Activity of rat cytosolic thioredoxin reductase is strongly decreased by trans-[bis(2-amino-5methylthiazole)tetrachlororuthenate(III)]: First report of relevant thioredoxin reductase inhibition for a ruthenium compound

A novel '' Keppler type '' ruthenium(III) compound trans[bis(2-amino 5-methylthiazole)tetrachlororuthenate(III)] 1, of potential interest as an anticancer agent, was designed, synthesized, and characterized. Its interactions with various proteins were analyzed, including the selenoenzyme thioredoxin reductase, an emerging target for anticancer metallodrugs. The selective inhibition of the cytosolic form of this selenoenzyme was documented, this being the first report of significant thioredoxin reductase inhibition by a ruthenium compound.