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J Biol Chem, Vol. 274, Issue 51, 36039-36042, December 17, 1999

COMMUNICATION
Reactivity of Glutaredoxins 1, 2, and 3 from Escherichia coli Shows That Glutaredoxin 2 Is the Primary Hydrogen Donor to ArsC-catalyzed Arsenate Reduction^*

Jin Shi, Alexios Vlamis-Gardikas^§, Fredrik Åslund^§, Arne Holmgren^§, and Barry P. Rosen^¶

From the  Department of Biochemistry and Molecular Biology, Wayne State University, School of Medicine, Detroit, Michigan 48201 and the ^§ Medical Nobel Institute for Biochemistry, Department of Medical Biochemistry and Biophysics, Karolinska Institute, S-171 77, Stockholm, Sweden

In Escherichia coli ArsC catalyzes the reduction of arsenate to arsenite using GSH with glutaredoxin as electron donors. E. coli has three glutaredoxins: 1, 2, and 3, each with a classical -Cys-Pro-Tyr-Cys- active site. Glutaredoxin 2 is the major glutathione disulfide oxidoreductase in E. coli, but its function remains unknown. In this report glutaredoxin 2 is shown to be the most effective hydrogen donor for the reduction of arsenate by ArsC. Analysis of single or double cysteine-to-serine substitutions in the active site of the three glutaredoxins indicated that only the N-terminal cysteine residue is essential for activity. This suggests that, during the catalytic cycle, ArsC forms a mixed disulfide with GSH before being reduced by glutaredoxin to regenerate the active ArsC reductase.

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^* This work was supported by United States Public Health Service Grant GM52216 (to B. P. R.) and Swedish Cancer Society Grant 961 (to A.H.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ To whom correspondence and reprint requests should be addressed: Dept. of Biochemistry and Molecular Biology, Wayne State University, School of Medicine, 540 E. Canfield Ave., Detroit, MI 48201. Tel.: 313-577-1512; Fax: 313-577-2765; E-mail: brosen@med.wayne.edu.

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Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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