- 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
Artykuł