Metal Ion Binding in Wild-Type and Mutated Frataxin: A Stability Study

Morante, S.; Botticelli, S.; Chiaraluce, R.; Consalvi, V.; La Penna, G.; Novak, L.; et al. (2022); Frontiers. Collection. doi:10.3389/fmolb.2022.878017

We can explain the surprising feature emerging from a detailed analysis of the XANES region of the spectrum, showing that the longer 81-210 frataxin fragment has a smaller propensity for Co2+ binding than the shorter 90-210 one. This fact is explained by the peculiar role of the N-terminal disordered tail in modulating the protein ability to interact with the metal.

Metal Ion Binding in Wild-Type and Mutated Frataxin: A Stability Study