Purification and characterization of 2,4-dichlorophenol hydroxylase isolated from a bacterium of the α-2 subgroup of the Proteobacteria

1 December 1997

journal article
Published by Oxford University Press (OUP) in FEMS Microbiology Letters

Vol. 157 (1) , 95-101
https://doi.org/10.1016/s0378-1097(97)00460-6

Abstract

2,4-Dichlorophenol hydroxylase (EC 1.14.13.20) was purified to apparent homogeneity from the bacterial strain S1, a member of the α-2 subgroup of the Proteobacteria . The molecular masses of the native enzyme and the subunit were determined to be 256 and 64 kDa, respectively, suggesting a homotetrameric structure. The enzyme converted 2,4-dichlorophenol to 3,5-dichlorocatechol. The apparent K m values for 2,4-dichlorophenol, NADPH and NADH were 3, 240 and 420 μM, respectively. The enzyme hydroxylated a broad range of halogenated phenols. 3-Chloro-, 2,6-dichloro- and 2,4,6-trichlorophenol acted as `non-substrate' effectors. The N-terminal sequence revealed 72% identity with the amino acid sequence deduced from the pJP4-encoded tfdB gene.

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