Intramolecular determination of primary kinetic isotope effects in hydroxylations catalyzed by cytochrome P-450

Leonard M Hjelmeland, Lewis Aronow, James R. Trudell

Research output: Contribution to journalArticle

122 Scopus citations

Abstract

Isotope effects for hydroxylation reactions catalyzed by cytochrome P-450 have usually been measured by comparing the overall reaction velocities of deuterated and nondeuterated substrates. Since the rate-limiting step is probably not the single reaction involving covalent bond cleavage, such an approach does not yield information about the primary isotope effect. We measured the primary kinetic isotope effect for benzylic hydroxylation by a method utilizing intramolecular competition, using the symmetrical substrate 1,3-diphenylpropane-1,1-d2. These experiments yield a value of kH kD = 11, a larger effect than has previously been reported for benzylic hydroxylations.

Original languageEnglish (US)
Pages (from-to)541-549
Number of pages9
JournalBiochemical and Biophysical Research Communications
Volume76
Issue number2
DOIs
StatePublished - May 23 1977
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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