ThDP-dependent enzyme catalyzed oxidation of aldehydes
Natural thiamine diphosphate (ThDP)-dependent enzymes are frequently utilized to catalyze the decarboxylation of β-keto acids and the benzoin condensation of aldehydes. Herein, we present a ThDP-dependent enzymatic oxidation of aldehydes mediated by sequential single electron transfer (SET) processes, utilizing hexachloroethane (C<sub>2</sub>Cl<sub>6</sub>) as the oxidant. The reaction exhibits high efficiency (yield up to 99% and turnover number up to 2000) and achieves effective stereoselective control for dynamic kinetic resolutions (e.e. up to 99%). This study uncovers a previously undiscovered capability of ThDP-dependent enzymes, thus broadening the functional repertoire of this enzyme class.
Authors
- Jian Xu (ORCID: https://orcid.org/0000-0003-1728-9536)
- Xinyu Duan
- Xiaohe Chu (ORCID: https://orcid.org/0000-0001-6398-5917)
- Meiting Zhou
- Yuting Zhang (ORCID: https://orcid.org/0000-0002-2171-2096)
- Xiaoyang Chen (ORCID: https://orcid.org/0000-0001-8006-3279)
Institutions
- Jiaxing University (CN)
- Zhejiang University of Technology (CN)
Publication Details
- Journal
- Chemical Science
- Published
- 2025-01-01
- DOI
- https://doi.org/10.1039/d5sc03250d
- Citations
- 1
- Primary Topic
- Biochemical Acid Research Studies
- Type
- article
- Field-Weighted Citation Impact
- 1.11
Funders
- National Natural Science Foundation of China
- National Key Research and Development Program of China
- Natural Science Foundation of Zhejiang Province