Abstract:
:The 4-chlorobenzoyl-CoA dehalogenase catalyzes the hydrolytic dechlorination of 4-chlorobenzoyl-CoA via a two-step mechanism, namely nucleophilic aromatic substitution and ester hydrolysis. The mutation of an active-site Histidine residue has been shown to reduce the catalytic activity in both the substitution and subsequent hydrolysis steps. In this communication, we report a quantum mechanical/molecular mechanical simulation of the potential of mean force for the substitution step, which confirms the increased barrier height in the H90Q mutant and provides evidence on the electrostatic influence of two active-site waters on the rate-limiting barrier.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Xu D,Guo Hdoi
10.1016/j.febslet.2005.06.056keywords:
subject
Has Abstractpub_date
2005-08-15 00:00:00pages
4249-53issue
20eissn
0014-5793issn
1873-3468pii
S0014-5793(05)00801-Xjournal_volume
579pub_type
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