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) |
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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