Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 58, Issue 23, Pages 7873-7877Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201902380
Keywords
biocatalysis; formate oxidase; hydrogen peroxide; oxidation; oxyfunctionalisation
Categories
Funding
- European Research Commission (ERC consolidator grant) [648026]
- European Union [H2020-BBI-PPP-2015-2-1-720297]
- Netherlands Organisation for Scientific Research (VICI grant) [724.014.003]
- National Science Foundation (NSF) of the United States [IIP-1540017]
- Comunidad de Madrid Synergy CAM Project [Y2018/BIO-4738-EVOCHIMERA-CM]
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available