4.8 Article

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

Journal

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 58, Issue 23, Pages 7873-7877

Publisher

WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201902380

Keywords

biocatalysis; formate oxidase; hydrogen peroxide; oxidation; oxyfunctionalisation

Funding

  1. European Research Commission (ERC consolidator grant) [648026]
  2. European Union [H2020-BBI-PPP-2015-2-1-720297]
  3. Netherlands Organisation for Scientific Research (VICI grant) [724.014.003]
  4. National Science Foundation (NSF) of the United States [IIP-1540017]
  5. Comunidad de Madrid Synergy CAM Project [Y2018/BIO-4738-EVOCHIMERA-CM]

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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 insitu 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.

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