Mechanism based on the work of Lowther, W.T., Brot, N., Weissbach, H., Honek, J.F. and Matthews B.W. Thiol-disulfide exchange is involved in the catalytic mechanism of peptide methionine sulfoxide reductase Proc. Natl. Acad. Sci. USA 97 (2000) 6463-6468 [PMID: 10841552] and Boschi-Muller, S., Azza, S., Sanglier-Cianferani, S., Talfournier, F., Van Dorsselear, A. and Branlant, G. A sulfenic acid enzyme intermediate is involved in the catalytic mechanism of peptide methionine sulfoxide reductase from Escherichia coli. J. Biol. Chem. 275 (2000) 35908-35913 [PMID: 10964927] on EC 184.108.40.206 but presumably applies to EC 220.127.116.11, EC 18.104.22.168 and EC 22.214.171.124.
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After thiol-disulfide exchange, the disulfide bond of the enzyme is reduced by other reductants, often thiols.
EC 126.96.36.199 peptide-L-methionine (S)-S-oxide reductase
EC 188.8.131.52 peptide-methionine (R)-S-oxide reductase
EC 184.108.40.206 L-methionine (S)-S-oxide reductase
EC 220.127.116.11 L-methionine (R)-S-oxide reductase