Intermediate partitioning kinetic isotope effects for the NIH shift of 4-hydroxyphenylpyruvate dioxygenase and the hydroxylation reaction of hydroxymandelate synthase reveal mechanistic complexity

Dhara D. Shah; John A. Conrad; Graham R. Moran

doi:10.1021/bi400534q

Intermediate partitioning kinetic isotope effects for the NIH shift of 4-hydroxyphenylpyruvate dioxygenase and the hydroxylation reaction of hydroxymandelate synthase reveal mechanistic complexity

Dhara D. Shah, John A. Conrad, Graham R. Moran

Research output: Contribution to journal › Article › peer-review

Original language	English
Pages (from-to)	6097-6107
Number of pages	11
Journal	Physics Faculty Research and Publications
Volume	52
Issue number	35
DOIs	https://doi.org/10.1021/bi400534q
State	Published - Sep 2 2013
Externally published	Yes

ASJC Scopus Subject Areas

Biochemistry

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10.1021/bi400534q

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Intermediate partitioning kinetic isotope effects for the NIH shift of 4-hydroxyphenylpyruvate dioxygenase and the hydroxylation reaction of hydroxymandelate synthase reveal mechanistic complexity. / Shah, Dhara D.; Conrad, John A.; Moran, Graham R.
In: Physics Faculty Research and Publications, Vol. 52, No. 35, 02.09.2013, p. 6097-6107.

Research output: Contribution to journal › Article › peer-review

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Intermediate partitioning kinetic isotope effects for the NIH shift of 4-hydroxyphenylpyruvate dioxygenase and the hydroxylation reaction of hydroxymandelate synthase reveal mechanistic complexity

ASJC Scopus Subject Areas

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