Issue Date: October 2, 2017
Radical reaction caught on the rebound
For more than 40 years, chemists and biologists have used the radical rebound mechanism to describe what happens when enzymes with transition metals, such as cytochrome P450, hydroxylate C–H bonds. Such enzymes first remove a hydrogen atom from a C–H bond using a high-valent metal-oxo species. This produces a carbon radical and a metal-OH intermediate that then rebounds—the hydroxyl group moves onto the carbon radical and the metal is reduced by one electron. Although plenty . . .
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