Ability of bacterial biphenyl dioxygenases from Burkholderia sp. LB400 and Comamonas testosteroni B-356 to catalyse oxygenation of ortho-hydroxychlorobiphenyls formed from PCBs by plants
Jazyk angličtina Země Velká Británie, Anglie Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
14553993
DOI
10.1016/s0269-7491(03)00257-4
PII: S0269749103002574
Knihovny.cz E-zdroje
- MeSH
- biodegradace MeSH
- Burkholderia enzymologie MeSH
- Comamonas testosteroni enzymologie MeSH
- gramnegativní bakterie enzymologie MeSH
- katalýza MeSH
- látky znečišťující půdu metabolismus MeSH
- oxidace-redukce MeSH
- oxygenasy metabolismus MeSH
- polychlorované bifenyly metabolismus MeSH
- rostliny metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- biphenyl-1,2-dioxygenase MeSH Prohlížeč
- látky znečišťující půdu MeSH
- oxygenasy MeSH
- polychlorované bifenyly MeSH
Capacity of enzymes of the biphenyl/chlorobiphenyl pathway, especially biphenyl dioxygenase (BPDO) of two polychlorinated biphenyls (PCB) degrading bacteria, Burkholderia sp. LB400 and Comamonas testosteroni B-356, to metabolize ortho-substituted hydroxybiphenyls was tested.,These compounds found among plant products of PCB metabolism, are carrying chlorine atoms on the hydroxyl-substituted ring. The abilities of His-tagged purified LB400 and B-356 BPDOs to catalyze the oxygenation of 2-hydroxy-3-chlorobiphenyl, 2-hydroxy-5-chlorobiphenyl and 2-hydroxy-3,5-dichlorobiphenyl were compared. Both enzyme preparations catalyzed the hydroxylation of the three chloro-hydroxybiphenyls on the non-substituted ring. Neither LB400 BPDO nor B-356 BPDO oxygenated the substituted ring of the ortho-hydroxylated biphenyl. The fact that metabolites generated by both enzymes were identical for all three hydroxychlorobiphenyls tested; exclude any other mode of attack of these compounds by LB400 BPDOs than the ortho-meta oxygenation.
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