The N-terminal part (residues 44 to 51) of the α 2 helix containing the Cp residue Cys47 is completely unwound, allowing a movement of this residue in the direction of the Cr residue Cys151. It is also necessary to displace the region containing the Cr residue Cys151in the direction of Cys47. This second movement involved residues 145 to 156 and included the N-terminal part of the 6 α helix.

The combination of these two movements finally allows the formation of the intramolecular disulfide.

The Crystal Structures of Oxidized Forms of Human Peroxiredoxin 5 with an Intramolecular Disulfide Bond Confirm the Proposed Enzymatic Mechanism for Atypical 2-Cys Peroxiredoxins. Smeets, A.,  Declercq, J.P. (2008) Arch.Biochem.Biophys. 477: 98-104 (PubMed)

PDB Number:2VL2 (PDB)