Comparative Conformational Studies of Bacterial and Human Peroxiredoxins Using Hydrogen Deuterium Exchange Mass Spectrometry

摘要

HX-MS data of human Prx2 exhibited relatively lower deuterium incorporation levels compared to its bacterial counterparts. The retarded exchange dynamics observed for Prx2 provides good support to our hypothesis that higher propensity to overoxidation is associated with stabilizing interactions that hamper local unfolding of the active site loop region, which is required for disulfide formation in the catalytic cycle and protection against overoxidation. The peptide-level relative deuterium incorporation values complement the crystal structure-derived B-factors and assist in determining the dynamics and allosteric mechanisms governing the catalytic activity of Prxs, the sensitivity of the Cp-residue to hyperoxidation and redox-sensitive oligomerization.