Autor: Anderson, V. - Katalog OPAC zbiorów

Skocz do pozycji: 1.

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Skocz do pozycji: 2.

Tytuł:: DFT/PM3 study of the enoyl-CoA hydratase catalyzed reaction
Autorzy:: Pawlak, J.
Bahnson, B.
Anderson, V.
Powiązania:: https://bibliotekanauki.pl/articles/146962.pdf
Data publikacji:: 2002
Wydawca:: Instytut Chemii i Techniki Jądrowej
Tematy:: coenzyme-A
density functional theory
enoyl-CoA hydratase
kinetic isotope effect
ONIOM model
stepwise mechanism
thiolester enolate
Opis:: The enoyl-CoA hydratase catalyzed hydration of alfa,beta-unsaturated thiolesters has been modeled by using the crystal structure of 4-(N,N-dimethylamino)cinnamoyl-CoA bound at the active site. The quantum chemical calculation used the ONIOM mixed level procedure to permit the substrate thiolester and water molecule to be modeled using B3LYP/6-31G(d) level of theory and the active site residues modeled at a semiempirical level using the PM3 Hamiltonian. The results permitted the identification of a stable thiolester enolate intermediate, supporting a stepwise reaction mechanism. The calculation also suggests that the same proton removed from the nucleophilic water molecule is transferred to C alfa in the subsequent protonation of the enolate intermediate. This observation reconciles the stepwise mechanism with the previously reported double isotope effect study [3].
Źródło:: Nukleonika; 2002, 47,suppl.1; 33-36
0029-5922
1508-5791
Pojawia się w:: Nukleonika
Dostawca treści:: Biblioteka Nauki

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