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 language | English (US) |
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Pages (from-to) | 8194-8195 |
Number of pages | 2 |
Journal | Journal of the American Chemical Society |
Volume | 124 |
Issue number | 28 |
DOIs | |
State | Published - Jul 17 2002 |
ASJC Scopus subject areas
- Catalysis
- General Chemistry
- Biochemistry
- Colloid and Surface Chemistry