Ullah A J, Murray R I, Bhattacharyya P K, Wagner G C, Gunsalus I C
Department of Biochemistry, University of Illinois, Urbana 61801.
J Biol Chem. 1990 Jan 25;265(3):1345-51.
The cytochrome P-450 heme-thiolate monooxygenases that hydroxylate monoterpene hydrocarbon groups are effective models for the cytochrome P-450 family. We have purified and characterized the three proteins from a P-450-dependent linalool 8-methyl hydroxylase in Pseudomonas putida (incognita) strain PpG777. The proteins resemble the camphor 5-exohydroxylase components in chemical and physical properties; however, they show neither immunological cross-reactivity nor catalytic activity in heterogenous recombination. These two systems provide an excellent model to probe more deeply the heme-thiolate reaction center, molecular domains of substrate specificity, redox-pair interactions, and the regulation of the reaction cycle.
使单萜烃基发生羟基化反应的细胞色素P-450血红素硫醇盐单加氧酶是细胞色素P-450家族的有效模型。我们已从恶臭假单胞菌（未确定种）菌株PpG777中依赖细胞色素P-450的芳樟醇8-甲基羟化酶中纯化并鉴定了这三种蛋白质。这些蛋白质在化学和物理性质上类似于樟脑5-外羟化酶成分；然而，它们在异源重组中既不显示免疫交叉反应性，也不显示催化活性。这两个系统为更深入地探究血红素硫醇盐反应中心、底物特异性的分子结构域、氧化还原对相互作用以及反应循环的调控提供了一个极好的模型。
