Characterization of aromatic dehalogenases of Mycobacterium fortuitum CG-2.
Two different dehalogenation enzymes were found in cell extracts of Mycobacterium fortuitum CG-2. The first enzyme was a halophenol para-hydroxylase, a membrane-associated monooxygenase that required molecular oxygen and catalyzed the para-hydroxylation and dehalogenation of chlorinated, fluorinated, and brominated phenols to the corresponding halogenated hydroquinones. The membrane preparation with this activity was inhibited by cytochrome P-450 inhibitors and also showed an increase in the A448 caused by CO. The second enzyme hydroxylated and reductively dehalogenated tetrahalohydroquinones to 1,2,4-trihydroxybenzene. This halohydroquinone-dehalogenating enzyme was soluble, did not require oxygen, and was not inhibited by cytochrome P-450 inhibitors.
Uotila
J S
JS
Department of General Microbiology, University of Helsinki, Finland.
Kitunen
V H
VH
Saastamoinen
T
T
Coote
T
T
Häggblom
M M
MM
Salkinoja-Salonen
M S
MS
D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D008401:Gas Chromatography-Mass Spectrometry; D006846:Hydrocarbons, Halogenated / Q000378:metabolism*; D006873:Hydroquinones / Q000378:metabolism; D013058:Mass Spectrometry; D009161:Mycobacterium / Q000201:enzymology* / Q000648:ultrastructure; D010636:Phenols / Q000378:metabolism; D013053:Spectrophotometry; D013347:Subcellular Fractions / Q000201:enzymology
D006846:Hydrocarbons, Halogenated; D006873:Hydroquinones; D010636:Phenols; D003577:Cytochrome P-450 Enzyme System