Two-state reactivity mechanisms of hydroxylation and epoxidation by cytochrome P-450 revealed by theory

被引：296

作者：

Shaik, S ^{[1
]}

de Visser, SP

Ogliaro, F

Schwarz, H

Schröder, D

机构：

[1] Hebrew Univ Jerusalem, Dept Organ Chem, IL-91904 Jerusalem, Israel

[2] Hebrew Univ Jerusalem, Lise Meitner Minerva Ctr Computat Quantum Chem, IL-91904 Jerusalem, Israel

[3] Tech Univ Berlin, Inst Chem, D-10623 Berlin, Germany

来源：

CURRENT OPINION IN CHEMICAL BIOLOGY | 2002年 / 6卷 / 05期

基金：

以色列科学基金会;

关键词：

D O I：

10.1016/S1367-5931(02)00363-0

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Recent Computational studies of alkane hydroxylation and alkene epoxidation by a model active species of the enzyme cytochrome P-450 reveal a two-state reactivity (TSR) scenario in which the information content of the product distribution is determined jointly by two states. TSR is used to reconcile the dilemma of the consensus 'rebound mechanism' of alkane hydroxylation, which emerged from experimental studies of ultra-fast radical clocks. The dilemma, stated succinctly as 'radicals are both present and absent and the rebound mechanism is both right and wrong, is simply understood once one is cognizant that the mechanism operates by two states, one low-spin (LS) the other high-spin (HS). In both states, bond activation proceeds in a manner akin to the rebound mechanism, but the LS mechanism is effectively concerted, whereas the HS is stepwise with incursion of radical intermediates.

引用

页码：556 / 567

页数：12

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