Chrysotherapy is an important treatment for rheumatoid arthritis. 1,2 Metabolic transformations of the first-and secondgeneration gold drugs (Myochrysine, Solganol, and auranofin) begin with the displacement of their thiolate ligands via ligand exchange reactions with serum proteins and may culminate at inflammatory sites where dicyanoaurate(I) is formed. 3 It is a common metabolite of all three gold drugs, found in the serum and urine of patients, 4 and must be transported from the inflamed sites to the kidneys. Serum albumin carries up to 95% of the serum gold, and may be a transport agent for [Au(CN) 2 -].The dicyanoaurate(I) ion is linear with d(Au-C) ) 197.1(1) pm, d(CN) ) 146(1) pm, and ∠C-Au-C ) 179(2)°for three independent ions in Tl[Au(CN) 2 ] 5 and has an extremely large binding constant, log β 2 ) 36.6. 6 13 C NMR studies of albumindicyanoaurate(I) complexes, their equilibrium binding constants (K 1 ) 5.5 × 10 4 and K 2 ) 5.5 × 10 3 ), and the similarity of reactions of native and sulfhydryl-modified albumin all provide indirect evidence that multiple, intact dicyanoaurate(I) ions bind to albumin, 7,8 unlike gold drugs which undergo ligand exchange reactions preferentially or exclusively at cysteine 34. [9][10][11] Mo ¨ssbauer spectroscopy using the 77 keV resonance of 197 Au is a suitable technique for characterizing gold complexes [12][13][14][15][16][17] and is applicable to noncrystalline materials. It provides a method to distinguish among (i) adduct formation by intact dicyanoaurate-