Abstract
The motion of local substrate nuclei is incorporated into the quantum hydrogen transfer reaction which occurs in the active site of soybean lipoxygenase-1, modeled within a quantum trajectory (QT) framework. Interactions within the active site are obtained from on-the-fly electronic structure (ES) calculations at the density-functional tight-binding (DFTB) level. By selectively constraining substrate nuclei, changes in the rate constants and kinetic isotope effect are computed over a 100 K temperature range. Substrate motion, occurring on the time-scale of the hydrogen transfer, enhances both the rate constants and isotope effect, but does not change trends captured in a constrained substrate environment.
| Original language | English |
|---|---|
| Pages (from-to) | 104-109 |
| Number of pages | 6 |
| Journal | Chemical Physics Letters |
| Volume | 613 |
| DOIs | |
| State | Published - Oct 3 2014 |
| Externally published | Yes |
Funding
This material is based upon work partially supported by the National Science Foundation under Grants No. CHE-1056188 and CHE-1048629 , as well as EPSCoR GEAR:CI (J.M. and S.G.). Additional support was provided by the National Science Foundation Grant No. APRA-NSF-EPS-0919436 (J.J.). The XSEDE allocation TG-DMR110037 for time on Kraken at the National Institute for Computational Sciences is also acknowledged.