Identification and characterization of catabolic para-nitrophenol 4-monooxygenase and para-benzoquinone reductase from pseudomonas sp strain wbc-3 | |
Zhang, Jun-Jie; Liu, Hong; Xiao, Yi; Zhang, Xian-En; Zhou, Ning-Yi | |
刊名 | Journal of bacteriology |
2009-04-15 | |
卷号 | 191期号:8页码:2703-2710 |
ISSN号 | 0021-9193 |
DOI | 10.1128/jb.01566-08 |
通讯作者 | Zhou, ning-yi(n.zhou@pentium.whiov.ac.cn) |
英文摘要 | Pseudomonas sp. strain wbc-3 utilizes para-nitrophenol (pnp) as a sole source of carbon, nitrogen, and energy. in order to identify the genes involved in this utilization, we cloned and sequenced a 12.7-kb fragment containing a conserved region of nad(p) h: quinone oxidoreductase genes. of the products of the 13 open reading frames deduced from this fragment, pnpa shares 24% identity to the large component of a 3-hydroxy-phenylacetate hydroxylase from pseudomonas putida u and pnpb is 58% identical to an nad(p) h: quinone oxidoreductase from escherichia coli. both pnpa and pnpb were purified to homogeneity as his-tagged proteins, and they were considered to be a monomer and a dimer, respectively, as determined by gel filtration. pnpa is a flavin adenine dinucleotide-dependent single-component pnp 4-monooxygenase that converts pnp to para-benzoquinone in the presence of nadph. pnpb is a flavin mononucleotide-and nadph-dependent p-benzoquinone reductase that catalyzes the reduction of p-benzoquinone to hydroquinone. pnpb could enhance pnpa activity, and genetic analyses indicated that both pnpa and pnpb play essential roles in pnp mineralization in strain wbc-3. furthermore, the pnpcdef gene cluster next to pnpab shares significant similarities with and has the same organization as a gene cluster responsible for hydroquinone degradation (hapcdef) in pseudomonas fluorescens acb (m.j. moonen, n.m. kamerbeek, a.h. westphal, s.a. boeren, d.b. janssen, m.w. fraaije, and w.j. van berkel, j. bacteriol. 190: 5190-5198, 2008), suggesting that the genes involved in pnp degradation are physically linked. |
WOS关键词 | P-NITROPHENOL ; ESCHERICHIA-COLI ; GENE-CLUSTER ; MONOOXYGENASE CATALYZES ; SEQUENCE ALIGNMENT ; METHYL PARATHION ; FLUORESCENS ACB ; ARTHROBACTER SP ; HYDROXYLASE ; BIODEGRADATION |
WOS研究方向 | Microbiology |
WOS类目 | Microbiology |
语种 | 英语 |
出版者 | AMER SOC MICROBIOLOGY |
WOS记录号 | WOS:000264752600029 |
内容类型 | 期刊论文 |
URI标识 | http://www.corc.org.cn/handle/1471x/2375581 |
专题 | 武汉病毒研究所 |
通讯作者 | Zhou, Ning-Yi |
作者单位 | Chinese Acad Sci, Wuhan Inst Virol, State Key Lab Virol, Wuhan 430071, Peoples R China |
推荐引用方式 GB/T 7714 | Zhang, Jun-Jie,Liu, Hong,Xiao, Yi,et al. Identification and characterization of catabolic para-nitrophenol 4-monooxygenase and para-benzoquinone reductase from pseudomonas sp strain wbc-3[J]. Journal of bacteriology,2009,191(8):2703-2710. |
APA | Zhang, Jun-Jie,Liu, Hong,Xiao, Yi,Zhang, Xian-En,&Zhou, Ning-Yi.(2009).Identification and characterization of catabolic para-nitrophenol 4-monooxygenase and para-benzoquinone reductase from pseudomonas sp strain wbc-3.Journal of bacteriology,191(8),2703-2710. |
MLA | Zhang, Jun-Jie,et al."Identification and characterization of catabolic para-nitrophenol 4-monooxygenase and para-benzoquinone reductase from pseudomonas sp strain wbc-3".Journal of bacteriology 191.8(2009):2703-2710. |
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