Frataxin is a mitochondrial iron-binding protein involved in iron storage, detoxification and delivery for iron sulfur-cluster assembly and hemebiosynthesis. The ability of frataxin from different organisms to populate multiple oligomeric states in the presence of metal ions, e.g. Fe2+ and Co2+, led to the suggestion that different oligomers contribute to the functions of frataxin. Here we report on the complex between yeast frataxin and ferrochelatase, the terminal enzyme of heme biosynthesis. The data support the proposal that frataxin-mediated delivery of potentially toxic iron species overcomes formation of reactive oxygen species.

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