Hydrogen Bonding Modulates the Selectivity of Enzymatic Oxidation by P450: Chameleon Oxidant Behavior by Compound I The research was supported in parts by the Israel Science Foundation (ISF), the German Israeli Binational Foundation (GIF), and by the Ministry of Science, Culture, and Sports. F.O. thanks the European community for a Marie Curie Fellowship.

作者：Sam P. de Visser, François Ogliaro, Pankaz Kumar Sharma, Sason S. Shaik · 发表于：Angewandte Chemie International Edition · 年份：2002 · DOI：10.1002/1521-3773(20020603)41:11<1947::aid-anie1947>3.0.co;2-w · 被引用次数：144 · 研究领域：Metal-Catalyzed Oxygenation Mechanisms、Pharmacogenetics and Drug Metabolism、Computational Drug Discovery Methods

Changes of two orders of magnitude or more in the epoxidation to hydroxylation ratio of propene by the iron-oxo species 1, the primary active species of cytochrome P450 (see scheme) occur when the molecular species is subject to NH⋅⋅⋅S hydrogen bonding and electronic polarization as in the protein pocket.