Hydrogen tunneling in peptidylglycine α-hydroxylating monooxygenase

Wilson A. Francisco, Michael J. Knapp, Ninian J. Blackburn, Judith P. Klinman

Research output: Contribution to journalArticle

110 Scopus citations

Abstract

The temperature dependence of the primary and secondary intrinsic isotope effects for the C-H bond cleavage catalyzed by peptidylglycine α-hydroxylating monooxygenase has been determined. Analysis of the magnitude and Arrhenius behavior of the intrinsic isotope effects provides strong evidence for the use of tunneling as a primary catalytic strategy for this enzyme. Modeling of the isotope effect data allows for a comparison to the hydrogen transfer catalyzed by soybean lipoxygenase in terms of environmental reorganization energy and frequency of the protein vibration that controls the hydrogen transfer.

Original languageEnglish (US)
Pages (from-to)8194-8195
Number of pages2
JournalJournal of the American Chemical Society
Volume124
Issue number28
DOIs
StatePublished - Jul 17 2002

ASJC Scopus subject areas

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

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