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J Biol Chem, Vol. 274, Issue 29, 20287-20292, July 16, 1999
From the ortho-Chlorophenol reductive
dehalogenase of the halorespiring Gram-positive
Desulfitobacterium dehalogenans was purified 90-fold to
apparent homogeneity. The purified dehalogenase catalyzed the reductive
removal of a halogen atom from the ortho position of
3-chloro-4-hydroxyphenylacetate, 2-chlorophenol, 2,3-dichlorophenol, 2,4-dichlorophenol, 2,6-dichlorophenol, pentachlorophenol, and 2-bromo-4-chlorophenol with reduced methyl viologen as electron donor.
The dechlorination of 3-chloro-4-hydroxyphenylacetate was catalyzed by
the enzyme at a Vmax of 28 units/mg protein and
a Km of 20 µM. The pH and temperature
optimum were 8.2 and 52 °C, respectively. EPR analysis indicated one
[4Fe-4S] cluster (midpoint redox potential
(Em) =
Purification and Molecular Characterization of
ortho-Chlorophenol Reductive Dehalogenase, a Key Enzyme of
Halorespiration in Desulfitobacterium dehalogenans
,,
,,,, and
Laboratory of Microbiology, Wageningen
University, Hesselink van Suchtelenweg 4, NL-6703 CT Wageningen, The
Netherlands and the Laboratory of Biochemistry, Wageningen
University, Dreijenlaan 3, NL-6703 HA Wageningen, The Netherlands
440 mV), one [3Fe-4S] cluster
(Em = +70 mV), and one cobalamin per 48-kDa
monomer. The Co(I)/Co(II) transition had an Em of
370 mV. Via a reversed genetic approach based on the N-terminal
sequence, the corresponding gene was isolated from a D. dehalogenans genomic library, cloned, and sequenced. This
revealed the presence of two closely linked genes: (i)
cprA, encoding the o-chlorophenol reductive
dehalogenase, which contains a twin-arginine type signal sequence that
is processed in the purified enzyme; (ii) cprB, coding for
an integral membrane protein that could act as a membrane anchor of the
dehalogenase. This first biochemical and molecular characterization of
a chlorophenol reductive dehalogenase has revealed structural
resemblance with haloalkene reductive dehalogenases.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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