Abstract
Two different hydrolysis mechanisms of metabolic product from tirapazamine's enzymatic catalysis have been studied by density functional theory (DFT) at the B3LYP/6-31G(d) and B3LYP/6-311+G(d) levels. The results indicate that the activation barrier of rate-controling step of Brown's model is smaller than that of Denny's model. © World Scientific Publishing Company.
| Original language | English |
|---|---|
| Pages (from-to) | 235-242 |
| Journal | Journal of Theoretical and Computational Chemistry |
| Volume | 5 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Jun 2006 |
Bibliographical note
Publication details (e.g. title, author(s), publication statuses and dates) are captured on an “AS IS” and “AS AVAILABLE” basis at the time of record harvesting from the data source. Suggestions for further amendments or supplementary information can be sent to [email protected].Funding
The authors from China are thankful for the support from the National Natural Science Foundation, China (account number 20277014).
Research Keywords
- Activation barrier
- Hydrolysis mechanism
- Metabolic intermediates
- Reaction channels
- Tirapazamine
- Transition states
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