Chapter 24: Vanadium Chloroperoxidases as Versatile Biocatalysts

In this chapter the catalytic and structural properties of the vanadium chloroperoxidases will be discussed with an emphasis on their superb activity and stability under operational conditions. These properties make these enzymes attractive catalysts in organic synthesis and allow a number of applications. Some of the more recent findings are...

Selective aerobic oxidation reactions using a combination of photocatalytic water oxidation and enzymatic oxyfunctionalizations

Peroxygenases offer an attractive means to address challenges in selective oxyfunctionalization chemistry. Despite this, their application in synthetic chemistry remains challenging due to their facile inactivation by the stoichiometric oxidant H₂O₂. Often atom-inefficient peroxide generation systems are required, which...

Halofunctionalization of alkenes by vanadium chloroperoxidase from Curvularia inaequalis

The vanadium-dependent chloroperoxidase from Curvularia inaequalis is a stable and efficient biocatalyst for the hydroxyhalogenation of a broad range of alkenes into halohydrins. Up to 1 200 000 TON with 69 s−1 TOF were observed for the biocatalyst. A bienzymatic cascade to yield epoxides as reaction products is presented.

A Biocatalytic Aza-Achmatowicz Reaction

A catalytic, enzyme-initiated (aza-) Achmatowicz reaction is presented. The involvement of a robust vanadium-dependent peroxidase from Curvularia inaequalis allows the simple use of H₂O₂ and catalytic amounts of bromide.