Formate Oxidase (FOx) from Aspergillus oryzae: One Catalyst Enables Diverse H2O2‐Dependent Biocatalytic Oxidation Reactions

An increasing number of biocatalytic oxidation reactions rely on H2O2 as a clean oxidant. The poor robustness of most enzymes towards H2O2, however, necessitates more efficient systems for in situ H2O2 generation. In analogy to the well‐known formate dehydrogenase to promote NADH‐dependent reactions, we here propose employing formate oxidase (FOx) to promote H2O2‐dependent enzymatic oxidation reactions. Even under non‐optimised conditions, high turnover numbers for coupled FOx/peroxygenase catalysis were achieved. Out of thin air: The formate oxidase from Aspergillus oryzae (AoFOx) enables in situ H2O2 generation from formate and ambient oxygen and can be used to enable a broad range of biocatalytic oxidation/oxyfunctionalisation reactions. Even under non‐optimised conditions, high turnover numbers for coupled FOx/peroxygenase catalysis were achieved.