Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Daniela Breckau"'
Autor:
Gunhild Layer, Lothar Jänsch, Daniela Breckau, Stephen E. J. Rigby, Helen K. Leech, Dirk W. Heinz, Martin J. Warren, Dieter Jahn, Antonio J. Pierik, I. Astner, Katrin Grage, Matthias Trost, Peter Heathcote
Publikováno v:
Journal of Biological Chemistry. 281:15727-15734
During porphyrin biosynthesis the oxygen-independent coproporphyrinogen III oxidase (HemN) catalyzes the oxidative decarboxylation of the propionate side chains of rings A and B of coproporphyrinogen III to form protoporphyrinogen IX. The enzyme util
Autor:
Peter Heathcote, Gunhild Layer, Ava Masoumi, Volker Schünemann, Katrin Grage, Daniela Breckau, Thomas Teschner, Alfred X. Trautwein, Martina Jahn, Dieter Jahn
Publikováno v:
Journal of Biological Chemistry. 280:29038-29046
The S-adenosylmethionine (AdoMet) radical enzyme oxygen-independent coproporphyrinogen III oxidase HemN catalyzes the oxidative decarboxylation of coproporphyrinogen III to protoporphyrinogen IX during bacterial heme biosynthesis. The recently solved
Autor:
Martina Jahn, Jürgen Moser, Rebekka Biedendieck, Susanne Schröder, Daniela Breckau, Rodrigo Arias-Cartin, Kalle Möbius, Dörte Becher, Anna-Lena Hännig, Axel Magalon, Katrin Riedmann, Dieter Jahn
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, 2010, 107 (23), pp.10436-10441. ⟨10.1073/pnas.1000956107⟩
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2010, 107 (23), pp.10436-10441. ⟨10.1073/pnas.1000956107⟩
Proceedings of the National Academy of Sciences of the United States of America, 2010, 107 (23), pp.10436-10441. ⟨10.1073/pnas.1000956107⟩
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2010, 107 (23), pp.10436-10441. ⟨10.1073/pnas.1000956107⟩
Cellular energy generation uses membrane-localized electron transfer chains for ATP synthesis. Formed ATP in turn is consumed for the biosynthesis of cellular building blocks. In contrast, heme cofactor biosynthesis was found driving ATP generation v
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::423e3f4c3693c3e3bfb4ae4abdc1d972
https://hal.science/hal-03248745
https://hal.science/hal-03248745
Autor:
Gunhild, Layer, Katrin, Grage, Thomas, Teschner, Volker, Schünemann, Daniela, Breckau, Ava, Masoumi, Martina, Jahn, Peter, Heathcote, Alfred X, Trautwein, Dieter, Jahn
Publikováno v:
The Journal of biological chemistry. 280(32)
The S-adenosylmethionine (AdoMet) radical enzyme oxygen-independent coproporphyrinogen III oxidase HemN catalyzes the oxidative decarboxylation of coproporphyrinogen III to protoporphyrinogen IX during bacterial heme biosynthesis. The recently solved
Publikováno v:
The Journal of biological chemistry. 278(47)
During heme biosynthesis in Escherichia coli two structurally unrelated enzymes, one oxygen-dependent (HemF) and one oxygen-independent (HemN), are able to catalyze the oxidative decarboxylation of coproporphyrinogen III to form protoporphyrinogen IX
Publikováno v:
Biochemical Society Transactions. 30:A75-A75