Preferential oxidative dehalogenation upon conversion of 2-halophenols by Rhodococcus opacus 1G.
The regiospecificity of hydroxylation of C2-halogenated phenols by Rhodococcus opacus 1G was investigated. Oxidative defluorination at the C2 position ortho with respect to the hydroxyl moiety was preferred over hydroxylation at the non-fluorinated C6 position for all 2-fluorophenol compounds studied. Initial hydroxylation of 2,3, 5-trichlorophenol resulted in the exclusive formation of 3, 5-dichlorocatechol. These results indicate that, in contrast to all other phenol ortho-hydroxylases studied so far, phenol hydroxylase from R. opacus 1G is capable of catalyzing preferential oxidative defluorination but also oxidative dechlorination.
Bondar
V S
VS
Department of Biomolecular Sciences, Laboratory of Biochemistry, Wageningen University, Dreijenlaan 3, 6703 HA, Wageningen, The Netherlands.
Boersma
M G
MG
van Berkel
W J
WJ
Finkelstein
Z I
ZI
Golovlev
E L
EL
Baskunov
B P
BP
Vervoort
J
J
Golovleva
L A
LA
Rietjens
I M
IM
D001673:Biodegradation, Environmental; D002733:Chlorophenols / Q000378:metabolism; D002851:Chromatography, High Pressure Liquid; D003600:Cytosol / Q000201:enzymology; D009682:Magnetic Resonance Spectroscopy; D008861:Microsomes / Q000201:enzymology; D006899:Mixed Function Oxygenases / Q000378:metabolism; D010084:Oxidation-Reduction; D010636:Phenols / Q000378:metabolism*; D012240:Rhodococcus / Q000201:enzymology* / Q000254:growth & development
D002733:Chlorophenols; D010636:Phenols; C056693:2,3,5-trichlorophenol; D006899:Mixed Function Oxygenases; C022336:phenol 2-monooxygenase