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

ABSTRACT: This work studies the stability of wild-type frataxin and some of its variants found in cancer tissues upon Co²⁺ binding. Although the physiologically involved metal ion in the frataxin enzymatic activity is Fe²⁺, as it is customarily done, Co²⁺ is most often used in experiments because Fe²⁺ is extremely unstable owing to the fast oxidation reaction Fe²⁺ → Fe³⁺. Protein stability is monitored following the conformational changes induced by Co²⁺ binding as measured by circular dichroism, fluorescence spectroscopy, and melting temperature measurements. The stability ranking among the wild-type frataxin and its variants obtained in this way is confirmed by a detailed comparative analysis of the XAS spectra of the met

SUBMITTER: Morante S 

PROVIDER: S-EPMC9195147 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature