Formate Oxidase (FOx) from Aspergillus oryzae: One Catalyst Enables Diverse H O -Dependent Biocatalytic Oxidation Reactions.

An increasing number of biocatalytic oxidation reactions rely on H O as a clean oxidant. The poor robustness of most enzymes towards H O , however, necessitates more efficient systems for in situ H O generation. In analogy to the well-known formate dehydrogenase to promote NADH-dependent reactions, we here propose employing formate oxidase (FOx) to promote H O -dependent enzymatic oxidation reactions.

Multienzymatic in situ hydrogen peroxide generation cascade for peroxygenase-catalysed oxyfunctionalisation reactions.

There is an increasing interest in the application of peroxygenases in biocatalysis, because of their ability to catalyse the oxyfunctionalisation reaction in a stereoselective fashion and with high catalytic efficiencies, while using hydrogen peroxide or organic peroxides as oxidant. However, enzymes belonging to this class exhibit a very low stability in the presence of peroxides. With the aim of bypassing this fast and irreversible inactivation, we study the use of a gradual supply of hydrogen peroxide to maintain its concentration at stoichiometric levels.