Zobrazeno 1 - 10
of 24
pro vyhledávání: '"Markus J. Bröcker"'
Autor:
Edward J. Reijerse, Hugo Scheer, Wolfhart Rüdiger, Svenja Kiesel, Dieter Jahn, Denise Wätzlich, Jürgen Moser, Markus J. Bröcker, Christiane Lange, Wolfgang Lubitz
Publikováno v:
Journal of Biological Chemistry. 290:1141-1154
Bacteriochlorophyll a biosynthesis requires the stereo- and regiospecific two electron reduction of the C7-C8 double bond of chlorophyllide a by the nitrogenase-like multisubunit metalloenzyme, chlorophyllide a oxidoreductase (COR). ATP-dependent COR
Publikováno v:
Angewandte Chemie. 126:325-330
Der Selenocystein(Sec)-Einbau in Proteine erfolgt in der Natur durch die kotranslationale Umkodierung eines UGA-Stopp-Codons. Diese Studie zeigt nun, dass Sec nicht ausschlieslich durch UGA, sondern vielmehr durch 58 aller 64 moglichen Codons kodiert
Autor:
Laure Prat, Gifty Hammond, Caroline Aldag, Abigail Plummer, Markus J. Bröcker, Michael J. Hohn, Dieter Söll
Publikováno v:
Angewandte Chemie International Edition. 52:1441-1445
Autor:
Wolf-Dieter Schubert, Sebastian Schomburg, Jürgen Moser, Markus J. Bröcker, Dieter Jahn, Dirk W. Heinz
Publikováno v:
Journal of Biological Chemistry. 285:27336-27345
During (bacterio)chlorophyll biosynthesis of many photosynthetically active organisms, dark operative protochlorophyllide oxidoreductase (DPOR) catalyzes the two-electron reduction of ring D of protochlorophyllide to form chlorophyllide. DPOR is comp
Autor:
Jürgen Moser, Friedhelm Lendzian, Markus J. Bröcker, Denise Wätzlich, Miguel Saggu, Dieter Jahn
Publikováno v:
Journal of Biological Chemistry. 285:8268-8277
Dark operative protochlorophyllide oxidoreductase (DPOR) catalyzes the light-independent two-electron reduction of protochlorophyllide a to form chlorophyllide a, the last common precursor of chlorophyll a and bacteriochlorophyll a biosynthesis. Duri
Autor:
Simone Virus, Jürgen Moser, Frank Uliczka, Dieter Jahn, Denise Wätzlich, Markus J. Bröcker, Markus W. Ribbe
Publikováno v:
Journal of Biological Chemistry. 284:15530-15540
Nitrogenase-like light-independent protochlorophyllide oxidoreductase (DPOR) is involved in chlorophyll biosynthesis. Bacteriochlorophyll formation additionally requires the structurally related chlorophyllide oxidoreductase (COR). During catalysis,
Autor:
Manfred Nimtz, Markus J. Bröcker, Denise Wätzlich, Jürgen Moser, Manfred Rohde, Johannes Walther, Dieter Jahn
Publikováno v:
FEMS Microbiology Letters. 290:156-163
The growing resistance against antibiotics demands the search for alternative treatment strategies. Photodynamic therapy is a promising candidate. The natural intermediate of chlorophyll biosynthesis, protochlorophyllide, was produced, purified and t
Autor:
Hugo Scheer, Miguel Saggu, Denise Wätzlich, Jürgen Moser, Markus J. Bröcker, Wolfhart Rüdiger, Dieter Jahn, Frank Uliczka, Friedhelm Lendzian, Simone Virus
Publikováno v:
Journal of Biological Chemistry. 283:29873-29881
Chlorophyll and bacteriochlorophyll biosynthesis requires the two-electron reduction of protochlorophyllide a ringDbya protochlorophyllide oxidoreductase to form chlorophyllide a. A light-dependent (light-dependent Pchlide oxidoreductase (LPOR)) and
Autor:
Stefanie Ganskow, Wolf-Dieter Schubert, Markus J. Bröcker, Simone Virus, Peter Heathcote, Jürgen Moser, Dieter Jahn, Dirk W. Heinz
Publikováno v:
Journal of Biological Chemistry. 283:10559-10567
During chlorophyll and bacteriochlorophyll biosynthesis in gymnosperms, algae, and photosynthetic bacteria, dark-operative protochlorophyllide oxidoreductase (DPOR) reduces ring D of aromatic protochlorophyllide stereospecifically to produce chloroph
Selenocysteine (Sec) is naturally incorporated into proteins by recoding the stop codon UGA. Sec is not hardwired to UGA, as the Sec insertion machinery was found to be able to site-specifically incorporate Sec directed by 58 of the 64 codons. For 15
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d7ec9c6630df8beaeff65098cadbc7ce
https://europepmc.org/articles/PMC4004526/
https://europepmc.org/articles/PMC4004526/