Skjeldal L, Dahl K H, McKinley-McKee J S
Biosci Rep. 1982 Jul;2(7):509-14. doi: 10.1007/BF01115249.
Each subunit of the liver alcohol dehydrogenase dimer contains one catalytic and one structural Zn(II) atom. Enzyme with the catalytic metal atoms selectively removed is inactive but can be partly reactivated in the presence of Ag(I) ions. Reactivation results from Ag(I) ions entering the empty metal-binding site in the catalytic center. The specific activity of this silver enzyme reached 24% of the native enzyme. Atomic absorption analysis gave equal amounts of Ag(I) and Zn(II), corresponding to one mole of each metal per monomer. Metal-directed affinity labelling using bromo-imidazolyl propionate showed that the properties of the silver-reactivated enzyme were distinct from those of the native enzyme.
肝脏乙醇脱氢酶二聚体的每个亚基都含有一个催化性锌（II）原子和一个结构性锌（II）原子。催化性金属原子被选择性去除的酶没有活性，但在银（I）离子存在的情况下可以部分重新激活。重新激活是由于银（I）离子进入催化中心的空金属结合位点。这种银酶的比活性达到了天然酶的24%。原子吸收分析表明银（I）和锌（II）的量相等，相当于每个单体一摩尔的每种金属。使用溴代咪唑基丙酸进行的金属导向亲和标记表明，银重新激活的酶的性质与天然酶不同。
