A mechanistic investigation of the thiol-disulfide exchange step in the reductive dehalogenation catalyzed by tetrachlorohydroquinone dehalogenase

Authors :: Warner, Joseph R.
Lawson, Sherry L.
Copley, Shelley D.
Source :: Biochemistry. August 2, 2005, Vol. 44 Issue 30, 10360-10368
Publication Year :: 2005
Abstract: The thiol exchange reaction is investigated using rapid flow-quench kinetic studies of the reaction between thiols and ESSG, the form of the enzyme in which glutathione is covalently attached to Cys13. The results suggest that the second glutathione binds very weakly and that its pK(super a) is not significantly perturbed from that observed in solution.

Subjects :: Thiols -- Chemical properties
Thiols -- Research
Halogenation -- Analysis
Glutathione -- Chemical properties
Glutathione -- Research
Biological sciences
Chemistry

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