Paramagnetic tailored experiments for the NMR investigation of reduced and oxidized [2Fe-2S]-mitoNEET

We report here the complete data sets and the pulse programs for the NMR spectra of the human iron sulfur binding protein mitoNEET, in its oxidized and reduced states. These data have been used in the publication “The long-standing relationship between Paramagnetic NMR and Iron-Sulfur proteins: the mitoNEET example. An old method for new stories or the other way around?”. This folder includes: paramagnetic 1D proton NOE experiments, ¹⁵N-IR-HSQC-AP experiments and CON ¹³C direct detection experiments in their diamagnetic and paramagnetic version. All these data have been used to identify NMR signals of residues surrounding the metal cofactor. Along with the raw data we report also the pulse programs of the paramagnetic tailored experiments. The NMR spectra of both oxidation states of mitoNEET are significantly different from those reported for previously investigated [Fe₂S₂]^2+/+ proteins and provide a detailed description of the unique electronic properties of mitoNEET, that is essential for the understanding of its the biological function.