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NCCR MSE - Molecular Factories Based on Artificial Metalloenzymes

Research Project
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01.07.2014
 - 30.06.2018

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.

URLs
URLs

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.

URLs
URLs

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.

URLs
URLs

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.

URLs
URLs

Members (3)

Profile Photo

Thomas R. Ward

Principal Investigator
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Tillmann Heinisch

Project Member
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Yasunori Okamoto

Project Member