浸矿细菌中硫化氢-三价铁氧化还原酶的纯化
来源期刊：中南大学学报(自然科学版)2004年第1期
论文作者：傅建华 邱冠周 胡岳华 柳建设
文章页码：43 - 48
关键词：氧化亚铁硫杆菌;硫化氢-三价铁氧化还原酶;纯化
Key words：Thiobacillus ferrooxidans; hydrogen sulfide-ferric ion oxidoreductase; purification
摘 要：利用Fe3+作为元素硫的电子受体,由铁生长的T.f硫化氢-三价铁氧化还原酶纯化至电泳匀质状态,对主要浸矿细菌氧化亚铁硫杆菌(T.f-dx)中的硫氧化酶关键酶进行分离与纯化。用质谱仪测定硫氧化酶的相对分子质量为46 072.06(精确度为±0.01%);SDS-PAGE(电泳)结果表明硫氧化酶由2个相同的亚基组成。在硫氧化过程中硫氧化酶绝对依赖于还原型谷胱苷肽(GSH),该酶的等电点和最适pH值分别为4.6和6.5。
Abstract: The key enzyme of sulfur oxide from theT.fwas separated and purified. Hydrogen sulfide ferric ion oxidoreductase, which utilizes ferric ion as an electron acceptor of elemental sulfur, was purified from iron-grownThiobacillus ferrooxidans(T. f-dx) to an electrophoretically homogeneous state. The enzyme has a relative molecular mass of 46 072.06(±0.01%), and it is composed of two identical subunits as estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Sulfur oxidation by this enzyme is absolutely dependent on the presence of reduced glutamine. The enzyme has an isoelectric point and optimum pH value at 4.6 and 6.5, respectively.
