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J. Biol. Chem., Vol. 281, Issue 42, 31184-31187, October 20, 2006
Selenocompounds Can Serve as Oxidoreductants with the Methionine Sulfoxide Reductase Enzymes*![]() ![]() ![]() 1
From the
In a recent study on the reducing requirement for the methionine sulfoxide reductases (Msr) (Sagher, D., Brunell, D., Hejtmancik, J. F., Kantorow, M., Brot, N. & Weissbach, H. (2006) Proc. Natl. Acad. Sci. U. S. A. 103, 86568661), we have shown that thioredoxin, although an excellent reducing system for Escherichia coli MsrA and MsrB and bovine MsrA, is not an efficient reducing agent for either human MsrB2 (hMsrB2) or human MsrB3 (hMsrB3). In a search for another reducing agent for hMsrB2 and hMsrB3, it was recently found that thionein, the reduced, metal-free form of metallothionein, could function as a reducing system for hMsrB3, with weaker activity using hMsrB2. In the present study, we provide evidence that some selenium compounds are potent reducing agents for both hMsrB2 and hMsrB3.
Received for publication, July 21, 2006 , and in revised form, August 15, 2006. * This is Contribution P200524 from the Center of Excellence in Biomedical and Marine Biotechnology, Florida Atlantic University, Boca Raton, FL, which partially funded these studies. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact. 1 To whom correspondence should be addressed: Center for Molecular Biology and Biotechnology, FL Atlantic University, 777 Glades Rd., Boca Raton, FL 33431. Tel.: 561-297-2596; Fax: 561-297-2594; E-mail: hweissba{at}fau.edu.
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