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During systemic inflammation, indoleamine 2,3-dioxygenase 1 (IDO1) becomes expressed in endothelial cells where it uses hydrogen peroxide (H 2 O 2 ) to oxidize L-tryptophan to the tricyclic hydroperoxide,  cis -WOOH, that then relaxes arteries via oxidation of protein kinase G 1α. Here we show that arterial glutathione peroxidases and peroxiredoxins that rapidly eliminate H 2 O 2 , have little impact on relaxation of IDO1-expressing arteries, and that purified IDO1 forms  cis -WOOH in the presence of peroxiredoxin 2.  cis -WOOH oxidizes protein thiols in a selective and stereospecific manner. Compared with its epimer  trans -WOOH and H 2 O 2 ,  cis -WOOH reacts slower with the major arterial forms of glutathione peroxidases and peroxiredoxins while it reacts more readily with its target, protein kinase G 1α. Our results indicate a paradigm of redox signaling by H 2 O 2  via its enzymatic conversion to an amino acid-derived hydroperoxide that ‘escapes’ effective reductive inactivation to engage in selective oxidative activation of key target proteins.

Hydrogen peroxide signaling via its transformation to a stereospecific alkyl hydroperoxide that escapes reductive inactivation