Confirmation of oxidative dehalogenation of pentachlorophenol by a Flavobacterium pentachlorophenol hydroxylase.
AUTOR(ES)
Xun, L
RESUMO
Pentachlorophenol (PCP) hydroxylase purified from Flavobacterium sp. strain ATCC 39723 converted PCP or 2,3,5,6-tetrachlorophenol to tetrachloro-p-hydroquinone (TeCH) with the co-consumption of O2 and NADPH. The purified enzyme incorporated 18O from 18O2 but not from H218O into the reaction end product TeCH. The results clearly demonstrate that PCP is oxidatively converted to TeCH by a monooxygenase-type enzyme from Flavobacterium sp. strain ATCC 39723.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=206524Documentos Relacionados
- Diverse substrate range of a Flavobacterium pentachlorophenol hydroxylase and reaction stoichiometries.
- Purification and Properties of Pentachlorophenol Hydroxylase, a Flavoprotein from Flavobacterium sp. Strain ATCC 39723
- Purification and properties of pentachlorophenol hydroxylase, a flavoprotein from Flavobacterium sp. strain ATCC 39723.
- Influence of readily metabolizable carbon on pentachlorophenol metabolism by a pentachlorophenol-degrading Flavobacterium sp.
- Degradation of pentachlorophenol by polyurethane-immobilized Flavobacterium cells.
