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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.
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]
Copyright of Process Biochemistry is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Engineering Source
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DbLabel: Engineering Source
An: 120017062
AccessLevel: 6
PubType: Academic Journal
PubTypeId: academicJournal
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  Label: Title
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  Data: Characterization of a cytochrome P450 monooxygenase capable of high molecular weight PAHs oxidization from Rhodococcus sp. P14.
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  Data: <searchLink fieldCode="AR" term="%22Luo%2C+An%22">Luo, An</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Wu%2C+Yi-Rui%22">Wu, Yi-Rui</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Xu%2C+Yan%22">Xu, Yan</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Kan%2C+Jie%22">Kan, Jie</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Qiao%2C+Jing%22">Qiao, Jing</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Liang%2C+Lei%22">Liang, Lei</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Huang%2C+Tongwang%22">Huang, Tongwang</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Hu%2C+Zhong%22">Hu, Zhong</searchLink><relatesTo>1</relatesTo><i> hzh@stu.edu.cn</i>
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  Data: <searchLink fieldCode="JN" term="%22Process+Biochemistry%22">Process Biochemistry</searchLink>. Dec2016, Vol. 51 Issue 12, p2127-2133. 7p.
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  Data: <searchLink fieldCode="DE" term="%22Cytochrome+P-450%22">Cytochrome P-450</searchLink><br /><searchLink fieldCode="DE" term="%22Polycyclic+aromatic+hydrocarbons%22">Polycyclic aromatic hydrocarbons</searchLink><br /><searchLink fieldCode="DE" term="%22Monooxygenases%22">Monooxygenases</searchLink><br /><searchLink fieldCode="DE" term="%22Rhodococcus%22">Rhodococcus</searchLink><br /><searchLink fieldCode="DE" term="%22Nucleotide+sequencing%22">Nucleotide sequencing</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: 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]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Process Biochemistry is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1016/j.procbio.2016.07.024
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        Text: English
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      – SubjectFull: Cytochrome P-450
        Type: general
      – SubjectFull: Polycyclic aromatic hydrocarbons
        Type: general
      – SubjectFull: Monooxygenases
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      – SubjectFull: Rhodococcus
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      – SubjectFull: Nucleotide sequencing
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      – TitleFull: Characterization of a cytochrome P450 monooxygenase capable of high molecular weight PAHs oxidization from Rhodococcus sp. P14.
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              M: 12
              Text: Dec2016
              Type: published
              Y: 2016
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