Abstract
H-transfer was studied in the complex kinetic cascade of dihydrofolate reductase. Intrinsic kinetic isotope effects, their temperature dependence, and other temperature-dependent parameters indicated H-tunneling, but no 1° to 2° coupled motion. The data also suggested environmentally coupled tunneling and commitment to catalysis on pre-steady-state isotope effects.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 4778-4779 |
| Number of pages | 2 |
| Journal | Journal of the American Chemical Society |
| Volume | 126 |
| Issue number | 15 |
| DOIs | |
| State | Published - Apr 21 2004 |
All Science Journal Classification (ASJC) codes
- Catalysis
- General Chemistry
- Biochemistry
- Colloid and Surface Chemistry
Fingerprint
Dive into the research topics of 'Tunneling and Coupled Motion in the Escherichia coli Dihydrofolate Reductase Catalysis'. Together they form a unique fingerprint.Cite this
- APA
- Author
- BIBTEX
- Harvard
- Standard
- RIS
- Vancouver