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Pre-Steady-State Kinetic Studies of the Reductive Dehalogenation Catalyzed by Tetrachlorohydroquinone Dehalogenase†

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University of Colorado at Boulder, Department of Molecular, Cellular, and Developmental Biology and Cooperative Institute for Research in Environmental Sciences, University of Colorado at Boulder, Boulder, Colorado 80309
Cite this: Biochemistry 2007, 46, 45, 13211–13222
Publication Date (Web):October 23, 2007
https://doi.org/10.1021/bi701069n
Copyright © 2007 American Chemical Society
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    Abstract

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    Tetrachlorohydroquinone dehalogenase catalyzes two successive reductive dehalogenation reactions in the pathway for degradation of pentachlorophenol in the soil bacterium Sphingobium chlorophenolicum. We have used pre-steady-state kinetic methods to probe both the mechanism and the rates of elementary steps in the initial stages of the reductive dehalogenation reaction. Binding of trichlorohydroquinone (TriCHQ) to the active site is followed by rapid deprotonation to form TriCHQ-2 and subsequent formation of 3,5,6-trichloro-4-hydroxycyclohexa-2,4-dienone (TriCHQ*). Further conversion of TriCHQ* to 2,6-dichlorohydroquinone (DCHQ) proceeds only in the presence of glutathione. Conversion of TriCHQ to DCHQ during the first turnover is quite rapid, occurring at about 25 s-1 when the enzyme is saturated with TriCHQ and glutathione. The rate of subsequent turnovers is limited by the rate of the thiol−disulfide exchange reaction required to regenerate the free enzyme after turnover, a reaction that is intrinsically less difficult, but is hampered by premature binding of the aromatic substrate to the active site before the catalytic cycle is completed.

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    †

     This work was supported by NSF Grant MCB-0077569.

    *

     To whom correspondence should be addressed. Phone:  (303) 492-6328. Fax:  (303) 492-1149. E-mail:  [email protected].

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    Description of the determination of the KD for GS-Me and TCHQ dehalogenase in the presence of saturating TriCHQ. This material is available free of charge via the Internet at http://pubs.asc.org.

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