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
Language English Country England, Great Britain Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
14553993
DOI
10.1016/s0269-7491(03)00257-4
PII: S0269749103002574
Knihovny.cz E-resources
- MeSH
- Biodegradation, Environmental MeSH
- Burkholderia enzymology MeSH
- Comamonas testosteroni enzymology MeSH
- Gram-Negative Bacteria enzymology MeSH
- Catalysis MeSH
- Soil Pollutants metabolism MeSH
- Oxidation-Reduction MeSH
- Oxygenases metabolism MeSH
- Polychlorinated Biphenyls metabolism MeSH
- Plants metabolism MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- biphenyl-1,2-dioxygenase MeSH Browser
- Soil Pollutants MeSH
- Oxygenases MeSH
- Polychlorinated Biphenyls 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.
References provided by Crossref.org
