Glutaredoxin serves as a reductant for methionine sulfoxide reductases with or without resolving cysteine.

Methionine sulfoxide reductases A and B (MsrA and MsrB) have been known to be thioredoxin (Trx)-dependent enzymes that catalyze the reduction of methionine sulfoxide in a stereospecific manner. This work reports that glutaredoxin, another major thiol-disulfide oxidoreductase, can serve as a reductant for both MsrA and MsrB. Glutaredoxins efficiently reduced 1-Cys MsrA lacking a resolving Cys, which is not reducible by Trx. Glutaredoxins also reduced 3-Cys MsrA containing two resolving Cys. The glutaredoxin-dependent activity of the 3-Cys MsrA was comparable with the Trx-dependent activity. The kinetic data suggest that 1-Cys MsrA is more efficiently reduced by glutaredoxin than 3-Cys form. Also, glutaredoxins could function as a reductant for 1-Cys MsrB lacking a resolving Cys as previously reported. In contrast to the previous report, 2-Cys MsrB containing a resolving Cys was reducible by the glutaredoxins. Collectively, this study demonstrates that glutaredoxins reduce MsrAs and MsrBs with or without resolving Cys.

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