Beyond ferryl-mediated hydroxylation: 40 years of the rebound mechanism and C-H activation.

ABSTRACT: Since our initial report in 1976, the oxygen rebound mechanism has become the consensus mechanistic feature for an expanding variety of enzymatic C-H functionalization reactions and small molecule biomimetic catalysts. For both the biotransformations and models, an initial hydrogen atom abstraction from the substrate (R-H) by high-valent iron-oxo species (Feⁿ=O) generates a substrate radical and a reduced iron hydroxide, [Fe^n-1-OH ·R]. This caged radical pair then evolves on a complicated energy landscape through a number of reaction pathways, such as oxygen rebound to form R-OH, rebound to a non-oxygen atom affording R-X, electron transfer of the incipient radical to yield a carbocation, R⁺, desaturation to form olefins, and radical cage escape. These vari

SUBMITTER: Huang X 

PROVIDER: S-EPMC5350257 | biostudies-literature | 2017 Apr

REPOSITORIES: biostudies-literature