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J. Biol. Chem., Vol. 276, Issue 44, 40991-40997, November 2, 2001
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From the The United Nations and the U.S. Environmental
Protection Agency have identified a variety of chlorinated aromatics
that constitute a significant health and environmental risk as
"priority organic pollutants," the so-called "dirty dozen."
Microbes have evolved the ability to utilize chlorinated aromatics as
terminal electron acceptors in an energy-generating process called
dehalorespiration. In this process, a reductive dehalogenase (CprA),
couples the oxidation of an electron donor to the reductive elimination
of chloride. We have characterized the B12 and
iron-sulfur cluster-containing 3-chloro-4-hydroxybenzoate reductive
dehalogenase from Desulfitobacterium chlororespirans. By
defining the substrate and inhibitor specificity for the dehalogenase,
the enzyme was found to require an hydroxyl group
ortho to the halide. Inhibition studies indicate that the hydroxyl group is required for substrate binding. The carboxyl group
can be replaced by other functionalities, e.g. acetyl or halide groups, ortho or meta to the chloride to
be eliminated. The purified D. chlororespirans enzyme could
dechlorinate an hydroxylated PCB
(3,3',5,5'-tetrachloro-4,4'-biphenyldiol) at a rate about 1% of that
with 3-chloro-4-hydroxybenzoate. Solvent deuterium isotope effect
studies indicate that transfer of a single proton is partially
rate-limiting in the dehalogenation reaction.
Characterization of the B12- and
Iron-Sulfur-containing Reductive Dehalogenase from
Desulfitobacterium chlororespirans*,
,¶
Department of Biochemistry, Beadle Center,
University of Nebraska, Lincoln, Nebraska 68588-0664 and
§ Skidaway Institute of Oceanography, Savannah, Georgia
31411
*
This work was supported by National Science Foundation Grant
MCB9974836 (to S. W. R).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
The on-line version of this article (available at
http://www.jbc.org) contains Supplemental Figures 1S and 2S.
¶
To whom correspondence should be addressed: Dept. of
Biochemistry, Beadle Center, University of Nebraska, Lincoln, NE
68588-0664. Tel.: 402-472-2943; Fax: 402-472-7842; E-mail:
sragsdale1@unl.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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