Biodegradation of Dibenzofuran by Janibacter terrae Strain XJ-1

Jin, Shiwei; Zhu, Tao; Xu, Xudong; Xu, Ying

doi:10.1007/s00284-005-0180-1

Cited by 29 publications

(12 citation statements)

References 35 publications

(32 reference statements)

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“…Janibacter marinus had no other report except its 16S partial sequence record in GenBank. According to previous study, the genus Janibacter has the ability of degrading fluorene, diphenyl ether, carbazole, dibenzo-p-dioxin [47], anthracene, phenanthrene [48], mono-chlorinated dibenzo-p-dioxins [49], dibenzofuran [48,50], and polychlorinated biphenyls (Aroclor 1242) [51]. The aim of the present work was to isolate and characterize a PAHdegrading bacterium, J. anophelis strain JY11 from contaminated environmental samples, and to evaluate its PAHs-degradation potential.…”

mentioning

confidence: 99%

Isolation and characterization of a newly isolated polycyclic aromatic hydrocarbons-degrading Janibacter anophelis strain JY11

Zhang

Ling

Sun

et al. 2009

Journal of Hazardous Materials

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confidence: 99%

Isolation and characterization of a newly isolated polycyclic aromatic hydrocarbons-degrading Janibacter anophelis strain JY11

Zhang

Ling

Sun

et al. 2009

Journal of Hazardous Materials

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“…Primary sequence analysis of these dioxygenases shows that amino acid residues responsible for active-site metal binding are strongly conserved, which is further supported by structural studies on a subset of these enzymes. One of the common peptide folds of dioxygenases is called a bicupin structure, which is characterized by two homologous b-barrel (cupin) domains in each subunit (Jin et al 2006). A functional cupin domain is characterized by two highly conservative sequence motifs of G(X) 5 HXH(X) 3,4 E(X) 6 G and G(X) 5 PXG(X) 2 H(X) 3 N (Dunwell et al 2001).…”

mentioning

confidence: 99%

Crystal structure and mutagenic analysis of GDOsp, a gentisate 1,2‐dioxygenase from Silicibacter Pomeroyi

Chen

Wang

et al. 2008

Protein Science

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Dioxygenases catalyze dioxygen incorporation into various organic compounds and play a key role in the complex degradation pathway of mono-and polycyclic aromatic and hetero-aromatic compounds. Here we report the crystal structure of gentisate 1,2-dioxygenase from Silicibacter pomeroyi (GDOsp) at a 2.8 Å resolution. The enzyme possessed a conserved three-dimensional structure of the bicupin family, forming a homotetramerization. However, each subunit of GDOsp unusually contained two ferrous centers that were located in its two homologous cupin domains, respectively. Further mutagenic analysis indicated that the enzyme activity of GDOsp depends on the microenvironment in both metal-binding sites. Moreover, homologous structural comparison and functional study on GDOsp variants unveiled a group of functionally essential residues and suggested that the active site of the enzyme is located in the amino-terminal domain, but could be influenced by changes in the carboxyl domain. Therefore, GDOsp may provide a working model for studying long-distance communication within a protein (or its complex).

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“…Jin et al . () has reported that the location of ‘DF‐degrading genes’ dispersed not only in chromosomal but also extrachromosomal DNA, like bacterial plasmid. It could be a good approach to explain the DF‐degrading activity of strain PH‐08 in both angular and lateral dioxygenation.…”

Section: Resultsmentioning

confidence: 99%

Degradation of dibenzofuran via multiple dioxygenation by a newly isolated Agrobacterium sp. PH-08

Murugesan

Nam

et al. 2013

J Appl Microbiol

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Aims: To demonstrate the biodegradation of dibenzofuran (DF) and its structural analogs by a newly isolated Agrobacterium sp. PH-08. Methods and Results: To assess the biodegradation potential of newly isolated Agrobacterium sp. PH-08, various substrates were evaluated as sole carbon sources in growth and biotransformation experiments. ESI LC-MS/MS analysis revealed the presence of angular degrading by-products as well as lateral dioxygenation metabolites in the upper pathway. The metabolites in the lower pathway also were detected. In addition, the cometabolically degraded daughter compounds of DF-related compounds such as BP and dibenzothiophene (DBT) in dual substrate degradation were observed. Strain PH-08 exhibited the evidence of meta-cleavage pathway as confirmed by the activity and gene expression of catechol-2,3-dioxygenase. Conclusions: Newly isolated bacterial strain, Agrobacterium sp. PH-08, grew well with and degraded DF via both angular and lateral dioxygenation as demonstrated by metabolites identified through ESI LC-MS/MS and GC-MS analyses. The other heterocyclic pollutants were also cometabolically degraded. Significance and Impact of the Study: Few reports have described the complete degradation of DF by a cometabolic lateral pathway. Our study demonstrates the novel results that the newly isolated strain utilized the DF as a sole carbon source and mineralized it via multiple dioxygenation.

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Biodegradation of Dibenzofuran by Janibacter terrae Strain XJ-1

Cited by 29 publications

References 35 publications

Isolation and characterization of a newly isolated polycyclic aromatic hydrocarbons-degrading Janibacter anophelis strain JY11

Isolation and characterization of a newly isolated polycyclic aromatic hydrocarbons-degrading Janibacter anophelis strain JY11

Crystal structure and mutagenic analysis of GDOsp, a gentisate 1,2‐dioxygenase from Silicibacter Pomeroyi

Degradation of dibenzofuran via multiple dioxygenation by a newly isolated Agrobacterium sp. PH-08

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