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Diastereoselective reduction of protein‐bound methionine sulfoxide by methionine sulfoxide reductase
Author(s) -
Sharov Victor S.,
Ferrington Deborah A.,
Squier Thomas C.,
Schöneich Christian
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00888-1
Subject(s) - methionine sulfoxide reductase , methionine , methionine sulfoxide , sulfoxide , chemistry , biochemistry , reduction (mathematics) , dimethyl sulfoxide , organic chemistry , amino acid , mathematics , geometry
Methionine sulfoxide (MetSO) in calmodulin (CaM) was previously shown to be a substrate for bovine liver peptide methionine sulfoxide reductase (pMSR, EC 1.8.4.6), which can partially recover protein structure and function of oxidized CaM in vitro. Here, we report for the first time that pMSR selectively reduces the D ‐sulfoxide diastereomer of CaM‐bound L ‐MetSO ( L ‐Met‐ D ‐SO). After exhaustive reduction by pMSR, the ratio of L ‐Met‐ D ‐SO to L ‐Met‐ L ‐SO decreased to about 1:25 for hydrogen peroxide‐oxidized CaM, and to about 1:10 for free MetSO. The accumulation of MetSO upon oxidative stress and aging in vivo may be related to incomplete, diastereoselective, repair by pMSR.