硫丹是一种有机氯杀虫剂,广泛用于农业病虫害防治。由于其对鱼类和水生无脊椎动物的极端毒性,世界上许多国家都限制或完全禁止了它。节杆菌sp.菌株KW具有降解α的能力,β硫丹及其中间代谢产物硫酸盐;这种降解与Ese蛋白有关,一种双组分黄素依赖性单加氧酶(TC-FDM)。采用硅片工具,我们得到了Ese蛋白的三维模型,我们的结果表明它属于荧光素酶样单加氧酶家族(LLM)。对接研究表明,V59、V315、D316和T335残基与α-硫丹相互作用。这些残基:V59、T60、V315、D316和T335与β-硫丹的相互作用位点有关,和残基:H17,V315,D316,T335,N364和Q363参与与内硫酸盐的相互作用。通过分子中原子的量子理论(QTAIM)和非共价相互作用(NCI)指数对电子密度进行拓扑分析,表明Ese-配体配合物主要是通过分散力形成的,其中Cl原子起主要作用。由于Ese是单加氧酶成员,我们预测了同源二聚体的形成。然而,必须开展酶学研究来研究Ese蛋白的酶和催化活性。
Endosulfan is an organochlorine insecticide widely used for agricultural pest control. Many nations worldwide have restricted or completely banned it due to its extreme toxicity to fish and aquatic invertebrates. Arthrobacter sp. strain KW has the ability to degrade α, β endosulfan and its intermediate metabolite endosulfate; this degradation is associated with
Ese protein, a two-component flavin-dependent monooxygenase (TC-FDM). Employing in silico tools, we obtained the 3D model of
Ese protein, and our results suggest that it belongs to the Luciferase Like Monooxygenase family (LLM). Docking studies showed that the residues V59, V315, D316, and T335 interact with α-endosulfan. The residues: V59, T60, V315, D316, and T335 are implicated in the interacting site with β-endosulfan, and the residues: H17, V315, D316, T335, N364, and Q363 participate in the interaction with endosulfate. Topological analysis of the electron density by means of the Quantum Theory of Atoms in Molecules (QTAIM) and the Non-Covalent Interaction (NCI) index reveals that the
Ese-ligands complexes are formed mainly by dispersive forces, where Cl atoms have a predominant role. As
Ese is a monooxygenase member, we predict the homodimer formation. However, enzymatic studies must be developed to investigate the
Ese protein\'s enzymatic and catalytic activity.