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Issue 32, 2017
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Catalysis by solvation rather than the desolvation effect: exploring the catalytic efficiency of SAM-dependent chlorinase

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Abstract

Chlorinase SalL halogenate S-adenosyl-L-methionine (SAM) reacts with chloride to generate 5′-chloro-5′-deoxyadenosine and L-methionine through a nucleophilic substitution mechanism. Although it is known that chlorinase enhances the rate of reaction by a factor of 1.2 × 1017 fold, it is not entirely clear how this is accomplished. The search for the origin of the catalysis of chlorinase and other enzymes has led to a desolvation hypothesis. In the present work, we have used well defined computational simulations in order to evaluate the origin of the catalytic efficiency of chlorinase. The results demonstrate that the catalytic effect of chlorinase is associated with the fact that Cl is “solvated” by the protein more than by the reference solution reaction, which is not in accordance with proposed catalysis by desolvation. It is found that chlorinase SalL active sites provide electrostatic stabilization of the transition state which is the origin of its catalytic effect.

Graphical abstract: Catalysis by solvation rather than the desolvation effect: exploring the catalytic efficiency of SAM-dependent chlorinase

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Publication details

The article was received on 30 Apr 2017, accepted on 14 Jul 2017 and first published on 17 Jul 2017


Article type: Paper
DOI: 10.1039/C7CP02811C
Citation: Phys. Chem. Chem. Phys., 2017,19, 21350-21356
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    Catalysis by solvation rather than the desolvation effect: exploring the catalytic efficiency of SAM-dependent chlorinase

    E. Araújo, A. H. Lima and J. Lameira, Phys. Chem. Chem. Phys., 2017, 19, 21350
    DOI: 10.1039/C7CP02811C

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