Ground-state electronic destabilization via hyperconjugation in aspartate aminotransferase

Wait R. Griswold, Joan Nieto Castro, Andrew J Fisher, Michael D. Toney

Research output: Contribution to journalArticle

14 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)8436-8438
Number of pages3
JournalJournal of the American Chemical Society
Volume134
Issue number20
DOIs
StatePublished - May 23 2012

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Aspartate Aminotransferases
Isotopes
Ground state
Aspartic Acid
Pyridine
Nitrogen
pyridine
1-deazapyridoxal 5'-phosphate

ASJC Scopus subject areas

  • Chemistry(all)
  • Catalysis
  • Biochemistry
  • Colloid and Surface Chemistry

Cite this

Ground-state electronic destabilization via hyperconjugation in aspartate aminotransferase. / Griswold, Wait R.; Castro, Joan Nieto; Fisher, Andrew J; Toney, Michael D.

In: Journal of the American Chemical Society, Vol. 134, No. 20, 23.05.2012, p. 8436-8438.

Research output: Contribution to journalArticle

Griswold, Wait R. ; Castro, Joan Nieto ; Fisher, Andrew J ; Toney, Michael D. / Ground-state electronic destabilization via hyperconjugation in aspartate aminotransferase. In: Journal of the American Chemical Society. 2012 ; Vol. 134, No. 20. pp. 8436-8438.
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