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Bacterial pyridine hydroxylation is ubiquitous in environment.
Sun, Ji-Quan; Xu, Lian; Tang, Yue-Qin; Chen, Fu-Ming; Zhao, Jing-Jing; Wu, Xiao-Lei.
Afiliação
  • Sun JQ; College of Engineering, Peking University, Beijing, 100871, People's Republic of China.
Appl Microbiol Biotechnol ; 98(1): 455-64, 2014 Jan.
Article em En | MEDLINE | ID: mdl-23519734
Ten phenol-degrading bacterial strains were isolated from three geographically distant environments. Five of them, identified as Diaphorobacter, Acidovorax, Acinetobacter (two strains), and Corynebacterium, could additionally transform pyridine, through the transcription of phenol hydroxylase genes induced both by phenol and pyridine. HPLC-UV and LC-MS analyses indicated that one metabolite (m/e = 96.07) with the same molecular weight as monohydroxylated pyridine was produced from the five phenol-degrading strains, when pyridine was the sole carbon source. Phenol (50 mg l(-1)) could initially inhibit and later stimulate the pyridine transformation. In addition, heterologous expression of the phenol hydroxylase gene (pheKLMNOP) resulted in the detection of monohydroxylated pyridine, which confirmed the phenol hydroxylase could catalyze pyridine hydroxylation. Phylogeny of the phenol hydroxylase genes revealed that the genes from the five pyridine-hydroxylating strains form a clade with each other and with those catalyzing the hydroxylation of phenol, BTEX (acronym of benzene, toluene, ethylbenzene, and xylene), and trichloroethylene. These results suggest that pyridine transformation via hydroxylation by phenol hydroxylase may be prevalent in environments than expected.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Piridinas / Acinetobacter / Corynebacterium / Comamonadaceae / Microbiologia Ambiental / Oxigenases de Função Mista Idioma: En Revista: Appl Microbiol Biotechnol Ano de publicação: 2014 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Piridinas / Acinetobacter / Corynebacterium / Comamonadaceae / Microbiologia Ambiental / Oxigenases de Função Mista Idioma: En Revista: Appl Microbiol Biotechnol Ano de publicação: 2014 Tipo de documento: Article