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. 1992 Sep;174(17):5669–5675. doi: 10.1128/jb.174.17.5669-5675.1992

Characterization of aromatic dehalogenases of Mycobacterium fortuitum CG-2.

J S Uotila 1, V H Kitunen 1, T Saastamoinen 1, T Coote 1, M M Häggblom 1, M S Salkinoja-Salonen 1
PMCID: PMC206514  PMID: 1512199

Abstract

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.

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Selected References

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