Powlowski J, Shingler V
Unit for Applied Cell and Molecular Biology, University of Umeå, Sweden.
J Bacteriol. 1990 Dec;172(12):6834-40. doi: 10.1128/jb.172.12.6834-6840.1990.
An in vitro study of the multicomponent phenol hydroxylase from Pseudomonas sp. strain CF600 was performed. Phenol-stimulated oxygen uptake from crude extracts was strictly dependent on the addition of NAD(P)H and Fe2+ to assay mixtures. Five of six polypeptides required for growth on phenol were necessary for in vitro activity. One of the polypeptides was purified to homogeneity and found to be a flavin adenine dinucleotide containing iron-sulfur protein with significant sequence homology, at the amino terminus, to plant-type ferredoxins. This component, as in other oxygenase systems, probably functions to transfer electrons from NAD(P)H to the iron-requiring oxygenase component. Phenol hydroxylase from this organism is thus markedly different from bacterial flavoprotein monooxygenases commonly used for hydroxylation of other phenolic compounds, but bears a number of similarities to multicomponent oxygenase systems for unactivated compounds.
对来自假单胞菌属CF600菌株的多组分苯酚羟化酶进行了一项体外研究。粗提物中苯酚刺激的氧气摄取严格依赖于向测定混合物中添加NAD(P)H和Fe2+。在苯酚上生长所需的六种多肽中的五种对于体外活性是必需的。其中一种多肽被纯化至同质，发现是一种含有黄素腺嘌呤二核苷酸的铁硫蛋白，在氨基末端与植物型铁氧还蛋白具有显著的序列同源性。与其他加氧酶系统一样，该组分可能起到将电子从NAD(P)H转移到需要铁的加氧酶组分的作用。因此，这种生物体的苯酚羟化酶与通常用于其他酚类化合物羟基化的细菌黄素蛋白单加氧酶明显不同，但与用于未活化化合物的多组分加氧酶系统有许多相似之处。
