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Hydrogen peroxide (H 2 O 2 ) acts as a signaling messenger by triggering the reversible oxidation of redox-regulated proteins. It remains unclear how proteins can be oxidized by signaling levels of H 2 O 2 in the presence of peroxiredoxins, which are highly efficient peroxide scavengers. Here we show that the rapid formation of disulfide bonds in cytosolic proteins is enabled, rather than competed, by cytosolic 2-Cys peroxiredoxins. Under the conditions tested, the combined deletion or depletion of cytosolic peroxiredoxins broadly frustrated H 2 O 2 -dependent protein thiol oxidation, which is the exact opposite of what would be predicted based on the assumption that H 2 O 2 oxidizes proteins directly. We find that peroxiredoxins enable rapid and sensitive protein thiol oxidation by relaying H 2 O 2 -derived oxidizing equivalents to other proteins. Although these findings do not rule out the existence of Prx-independent H 2 O 2 signaling mechanisms, they suggest a broader role for peroxiredoxins as sensors and transmitters of H 2 O 2 signals than hitherto recognized.

A role for 2-Cys peroxiredoxins in facilitating cytosolic protein thiol oxidation