50502-46-0Relevant articles and documents
Tailoring chemoenzymatic oxidation: Via in situ peracids
Re, Rebecca N.,Proessdorf, Johanna C.,La Clair, James J.,Subileau, Maeva,Burkart, Michael D.
supporting information, p. 9418 - 9424 (2019/11/14)
Epoxidation chemistry often suffers from the challenging handling of peracids and thus requires in situ preparation. Here, we describe a two-phase enzymatic system that allows the effective generation of peracids and directly translate their activity to the epoxidation of olefins. We demonstrate the approach by application to lipid and olefin epoxidation as well as sulfide oxidation. These methods offer useful applications to synthetic modifications and scalable green processes.
An investigation into oxo analogues of molybdenum olefin metathesis complexes as epoxidation catalysts for alkenes
Anderson, James C.,Smith, Neil M.,Robertson, Michelle,Scott, Mark S.
experimental part, p. 5344 - 5346 (2009/12/06)
The oxo-imido molybdenum complex 2a is an effective catalyst at low catalyst loadings (0.5 mol % or below) for the epoxidation of a range of alkenes with tBuOOH in PhMe at 90 °C. Reactions are complete in less than 4 h and the products are isolated in high yields. The catalytic system is chemoselective for the epoxidation of electron-rich alkenes and allylic alcohols.
New synthetic models of cytochrome P450: How different are they from the natural species?
Kozuch, Sebastian,Leifels, Tycho,Meyer, Dominik,Sbaragli, Laura,Shaik, Sason,Woggon, Wolf-D.
, p. 675 - 684 (2007/10/03)
Soluble and matrix-bound P450 enzyme models have been synthesized carrying a SO3- ligand coordinating to iron. These complexes display features very similar to cofactors of enzymes such as P450cam with respect to electrochemistry and UV/Vis spectroscopy. Further they catalyze epoxidation reactions with turnover numbers up to 1800. DFT calculations revealed that the coordination of SO3- to Fe(III) produces an active species that displays allylic hydroxylation and epoxidation reactivity patterns that are nearly indistinguishable from those calculated for the natural active species of the enzyme cytochrome P450.