Characterization of a cytochrome P450 monooxygenase capable of high molecular weight PAHs oxidization from Rhodococcus sp. P14.
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| Title: | Characterization of a cytochrome P450 monooxygenase capable of high molecular weight PAHs oxidization from Rhodococcus sp. P14. |
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| Authors: | Luo, An1, Wu, Yi-Rui1, Xu, Yan1, Kan, Jie1, Qiao, Jing1, Liang, Lei1, Huang, Tongwang1, Hu, Zhong1 hzh@stu.edu.cn |
| Source: | Process Biochemistry. Dec2016, Vol. 51 Issue 12, p2127-2133. 7p. |
| Subjects: | Cytochrome P-450, Polycyclic aromatic hydrocarbons, Monooxygenases, Rhodococcus, Nucleotide sequencing |
| 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. [ABSTRACT FROM AUTHOR] |
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| Database: | Engineering Source |
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