Alkane hydroxylation by cytochrome P450: Is kinetic isotope effect a reliable probe of transition state structure?

François Ogliaro; Michael Filatov; Sason Shaik

doi:10.1002/1099-0682(200012)2000:12<2455::AID-EJIC2455>3.0.CO;2-4

Alkane hydroxylation by cytochrome P450: Is kinetic isotope effect a reliable probe of transition state structure?

François Ogliaro
, Michael Filatov
, Sason Shaik^*

^*Corresponding author for this work

Institute of Chemistry

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

45 Scopus citations

Abstract

Computed kinetic isotope effect (KIE) values for methane hydroxylation by Cytochrome P450, in both high- and low-spin states, compare well with KIE's for model hydrogen abstraction reactions, thereby demonstrating the utility of KIE as a mechanistic probe and supporting a two-state-rebound mechanism.

Original language	English
Pages (from-to)	2455-2458
Number of pages	4
Journal	European Journal of Inorganic Chemistry
Issue number	12
DOIs	https://doi.org/10.1002/1099-0682(200012)2000:12<2455::AID-EJIC2455>3.0.CO;2-4
State	Published - Dec 2000

Keywords

Cytochrome P450
Density functional calculations
Hydroxylation
Isotope effects
Metalloenzymes

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10.1002/1099-0682(200012)2000:12<2455::AID-EJIC2455>3.0.CO;2-4

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title = "Alkane hydroxylation by cytochrome P450: Is kinetic isotope effect a reliable probe of transition state structure?",

abstract = "Computed kinetic isotope effect (KIE) values for methane hydroxylation by Cytochrome P450, in both high- and low-spin states, compare well with KIE's for model hydrogen abstraction reactions, thereby demonstrating the utility of KIE as a mechanistic probe and supporting a two-state-rebound mechanism.",

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T2 - Is kinetic isotope effect a reliable probe of transition state structure?

AU - Ogliaro, François

AU - Filatov, Michael

AU - Shaik, Sason

PY - 2000/12

Y1 - 2000/12

N2 - Computed kinetic isotope effect (KIE) values for methane hydroxylation by Cytochrome P450, in both high- and low-spin states, compare well with KIE's for model hydrogen abstraction reactions, thereby demonstrating the utility of KIE as a mechanistic probe and supporting a two-state-rebound mechanism.

AB - Computed kinetic isotope effect (KIE) values for methane hydroxylation by Cytochrome P450, in both high- and low-spin states, compare well with KIE's for model hydrogen abstraction reactions, thereby demonstrating the utility of KIE as a mechanistic probe and supporting a two-state-rebound mechanism.

KW - Cytochrome P450

KW - Density functional calculations

KW - Hydroxylation

KW - Isotope effects

KW - Metalloenzymes

UR - https://www.scopus.com/pages/publications/0033669428

U2 - 10.1002/1099-0682(200012)2000:12<2455::AID-EJIC2455>3.0.CO;2-4

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JO - European Journal of Inorganic Chemistry

JF - European Journal of Inorganic Chemistry

IS - 12

ER -

Alkane hydroxylation by cytochrome P450: Is kinetic isotope effect a reliable probe of transition state structure?

Abstract

Keywords

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