Molecular Interaction between Frataxin and Ferrochelatase During Heme Assembly

Abstract

Frataxin, a mitochondrial protein known to be important in cellular iron homeostasis, has been suggested to serve as an iron chaperone during heme synthesis. Here we report an extensive biophysical characterization of the intermolecular interaction between yeast frataxin (Yfhl) and yeast ferrochelatase (Hem15). Yfh1 iron-binding residues on the Hem15 binding surface were mutated and characterized regarding complex formation. Our results suggest redundancy in Yfhl iron-binding sites for in vivo iron delivery during heme biosynthesis.