Abstract
Cross-regulation of complex biochemical reaction networks is an essential feature of living systems. In a biomimetic spirit, we report on our efforts to program the temporal activation of an artificial metalloenzyme via cross-regulation by a natural enzyme. In the presence of urea, urease slowly releases ammonia that reversibly inhibits an artificial transfer hydrogenase. Addition of an acid, which acts as fuel, allows to maintain the system out of equilibrium.
| Original language | English |
|---|---|
| Pages (from-to) | 10156-10160 |
| Number of pages | 5 |
| Journal | Angewandte Chemie - International Edition |
| Volume | 56 |
| Issue number | 34 |
| DOIs | |
| Publication status | Published - 2017 |
Keywords
- artificial metalloenzymes
- biocatalysis
- cross-regulation
- hydrogenation
- urease
ASJC Scopus subject areas
- Catalysis
- Chemistry(all)
Fingerprint Dive into the research topics of 'Cross-Regulation of an Artificial Metalloenzyme'. Together they form a unique fingerprint.
Cite this
Okamoto, Y., & Ward, T. R. (2017). Cross-Regulation of an Artificial Metalloenzyme. Angewandte Chemie - International Edition, 56(34), 10156-10160. https://doi.org/10.1002/anie.201702181