Hydrogen tunneling in peptidylglycine α-hydroxylating monooxygenase

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

Research output: Contribution to journalArticle

109 Citations (Scopus)

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

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Mixed Function Oxygenases
Isotopes
Hydrogen
Lipoxygenase
Vibration control
Vibration
Soybeans
Enzymes
Proteins
Temperature
peptidylglycine monooxygenase

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Hydrogen tunneling in peptidylglycine α-hydroxylating monooxygenase. / Francisco, Wilson A.; Knapp, Michael J.; Blackburn, Ninian; Klinman, Judith P.

In: Journal of the American Chemical Society, Vol. 124, No. 28, 17.07.2002, p. 8194-8195.

Research output: Contribution to journalArticle

Francisco, Wilson A. ; Knapp, Michael J. ; Blackburn, Ninian ; Klinman, Judith P. / Hydrogen tunneling in peptidylglycine α-hydroxylating monooxygenase. In: Journal of the American Chemical Society. 2002 ; Vol. 124, No. 28. pp. 8194-8195.
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