Quinones and their glutathione conjugates as irreversible inhibitors of gluthathione S-transferases

article
Quinones are known for their reactivity towards sulfhydryl groups, and thus are potential protein alkylating compounds. Human exposure to these compounds arises either from naturally occurring quinones or from quinones formed as metabolites from aromatic compounds. Normally, quinones are detoxified by conjugation with glutathione, producing the hydroquinone conjugates. Certain quinones, however, retain their oxidized nature after conjugation (e.g. halogen substituted quinones), while the hydroquinone conjugates have been shown to undergo intracellular oxidation. Thus, glutathione conjugates of quinones are formed, which display a special type of reactivity, i.e. selective inhibition of glutathione S-transferase isoenzymes (GST). This paper describes the development and use of glutathione conjugates of chlorinated benzoquinones as inhibitors of glutathione S-transferases.
Chemicals/CAS: 2-gluthionyl-3,5,6-trichloro-1,4-benzoquinone, 117383-28-5; Benzoquinones; Chloranil, 118-75-2; Glutathione Transferase, EC 2.5.1.18; Glutathione, 70-18-8; Isoenzymes
TNO Identifier
63802
ISSN
0065275X
Publisher
Plenum Press
Source title
Biological reactive intermediates : IV. molecular and cellular effects and their impact on human health
Editor(s)
Witmer, C.M.
Snyder, R.L.
Jollow, D.J.
Place of publication
New York
Pages
403-406
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