Coffer M T, Shaw C F, Hormann A L, Mirabelli C K, Crooke S T
Department of Chemistry, University of Wisconsin, Milwaukee.
J Inorg Biochem. 1987 Jul;30(3):177-87. doi: 10.1016/0162-0134(87)80062-4.
Thiols (RSH = 2,3,4,6-tetra-O-acetyl-beta-1-D-thioglucose, beta-1-D-thioglucose, and glutathione) can displace either the albumin or the triethylphosphine from the protein-gold complex, AlbSAuPEt3. The albumin is displaced in preference to triethylphosphine, but irreversible oxidation of the latter eventually shifts the equilibria toward Et3PO and AlbSAuSR. Albumin disulfide bonds are the probable oxidants. Neither O2 nor oxidized glutathione substantially enhanced the rate or extent of Et3PO formation. The labilization of the phosphine in AlbSAuPEt3 is attributed to a strong trans effect of the albumin thiolate, Cys-34. The 31P NMR chemical shifts of various thiolato(triethylphosphine)gold(I) complexes are correlated directly with the affinity of the thiols for gold and inversely with their pKSH values. Deacetylated auranofin (1-thio-beta-D-glucopyranosato-S) (triethylphosphine)gold(I) reacts with the mercaptalbumin and oxidized mercaptalbumin (putatively AlbSOH) forms of bovine serum albumin to form AlbSAuPEt3 with displacement of the thioglucose ligand.
硫醇（RSH = 2,3,4,6 - 四 - O - 乙酰基 - β - 1 - D - 硫代葡萄糖、β - 1 - D - 硫代葡萄糖和谷胱甘肽）可从蛋白质 - 金络合物AlbSAuPEt3中取代白蛋白或三乙膦。白蛋白比三乙膦更易被取代，但三乙膦的不可逆氧化最终会使平衡向Et3PO和AlbSAuSR方向移动。白蛋白二硫键可能是氧化剂。O2和氧化型谷胱甘肽均未显著提高Et3PO形成的速率或程度。AlbSAuPEt3中膦的不稳定归因于白蛋白硫醇盐Cys - 34的强反位效应。各种硫醇基（三乙膦）金（I）络合物的31P NMR化学位移与硫醇对金的亲和力直接相关，与它们的pKSH值成反比。脱乙酰金诺芬（1 - 硫代 - β - D - 吡喃葡萄糖基 - S）（三乙膦）金（I）与牛血清白蛋白的巯基白蛋白和氧化型巯基白蛋白（推测为AlbSOH）形式反应，形成AlbSAuPEt3并取代硫代葡萄糖配体。
