Non‐natural Cofactor and Formate‐Driven Reductive Carboxylation of Pyruvate
| Autor: | Yuxue Liu, Zongbao K. Zhao, Xiaojia Guo, Xueying Wang, Qian Wang, Wujun Liu, Qing Li |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
biology
010405 organic chemistry Stereochemistry education Reducing equivalent Carbon fixation Malic enzyme Electron donor General Chemistry 010402 general chemistry Formate dehydrogenase 01 natural sciences Redox Catalysis Cofactor 0104 chemical sciences chemistry.chemical_compound chemistry biology.protein Formate |
| Zdroj: | Angewandte Chemie International Edition. 59:3143-3146 |
| ISSN: | 1521-3773 1433-7851 |
| Popis: | A non-natural cofactor and formate driven system for reductive carboxylation of pyruvate is presented. A formate dehydrogenase (FDH) mutant, FDH*, that favors a non-natural redox cofactor, nicotinamide cytosine dinucleotide (NCD), for generation of a dedicated reducing equivalent at the expense of formate were acquired. By coupling FDH* and NCD-dependent malic enzyme (ME*), the successful utilization of formate is demonstrated as both CO2 source and electron donor for reductive carboxylation of pyruvate with a perfect stoichiometry between formate and malate. When 13 C-isotope-labeled formate was used in in vitro trials, up to 53 % of malate had labeled carbon atom. Upon expression of FDH* and ME* in the model host E. coli, the engineered strain produced more malate in the presence of formate and NCD. This work provides an alternative and atom-economic strategy for CO2 fixation where formate is used in lieu of CO2 and offers dedicated reducing power. |
| Databáze: | OpenAIRE |
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