Ziel dieser Arbeit war die röntgenkristallographische Untersuchung und Strukturlösung der Protoporphyrinogen IX Oxidase aus Nicotiana tabacum (Tabak), des blauen Cupredoxins Umecyanin aus Armoracia rusticana (Meerrettich) und dreier Ligandenkomplexe der Lumazinsynthase-Mutante W27Y aus Schizosaccharomyces pombe (Spalthefe). Protoporphyrinogen IX Oxidase (PPO), das letzte gemeinsame Enzym der Häm- und der Chlorophyllbiosynthese, katalysiert die Oxidation von Protoporphyrinogen IX zum vollständig konjugierten Protoporphyrin IX. Im Rahmen dieser Arbeit wird die Kristallstruktur der mitochondrialen PPO aus Tabak (Nicotiana tabacum) bei einer Auflösung von 2,9 Å im Komplex mit einem Phenylpyrazol-Inhibitor vorgestellt und beschrieben. Die Struktur wurde mittels Single Wavelength Anomalous Diffraction (SAD) gelöst, eine Datensatzaufnahme war nur möglich mit Hilfe des Free-mounting System. Es wird ein Komplex mit der Ferrochelatase vorgestellt, dem nächsten Enzym in der Hämbiosynthese.     «

Ziel dieser Arbeit war die röntgenkristallographische Untersuchung und Strukturlösung der Protoporphyrinogen IX Oxidase aus Nicotiana tabacum (Tabak), des blauen Cupredoxins Umecyanin aus Armoracia rusticana (Meerrettich) und dreier Ligandenkomplexe der Lumazinsynthase-Mutante W27Y aus Schizosaccharomyces pombe (Spalthefe). Protoporphyrinogen IX Oxidase (PPO), das letzte gemeinsame Enzym der Häm- und der Chlorophyllbiosynthese, katalysiert die Oxidation von Protoporphyrinogen IX zum vollständig...     »

It was the aim of this work to characterize and solve the structure of the protoporphyrinogen IX oxidase from Nicotiana tabacum by x-ray crystallography, furthermore solve the structure of the blue cupredoxin Umecayanin fom Armoracia rusticana (horse raddish) and of three ligand complexes of the lumazine synthase W27Y mutant from SChizosaccharomyces pombe (fission yeast). Protoporphyrinogen IX Oxidase (PPO), the last common enzyme in heme and chlorophyll biosynthesis, catalyses the oxidation of protoporphyrinogen IX to the fully conjugates protoporphyrin IX. In the this work, the crystal structure of the mitochondrial PPO from common tobacco (Nicotiana tabacum) is described as it was solved at a resolution of 2.9 Å in complex with a phenylpyrazole inhibitor. The structure was solved via single wavelength anomalous diffraction (SAD), measuring a data set was only possible with the help of the free-mounting system. A modelled complex with ferrochelatase is presented, the next enzyme in heme biosynthesis. It was the aim of this work to characterize and solve the structure of the protoporphyrinogen IX oxidase from Nicotiana tabacum by x-ray crystallography, furthermore solve the structure of the blue cupredoxin Umecayanin fom Armoracia rusticana (horse raddish) and of three ligand complexes of the lumazine synthase W27Y mutant from SChizosaccharomyces pombe (fission yeast). Protoporphyrinogen IX Oxidase (PPO), the last common enzyme in heme and chlorophyll biosynthesis, catalyses the oxidation of protoporphyrinogen IX to the fully conjugates protoporphyrin IX. In the this work, the crystal structure of the mitochondrial PPO from common tobacco (Nicotiana tabacum) is described as it was solved at a resolution of 2.9 Å in complex with a phenylpyrazole inhibitor. The structure was solved via single wavelength anomalous diffraction (SAD), measuring a data set was only possible with the help of the free-mounting system. A modelled complex with ferrochelatase is presented, the next enzyme in heme biosynthesis.     «

It was the aim of this work to characterize and solve the structure of the protoporphyrinogen IX oxidase from Nicotiana tabacum by x-ray crystallography, furthermore solve the structure of the blue cupredoxin Umecayanin fom Armoracia rusticana (horse raddish) and of three ligand complexes of the lumazine synthase W27Y mutant from SChizosaccharomyces pombe (fission yeast). Protoporphyrinogen IX Oxidase (PPO), the last common enzyme in heme and chlorophyll biosynthesis, catalyses the oxidation of...     »