Abstract
Abstract Our laboratory has extensively examined the inorganic biochemistry of antiarthritic gold drugs and selected analogues, focusing on their protein chemistry. The reactions of oligomeric gold(I) drugs and the monomeric oral drug, auranofin, with serum albumin, hemoglobin and metallothionein and the nature of the gold binding sites on these proteins are described in this Comment. A possible mechanism for oxidation of triethylphosphine in serum and additional insights into the pharmacology of gold drugs are discussed.
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