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• W1998456427 abstract "Frataxin is a mitochondrial protein that is defective in Friedreich's ataxia resulting in iron accumulation and an environment prone to Fenton reactions. We report that frataxin is susceptible to carbonylation and nitration modifications in residues from the beta-sheet surface (Tyr143, Tyr174, Tyr205 and Trp155). Frataxin functions are not significantly affected: frataxin-mediated protection against ROS is still observed, as well as iron-binding (5 Fe(3+)mol(-1), K(d) from 13-36 microM) necessary for the metallochaperone activity. However, the protein is up to 1.0 kcal mol(-1) destabilized, with conformational opening. Interestingly, the strictly conserved Trp155, which is mutated in patients, may be a functional hotspot in frataxin." @default.
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• W1998456427 date "2009-12-01" @default.
• W1998456427 modified "2023-09-24" @default.
• W1998456427 title "The conserved Trp155 in human frataxin as a hotspot for oxidative stress related chemical modifications" @default.
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• W1998456427 doi "https://doi.org/10.1016/j.bbrc.2009.10.095" @default.
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