Combining solvent isotope effects with substrate isotope effects in mechanistic studies of alcohol and amine oxidation by enzymes

Paul F. Fitzpatrick

Research output: Contribution to journalReview articlepeer-review

20 Scopus citations

Abstract

Oxidation of alcohols and amines is catalyzed by multiple families of flavin- and pyridine nucleotide-dependent enzymes. Measurement of solvent isotope effects provides a unique mechanistic probe of the timing of the cleavage of the OH and NH bonds, necessary information for a complete description of the catalytic mechanism. The inherent ambiguities in interpretation of solvent isotope effects can be significantly decreased if isotope effects arising from isotopically labeled substrates are measured in combination with solvent isotope effects. The application of combined solvent and substrate (mainly deuterium) isotope effects to multiple enzymes is described here to illustrate the range of mechanistic insights that such an approach can provide. This article is part of a Special Issue entitled: Enzyme Transition States from Theory and Experiment.

Original languageEnglish (US)
Pages (from-to)1746-1755
Number of pages10
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Volume1854
Issue number11
DOIs
StatePublished - Nov 1 2015

Keywords

  • Dehydrogenase
  • Enzyme kinetics
  • Flavoprotein
  • Kinetic isotope effect
  • Oxidase
  • Solvent isotope effect

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biophysics
  • Biochemistry
  • Molecular Biology

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