Characterization of a cytochrome P450 monooxygenase capable of high molecular weight PAHs oxidization from Rhodococcus sp. P14. Issue 12 (December 2016)

• Record Type: Journal Article
• Authors: Luo, An; Wu, Yi-Rui; Xu, Yan; Kan, Jie; Qiao, Jing; Liang, Lei; Huang, Tongwang; Hu, Zhong
• Is Part Of: Process biochemistry. Volume 51:Issue 12(2016:Dec.)
• Page Start: 2127
• Page End: 2133
• Publication Date: 2016-12
• Subjects: Rhodococcus -- Cytochrome P450 monooxygenase -- PAHs -- CYP108J; Biochemical engineering -- Periodicals; Biotechnology -- Periodicals; Biochemistry -- periodicals; Biotechnology -- periodicals; Chemical Engineering -- periodicals; Génie biochimique -- Périodiques; Biotechnologie -- Périodiques; Biochemical engineering; Biotechnology; Periodicals; 660.63
• DOI: 10.1016/j.procbio.2016.07.024
• Languages: English
• ISSNs: 1359-5113

Abstract

Graphical abstract: Highlights: PAHs can induce the transcription of gene cyp108j1 . CYP108J1 initialize PAHs oxidization only with its own electron transport system. Metabolites were detected by using CYP108J1 on the treatment of different PAHs. Abstract: 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 DSM12444 in CYP108 family, respectively. The transcriptional level of gene cyp108j1 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.