Complex formation between protoporphyrinogen IX oxidase and ferrochelatase during haem biosynthesis in Thermosynechococcus elongatus

• DOI: 10.1099/mic.0.2008/018705-0
• Publication Date: 2008-12-02T01:32:59Z
• Authors: Ava Masoumi; Ilka Ursula Heine...; Manfred Rohde; Michael Koch; Martina Jahn; Dieter Jahn
• Keywords: Protoporphyrinogen oxidase; Protoporphyrin IX; Ferrochelatase; Flavoprotein; Flavin adenine dinucleotide

During haem and chlorophyll biosynthesis, flavin-dependent protoporphyrinogen IX oxidase catalyses the six-electron oxidation of to form protoporphyrin IX. In following step, iron is inserted into by ferrochelatase. Based on solved crystal structures these enzymes, an in silico model for a complex between two enzymes was proposed protect highly photoreactive intermediate The existence this verified independent techniques. First, co-immunoprecipitation experiments using antibodies directed against recombinantly produced purified Thermosynechococcus elongatus ferrochelatase demonstrated their physical interaction. Secondly, protein formation visualized vivo immunogold labelling electron microscopy with T. cells. Finally, oxygen-dependent coproporphyrinogen III oxidase, which IX, not found be part when analysed same methodology.