1082553-06-7Relevant articles and documents
cis-Dihydroxylation of alkenes by a non-heme iron enzyme mimic
Barry, Sarah M.,Rutledge, Peter J.
, p. 2172 - 2174 (2008)
Using the non-heme iron oxidase active site as a template, a peptidomimetic ligand has been designed, synthesized, and used to effect the dihydroxylation of alkene substrates. Fenton-type radical pathways are also observed. Georg Thieme Verlag Stuttgart.
Investigating the oxidation of alkenes by non-heme iron enzyme mimics
Barry, Sarah M.,Mueller-Bunz, Helge,Rutledge, Peter J.
, p. 7372 - 7381 (2012/10/08)
Iron is emerging as a key player in the search for efficient and environmentally benign methods for the functionalisation of C-H bonds. Non-heme iron enzymes catalyse a diverse array of oxidative chemistry in nature, and small-molecule complexes designed to mimic the non-heme iron active site have great potential as C-H activation catalysts. Herein we report the synthesis of a series of organic ligands that incorporate key features of the non-heme iron active site. Iron(ii) complexes of these ligands have been generated in situ and their ability to promote hydrocarbon oxidation has been investigated. Several of these systems promote the biomimetic dihydroxylation of cyclohexene at low levels, when hydrogen peroxide is used as the oxidant; allylic oxidation products are also observed. An investigation of ligand stability reveals formation of several breakdown products under the conditions of the oxidative turnover reactions. These products arise via oxidative decarboxylation, dehydration and deamination reactions. Taken together these results indicate that competing mechanisms are at play with these systems: biomimetic hydroxylation involving high-valent iron species, and allylic oxidation via Fenton chemistry and Haber-Weiss radical pathways.
