NCCR MSE - Molecular Factories Based on Artificial Metalloenzymes
Research Project
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01.07.2014
- 30.06.2018
UNIverse - Public Research Portal
Artificial metalloenzymes (ArMs) result from the incorporation of abiotic cofactors within a host protein. In collaboration with various groups of the NCCR, we aim at engineering metabolic pathways incorporating ArMs. The challenges addressed during this funding period include: i) successful compartmentalization and evolution of ArMs within the periplasm of E coli, ii) engineering enzyme cascades with ArMs and iii) cross-regulation of ArMs.
Publications
Heinisch, Tillmann et al. (2015) ‘Improving the catalytic performance of an artificial metalloenzyme by computational design’, Journal of the American Chemical Society, 137(32), pp. 10414–9. Available at: https://doi.org/10.1021/jacs.5b06622.
Heinisch, Tillmann and Ward, Thomas R. (2015) ‘Latest Developments in Metalloenzyme Design and Repurposing’, European Journal of Inorganic Chemistry, (21), pp. 3406–3418. Available at: https://doi.org/10.1002/ejic.201500408.
Quinto, Tommaso et al. (2015) ‘Artificial metalloenzymes for the diastereoselective reduction of NAD+ to NAD2H’, Organic and Biomolecular Chemistry, 13, pp. 357–360. Available at: https://doi.org/10.1039/c4ob02071e.
Reuter, Raphael and Ward, Thomas R. (2015) ‘Profluorescent substrates for the screening of olefin metathesis catalysts’, Beilstein journal of organic chemistry, 11, pp. 1886–92. Available at: https://doi.org/10.3762/bjoc.11.203.
Members (3)
Thomas R. Ward
Principal Investigator
Tillmann Heinisch
Project Member
Yasunori Okamoto
Project Member
Research Groups