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Carbon-Halogen Bond Cleavage

Goldman, Peter, Milne, G.W.A., Keister, David B.·1968·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(18)99310-5
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Abstract

Extracts of a pseudomonad isolated from soil have two halidohydrolases, one induced by chloroacetate, the other by dichloroacetate. Both enzymes have been partially purified and each catalyzes a variety of dehalogenations which conform to the general equation l-RCHXCOO- + OH- → d-RCHOHCOO- + X- where X = Cl or I. Like haloacetate halidohydrolase, these enzymes have a pH optimum of 9.0 to 9.4 and utilize the hydroxyl group from water to replace the halogen in the substrate. The inversion of the configuration which occurs during the dehalogenation of optically active substrates gives additional insight into the mechanism of this type of reaction.

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Research works printed but not linked: 21

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Metadata

Authors
Goldman, P., Milne, G. W. A., & Keister, D. B.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1968-01
Volume
243
Issue
2
Pages
428-434
ISSN
0021-9258
DOI
10.1016/s0021-9258(18)99310-5
Cited by
86
References
0
Language
en
Licence

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CoChat. (2026). Citation check: Carbon-Halogen Bond Cleavage. https://app.cochat.ai/papers/10.1016/s0021-9258(18)99310-5
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Goldman, P., Milne, G. W. A., & Keister, D. B. (1968). Carbon-Halogen Bond Cleavage. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)99310-5