QUANTITATIVE MODELING OF PROXIMITY EFFECTS ON ORGANIC-REACTIVITY
QUANTITATIVE MODELING OF PROXIMITY EFFECTS ON ORGANIC-REACTIVITY
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DOI：
10.1021/ar00172a003
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发表时间：
1990-04-01
影响因子：
18.3
通讯作者：
DORIGO, AE
中科院分区：
文献类型：
--
作者：
HOUK, KN;TUCKER, JA;DORIGO, AE
了解酶的巨大催化能力是我们这个时代最具挑战性和最令人兴奋的化学问题之一。1948年，Pauling提出酶与其催化的反应的过渡态是互补的，并且酶催化是通过与酶的吸引相互作用稳定过渡态的结果。酶促反应和分子内反应之间的相似性随后被认识到，并被用于开发酶促反应的化学模型。随后，提出了许多基于分子内反应中结构-反应性关系的理论来解释酶催化反应的速率。我们成功地使用力场过渡态模型来合理化有机反应的立体化学，这使我们研究了一种类似的方法来理解和预测分子内反应的相对速率。这个帐户描述了我们的力场模型的发展，提供定量预测的分子内反应速率，并比较这些与分子间的反应性。Bruice对分子内亲核催化的开创性研究使他得出结论，
Understanding the dramatic catalytic power of en-zymes is one of the most challenging and exciting chemical problems of our time. In 1948, Pauling1 proposed that enzymes are complementary to the transition states of the reactions that they catalyze, and that enzymatic catalysis results from stabilization of the transition state by attractive interactions with the en-zyme. The close analogy between enzymatic and in-tramolecular reactions was recognized subsequently and exploited to develop chemical models for enzymatic reactions. Subsequently, a number of theoriesbased on structure-reactivity relationships in intramolecular reactions have been advanced to account for the rates of enzyme-catalyzed reactions. Our successful use of force-field transition-state modeling to rationalize the stereochemistry of organic reactions2 led us to inves-tigate a similar approach for the understanding and prediction of the relative rates of intramolecular reac-tions. This Account describes our development of force-field models to provide quantitative predictions of intramolecular reaction rates and to compare these with intermolecular reactivities. Bruice’s3 pioneering studies of intramolecular nu-cleophilic catalysis led him to conclude that enzymes