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  • Title: Reduction and binding of arsenate and dimethylarsinate by glutathione: a magnetic resonance study.
    Author: Delnomdedieu M, Basti MM, Otvos JD, Thomas DJ.
    Journal: Chem Biol Interact; 1994 Feb; 90(2):139-55. PubMed ID: 8156604.
    Abstract:
    By observing the chemical shifts of the proton and carbon-13 nuclei of reduced glutathione, the interactions of arsenate, arsenite and dimethylarsinate with this tripeptide have been characterized. These spectral studies show the reduction and complexation of arsenic to be a two-step process. Initially, the oxidation of 2 mol of glutathione reduces arsenate to arsenite. Then, 3 mol of glutathione are consumed in the formation of a glutathione-arsenite complex. Similar experiments with arsenite identified a (glutathione)3-arsenite complex; however, no oxidized glutathione was detected. The arsenite binding site in the glutathione-arsenite complex is the cysteinyl sulfhydryl. The glutathione-arsenite complex is stable over the pH range from 1.5 to 7.0-7.5. At higher pH, dissociation occurs releasing reduced glutathione. For a glutathione to dimethylarsinate ratio of 3, oxidized glutathione is also coupled with a reduction to trivalent dimethylarsinous acid, prior to the formation of a 1:1 glutathione-dimethylarsinite complex. The role of reduced glutathione in the metabolism of arsenic is consistent with the previously described effects of this agent on the organismic toxicity of arsenic.
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