Selenocompounds can serve as oxidoreductants with the methionine sulfoxide reductase enzymes.
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, 8656-8661), 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.
Sagher
Daphna
D
Center for Molecular Biology and Biotechnology, Florida Atlantic University, Boca Raton, Florida 33431, USA.
Brunell
David
D
Brot
Nathan
N
Vallee
Bert L
BL
Weissbach
Herbert
H
D000818:Animals; D002417:Cattle; D003124:Colorimetry; D004305:Dose-Response Relationship, Drug; D004926:Escherichia coli / Q000378:metabolism; D006801:Humans; D008668:Metallothionein / Q000737:chemistry; D051150:Methionine Sulfoxide Reductases; D008956:Models, Chemical; D010088:Oxidoreductases / Q000737:chemistry* / Q000378:metabolism; D012643:Selenium / Q000737:chemistry; D051140:Selenoproteins / Q000737:chemistry*
D051140:Selenoproteins; D008668:Metallothionein; D010088:Oxidoreductases; D051150:Methionine Sulfoxide Reductases; C027219:methionine sulfoxide reductase; D012643:Selenium