Nqo15’s iron-binding properties were studied using NMR, fluorescence, and specific assays and its desulfurase activation by biochemical assays. We found that the recombinant Nqo15 isolated from complex I is monomeric, stable, folded in solution, and highly dynamic. Nqo15 does not share the iron-binding properties of FXN or its desulfurase activation function.
Tuesday, February 6, 2024
Searching for Frataxin Function: Exploring the Analogy with Nqo15, the Frataxin-like Protein of Respiratory Complex I from Thermus thermophilus
Doni, D.; Cavallari, E.; Noguera, M.E.; Gentili, H.G.; Cavion, F.; Parisi, G.; Fornasari, M.S.; Sartori, G.; Santos, J.; Bellanda, M.; et al. Searching for Frataxin Function: Exploring the Analogy with Nqo15, the Frataxin-like Protein of Respiratory Complex I from Thermus thermophilus. Int. J. Mol. Sci. 2024, 25, 1912. doi:10.3390/ijms25031912
