Solvent isotope effects and the nature of electrophilic catalysis m the action of the lactate dehydrogenase of bacillus stearothermophilus

Minli Xie, Javier Seravalli, W. Phillip Huskey, K. Barbara Schowen, Richard L. Schowen

Research output: Contribution to journalArticle

3 Scopus citations

Abstract

Deuterium oxide at atom fractions of deuterium from 0.0 to 0.97 has an effect of less than 20% on the kinetic term kcat/KmB (believed to reflect the transition state for the hydride-transfer step) for the reduction of pyruvic acid by NADH at 55 °C, with catalysis by the tetrameric form of the lactate dehydrogenase of Bacillus stearothermophilus. This observation suggests that the hydride-transfer event is not assisted by protonic bridging to the carbonyl group being reduced. The results are consistent with protonic bridging only if an opposing isotope effect is present, for example from a generalized conformation or solvation change. The results are consistent with other forms of electrophilic catalysis.

Original languageEnglish (US)
Pages (from-to)691-695
Number of pages5
JournalBioorganic and Medicinal Chemistry
Volume2
Issue number7
DOIs
StatePublished - Jul 1994

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmaceutical Science
  • Drug Discovery
  • Clinical Biochemistry
  • Organic Chemistry

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