ATP‐dependent modulation and autophosphorylation of rapeseed 2‐Cys peroxiredoxin

摘要: 2-Cys peroxiredoxins (2-Cys Prx) are ubiquitous thiol-containing peroxidases that have been implicated in antioxidant defense and signal transduction. Although their biochemical features extensively studied, little is known about the mechanisms link redox activity non-redox processes. Here we report concerted action of a nucleoside triphosphate Mg2+ on rapeseed 2-Cys Prx reversibly impairs peroxidase promotes formation high molecular mass species. Using protein intrinsic fluorescence analysis site-directed mutants, demonstrate ATP quenches emission intensity Trp179, residue close to conserved Cys175. More importantly, found facilitates autophosphorylation when successively reduced with thiol-bearing compounds oxidized hydroperoxides or quinones. MS analyses reveal incorporates phosphoryl group into Cys175 yielding sulfinic-phosphoryl [Prx-(Cys175)-SO2PO32−] sulfonic-phosphoryl [Prx-(Cys175)-SO3PO32−] anhydrides. Hence, functional coupling between Prx gives novel insights not only removal reactive oxygen species, but also energy status cell oxidation cysteine residues.