Selective oxyfunctionalisation of inert C-H bonds is an important but challenging transformation in organic synthesis. Enzymes excel in incorporating an oxygen atom into organic molecules selectively. The well described P450 monooxygenases in particular are extremely active thanks to their iron heme cofactor that can selectively oxidise non activated C-H bonds. These enzymes rely on a complex redox system, whereas peroxygenases utilise only peroxide as oxidant and therefore arise as a better alternative for synthetic chemistry. However, in presence of high concentration of peroxide, the heme cofactor is going through a self-destruction. An in situ generation system is consequently needed to mildly provide the peroxide to the enzyme for performing the catalysis efficiently. All systems are based on the reduction of O2. They all have their own advantages and drawbacks, but have in common the use of rather complex molecules as reductant. The aim of this thesis was to apply formate as an atom efficient reductant for H2O2-dependent enzymes, peroxizymes. The overall system is then the oxyfunctionalisation of molecules using only formate and O2 as reactant.
|Qualification||Doctor of Philosophy|
|Award date||10 Jun 2020|
|Place of Publication||Delft|
|Publication status||Published - 2020|