Abstract
Binding isotope effects for l-aspartate reacting with the inactive K258A mutant of PLP-dependent aspartate aminotransferase to give a stable external aldimine intermediate are reported. They provide direct evidence for electronic ground-state destabilization via hyperconjugation. The smaller equilibrium isotope effect with deazaPLP-reconstituted K258A indicates that the pyridine nitrogen plays an important role in labilizing the Cα-H bond.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 8436-8438 |
| Number of pages | 3 |
| Journal | Journal of the American Chemical Society |
| Volume | 134 |
| Issue number | 20 |
| DOIs | |
| State | Published - May 23 2012 |
ASJC Scopus subject areas
- Chemistry(all)
- Catalysis
- Biochemistry
- Colloid and Surface Chemistry
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Griswold, W. R., Castro, J. N., Fisher, A. J., & Toney, M. D. (2012). Ground-state electronic destabilization via hyperconjugation in aspartate aminotransferase. Journal of the American Chemical Society, 134(20), 8436-8438. https://doi.org/10.1021/ja302809e