The data reported in this study reveal that the currently reported binding stoichiometries should be taken with caution. The use of a spin label resistant to reduction, as well as the comparison of the binding effect of Fe2+ in wild type and in the pathological D122Y variant of frataxin, allowed us to characterize the Fe2+ binding properties of different protein sites and highlight the effect of the D122Y substitution on the surrounding residues. We suggest that both Fe2+ and Fe3+ might play a relevant role in the context of the proposed FXN physiological functions.
Friday, December 18, 2020
Effects of Fe2+/Fe3+ Binding to Human Frataxin and Its D122Y Variant, as Revealed by Site-Directed Spin Labeling (SDSL) EPR Complemented by Fluorescence and Circular Dichroism Spectroscopies
Doni, D.; Passerini, L.; Audran, G.; Marque, S.R.A.; Schulz, M.; Santos, J.; Costantini, P.; Bortolus, M.; Carbonera, Int. J. Mol. Sci. 2020, 21, 9619. doi:10.3390/ijms21249619
