Pietrowski R A, Cartwright N J
Microbios. 1977;19(76):89-102.
The meta O-dealkylase of Pseudomonas fluorescens Tp has been resolved into two protein components, neither of which is a cytochrome. The substrate binding terminal oxidase has been purified and shown to be a non-haem iron protein of approximate molecular weight 118,000, consisting of two seemingly identical subunits, each of molecular weight 55,000. Binding of substrate by the terminal oxidase has been established by difference spectroscopy. The amino acid composition of the protein has also been determined. The NADH-dependent reductase of the system has been partly purified and appears to have a molecular weight of 80,000. The similarity between this and other bacterial O-dealkylases is discussed.
荧光假单胞菌Tp的间位O-脱烷基酶已被分解为两个蛋白质组分，两者均不是细胞色素。底物结合末端氧化酶已被纯化，显示为一种分子量约为118,000的非血红素铁蛋白，由两个看似相同的亚基组成，每个亚基分子量为55,000。通过差示光谱法已确定末端氧化酶与底物的结合。该蛋白质的氨基酸组成也已确定。该系统的NADH依赖性还原酶已部分纯化，其分子量似乎为80,000。文中讨论了此酶与其他细菌O-脱烷基酶之间的相似性。
