期刊
NATURE CHEMISTRY
卷 3, 期 3, 页码 216-222出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/NCHEM.967
关键词
-
资金
- Pfizer
- Bristol-Myers Squibb
- UIUC
- Illinois Distinguished Fellowship
- Harold R. Snyder Fellowship
- National Science Foundation under the Center for Chemical Innovation in Stereoselective C H Functionalization [CHE 0943980]
- Ullyot Graduate Fellowship
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [0943980] Funding Source: National Science Foundation
Carboxylate-ligated, non-haem iron enzymes demonstrate the capacity for catalysing such remarkable processes as hydroxylations, chlorinations and desaturations of inert, aliphatic C-H bonds. A key to functional diversity is the enzymes' ability to divert fleeting radicals towards different types of functionalization using active site and/or substrate modifications. We report that a non-haem iron hydroxylase catalyst [Fe(PDP)] can also be diverted to catalytic, mixed hydroxylase/desaturase activity with aliphatic C-H bonds. Using a taxane-based radical trap that rearranges under Fe(PDP) oxidation to furnish a nortaxane skeleton, we provide the first direct evidence for a substrate radical using this class of stereoretentive hydroxylation catalysts. Hydroxylation and desaturation proceed by means of a short-lived radical that diverges in a substrate-dependent manner in the presence of carboxylic acids. The novel biomimetic reactivity displayed by this small molecule catalyst is harnessed to diversify natural product derivatives as well as interrogate their biosynthetic pathways.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据