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Applied and Environmental Microbiology, December 1998, p. 4637-4642, Vol. 64, No. 12
INRS-Santé, Université du
Québec, Pointe-Claire, Québec, Canada H9R
1G6,1 and
Départment de Biochimie,
Université Laval, Ste-Foy, Québec, Canada G1K
7P42
Received 17 July 1998/Accepted 18 September 1998
The ability of the dehydrogenase and ring cleavage dioxygenase of
the naphthalene degradation pathway to transform 3,4-dihydroxylated biphenyl metabolites was investigated.
1,2-Dihydro-1,2-dihydroxynaphthalene dehydrogenase was expressed as a
histidine-tagged protein. The purified enzyme transformed
2,3-dihydro-2,3-dihydroxybiphenyl, 3,4-dihydro-3,4-dihydroxybiphenyl,
and 3,4-dihydro-3,4-dihydroxy-2,2',5,5'-tetrachlorobiphenyl to
2,3-dihydroxybiphenyl, 3,4-dihydroxybiphenyl (3,4-DHB), and 3,4-dihydroxy-2,2',5,5'-tetrachlorobiphenyl (3,4-DH-2,2',5,5'-TCB), respectively. Our data also suggested that purified
1,2-dihydroxynaphthalene dioxygenase catalyzed the meta
cleavage of 3,4-DHB in both the 2,3 and 4,5 positions. This enzyme
cleaved 3,4-DH-2,2',5,5'-TCB and 3,4-DHB at similar rates. These
results demonstrate the utility of the naphthalene catabolic enzymes in
expanding the ability of the bph pathway to degrade
polychlorinated biphenyls.
0099-2240/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Degradation of Polychlorinated Biphenyl Metabolites
by Naphthalene-Catabolizing Enzymes
*
Corresponding author. Mailing address:
INRS-Santé, 245 Boul. Hymus, Pointe-Claire, Québec, Canada
H9R 1G6. Phone: (514) 630-8829. Fax: (514) 630-8850. E-mail:
Michel.Sylvestre{at}inrs-sante.uquebec.ca.
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