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Trimethylphosphate and Dimethylphosphate Hydrolysis by Binuclear Cd II , Mn II , and Zn II –Fe II Promiscuous Organophosphate‐Degrading Enzyme: Reaction Mechanisms
Author(s) -
Pinto Gaspar,
Mazzone Gloria,
Russo Nino,
Toscano Marirosa
Publication year - 2017
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201702379
Subject(s) - phosphodiester bond , chemistry , organophosphate , enzyme , hydrolysis , metal , manganese , stereochemistry , inorganic chemistry , organic chemistry , biochemistry , rna , pesticide , biology , agronomy , gene
Organophosphate‐degrading enzyme from Agrobacterium radiobacter P230 exhibits promiscuity, not only in the reactions it catalyzes, but also in the metals it uses to catalyze those reactions. Here, three different binuclear metal centers were studied: di‐Cd II , di‐Mn II and Zn II –Fe II . This enzyme uses these metal centers for hydrolyzing trimethyl‐ and dimethyl‐phosphates. Both mechanisms were studied at DFT level of theory using a cluster model approach. The ground spin state was determined for each enzyme. The outcomes confirmed that the hydrolysis of phosphotriester is faster than that of phosphodiester and in some case the phosphodiesterase reaction does not occur. The computed activation energies are in agreement with previous experimental results for phosphotriesterase enzymes.