryotes. Structural studies and prelimina
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::213d1bb242cf1375f8f57ca2d8a46223
http://hdl.handle.net/10261/123942
http://hdl.handle.net/10261/123942
Autor:
Stefan, Hofbauer, Clemens, Gruber, Katharina F, Pirker, Axel, Sündermann, Irene, Schaffner, Christa, Jakopitsch, Chris, Oostenbrink, Paul G, Furtmüller, Christian, Obinger
Publikováno v:
Biochemistry
Chlorite dismutases (Clds) are heme b-containing prokaryotic oxidoreductases that catalyze the reduction of chlorite to chloride with the concomitant release of molecular oxygen. Over time, they are irreversibly inactivated. To elucidate the mechanis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ae6742a6b1d7c4445c4658a692b27909
https://pubmed.ncbi.nlm.nih.gov/24754261
https://pubmed.ncbi.nlm.nih.gov/24754261
Autor:
Axel, Sündermann, Chris, Oostenbrink
Publikováno v:
Protein science : a publication of the Protein Society. 22(9)
Cytochrome P450 reductase (CYPOR) undergoes a large conformational change to allow for an electron transfer to a redox partner to take place. After an internal electron transfer over its cofactors, it opens up to facilitate the interaction and electr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::146bae0a1483b57f0bc24590d25dd4eb
https://pubmed.ncbi.nlm.nih.gov/23832577
https://pubmed.ncbi.nlm.nih.gov/23832577
Autor:
Stefan, Hofbauer, Marzia, Bellei, Axel, Sündermann, Katharina F, Pirker, Andreas, Hagmüller, Georg, Mlynek, Julius, Kostan, Holger, Daims, Paul G, Furtmüller, Kristina, Djinović-Carugo, Chris, Oostenbrink, Gianantonio, Battistuzzi, Christian, Obinger
Publikováno v:
Biochemistry
Chlorite dismutases (Clds) are heme b-containing oxidoreductases that convert chlorite to chloride and dioxygen. In this work, the thermodynamics of the one-electron reduction of the ferric high-spin forms and of the six-coordinate low-spin cyanide a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::0a9cffc1839d8a9e4f96b701501564aa
https://hdl.handle.net/11380/844090
https://hdl.handle.net/11380/844090