Characterization of a cytochrome P450 monooxygenase capable of high molecular weight PAHs oxidization from Rhodococcus sp P14
Characterization of a cytochrome P450 monooxygenase capable of high molecular weight PAHs oxidization from Rhodococcus sp P14
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能够氧化红球菌 P14 高分子量 PAH 的细胞色素 P450 单加氧酶的表征
DOI：
10.1016/j.procbio.2016.07.024
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发表时间：
2016-12-01
影响因子：
4.4
通讯作者：
Hu, Zhong
中科院分区：
文献类型：
--
作者：
Luo, An;Wu, Yi-Rui;Hu, Zhong
红球菌P14能够降解多种多环芳烃（PAHs）。通过分析其全基因组序列，预测了一个编码细胞色素P450单加氧酶（CYP 108 J1）、铁氧还蛋白（fdx）和铁氧还蛋白还原酶（hcaD）的基因簇，该基因簇与多环芳烃降解有关。CYP 108 J1与假单胞菌属（Pseudomonassp.）嗜芳香菌DSM 12/114。在以苯并[a]蒽、芘、菲和蒽为唯一碳源的培养基中，up 108 j1基因的转录水平均得到上调，分别是葡萄糖培养基的2.4、8.0、16.0和11.3倍。进一步研究了重组蛋白CYP 108 J1在大肠杆菌中的表达。大肠杆菌的研究表明，CYP 108 J1对联苯、菲、蒽和苯并[a]蒽等一系列多环芳烃化合物（从低分子量到高分子量）具有降解能力。(C)2016爱思唯尔有限公司版权所有。
Rhodococcus sp. P14 is able to degrade a wide range of polycyclic aromatic hydrocarbons (PAHs). By analyzing its whole genome sequence, a gene cluster encoding cytochrome P450 monooxygenase (CYP108J1) with ferredoxin (fdx) and ferredoxin reductase (hcaD) relating to polycyclic aromatic hydrocarbons degradation was predicted. Protein sequence analysis of CYP108J1 showed 47.9% and 36.4% identity to the CYP108A1 and CYP108D1 from Pseudomonas sp. and N. aromaticivorans DSM12/114 in CYP108 family, respectively. The transcriptional level of gene up108j1 was up-regulated when the strain was grown within the medium containing benz[a]anthracene, pyrene, phenanthrene and anthracene as the sole carbon source, and the increment was detected to be 2.4, 8.0, 16.0 and 11.3-fold, respectively, by comparing to that grown with glucose. Further investigation on the recombinant protein CYP108J1 in E. coli also indicates that CYP108J1 was capable of degrading a series of PAHs compounds (from low to high molecular weight), including biphenyl, phenanthrene, anthracene and benz[a]anthracene. (C) 2016 Elsevier Ltd. All rights reserved.