Thomas R. Ward

Department of Chemistry, University of Basel

Director of the NCCR Molecular Systems Engineering



+41 61 207 10 04

Read more about the Ward-Group here.


M. Hestericová, T. Heinisch, M. Lenz, T. R. WardFerritin Encapsulation of Artificial Metalloenzymes: Engineering a Tertiary Coordination Sphere for an Artificial Transfer Hydrogenase“ Dalton Trans. (2018). [Link]
X. Guo, Y. Okamoto, M. R. Schreier, T. R. WardO. WengerEnantioselective synthesis of amines by combining photoredox and enzymatic catalysis in a cyclic reaction network“ Chem. Sci. (2018). [Link]
Y. Okamoto, R. Kojima, F. Schwizer, E. Bartolami, T. Heinisch, S. MatileM. FusseneggerT. R. WardA cell-penetrating artificial metalloenzyme regulates a gene switch in a designer mammalian cell“ Nat. Commun. (2018). [Link]
J. Zhao, D. G. Bachmann, M. Lenz, D. G. Gillingham, T. R. WardAn artificial metalloenzyme for carbene transfer based on a biotinylated dirhodium anchored within streptavidin“ Catal. Sci. Technol. (2018). [Link]
S. G. Keller, B. Probst, T. Heinisch, R. Alberto, T. R. WardPhoto‐Driven Hydrogen Evolution by an Artificial Hydrogenase Utilizing the Biotin‐Streptavidin Technology“ Helv. Chim. Acta (2018). [Link]
H. Mallin, T. R. WardStreptavidin‐Enzyme Linked Aggregates for the One‐Step Assembly and Purification of Enzyme Cascades“ ChemCatChem (2018). [Link]
J. G. Rebelein, T. R. WardIn vivo catalyzed new-to-nature reactions“ Curr. Opin. Biotechnol. (2018). [Link]
M. M. Pellizzoni, F. Schwizer, C. W. Wood, V. Sabatino, Y. Cotelle, S. Matile, D. N. Woolfson, T. R. WardChimeric Streptavidins as Host Proteins for Artificial Metalloenzymes“ ACS Catal. (2018). [Link]
M. Jeschek, S. PankeT. R. WardArtificial Metalloenzymes on the Verge of New-to-Nature Metabolism“ Trends Biotechnol. (2017). [Link]
S. G. Keller, A. Pannwitz, H. Mallin, O. WengerT. R. WardStreptavidin as a Scaffold for Light-Induced Long-Lived Charge Separation“ Chem. Eur. J. (2017). [Link]
F. Schwizer, Y. Okamoto, T. Heinisch, Y. Gu, M. M. Pellizzoni, V. Lebrun, R. Reuter, V. Köhler, J. C. Lewis, T. R. WardArtificial Metalloenzymes: Reaction Scope and Optimization Strategies“ Chem. Rev. (2017). [Link]
Y. OkamotoT. R. WardCross-Regulation of an Artificial Metalloenzyme“ Angew. Chem. Int. Ed. (2017). [Link]
L. Liu, Y. Cotelle, J. Klehr, N. Sakai, T. R. WardS. MatileAnion-π catalysis: bicyclic products with four contiguous stereogenic centers from otherwise elusive diastereospecific domino reactions on π-acidic surfaces“ Chem. Sci. 8, 3770-74 (2017). [Link]
M. Jeschek, M. O. Bahls, V. Schneider, P. Marlière, T. R. WardS. PankeBiotin-independent Strains of Escherichia coli for Enhanced Streptavidin Production“ Metab. Eng. 40, 33-40 (2017). [Link]
Z. Liu, V. Lebrun, T. Kitanosono, H. Mallin, V. Köhler, D. Häussinger, D. Hilvert, S. Kobayashi, T. R. WardUpregulation of an Artificial Zymogen by Proteolysis“ Angew. Chem. Int. Ed. 55, 11587-90 (2016). [Link]
M. Jeschek, R. Reuter, T. Heinisch, C. Trindler, J. Klehr, S. PankeT. R. WardDirected evolution of artificial metalloenzymes for in vivo metathesis“ Nature doi:10.1038/nature19114 (2016). [Link] [More Information]
M. Hestericová, M. R. Correro, M. Lenz, P. F. Corvini, P. Shahgaldian, T. R. WardImmobilization of an artificial imine reductase within silica nanoparticles improves its performance“ Chem. Commun. 52, 9462-65 (2016). [Link]
S. G. Keller, A. Pannwitz, F. Schwizer, J. Klehr, O. WengerT. R. WardLight-driven electron injection from a biotinylated triarylamine donor to [Ru (diimine) 3] 2+-labeled streptavidin“ Org. Biomol. Chem. 14, 7197-201 (2016). [Link]
Y. OkamotoT. R. WardO. WengerFrom Photodriven Charge Accumulation to Fueling Enzyme Cascades in Molecular Factories“ Chimia 6, 395 (2016). [Link]
Y. CotelleN. Chuard, S. Lascano, V. Lebrun, R. Wehlauch, N. Bohni, S. Lörcher, V. Postupalenko, S. ReddyW. MeierC. G. Palivan, K. Gademann, T. R. WardS. MatileInterfacing Functional Systems“ Chimia 6, 418 (2016). [Link]
P. RottmannT. R. WardS. PankeCompartmentalization – A Prerequisite for Maintaining and Changing an Identity“ Chimia 6, 428 (2016).
M. Jeschek, S. PankeT. R. WardChapter Twenty-Three-Periplasmic Screening for Artificial Metalloenzymes“ Methods Enzymol. 580, 539-56 (2016). [Link]
E. A. Miłopolska, M. Kuss-Petermann, M. Neuburger, O. WengerT. R. WardN-Heterocyclic carbene ligands bearing a naphthoquinone appendage: Synthesis and coordination chemistry“ Polyhedron 103, 261-66 (2016). [Link]
Y. Cotelle, V. Lebrun, N. Sakai, T. R. WardS. MatileAnion‑π Enzymes“ ACS Cent. Sci., DOI: 10.1021/acscentsci.6b00097 (2016). [Link] [More Information]
Y. Okamoto, V. Köhler, C. E. Paul, F. Hollmann, T. R. WardEfficient In Situ Regeneration of NADH Mimics by an Artificial Metalloenzyme“ ACS Catal. 6, 3553 (2016). [Link]
Y. Okamoto, V. Köhler, T. R. WardAn NAD(P)H-Dependent Artificial Transfer Hydrogenase for Multienzymatic Cascades“ J. Am. Chem. Soc. 138, 5781 (2016). [Link]
H. Mallin, M. Hestericová, R. Reuter, T. R. WardLibrary design and screening protocol for artificial metalloenzymes based on the biotin-streptavidin technology“ Nat. Protoc. 11, 835 (2016). [Link]
Y. Cotelle, S. Benz, A. Avestro, T. R. Ward, N. Sakai, S. MatileAnion-π Catalysis of Enolate Chemistry: Rigidified Leonard Turns as a General Motif to Run Reactions on Aromatic Surfaces“ Angew. Chem. Int. Ed. 55, 4275 (2016). [Link]
T. Heinisch, M. Pellizzoni, M. Dürrenberger, C. E. Tinberg, V. Köhler, J. Klehr, D. Häussinger, D. Baker, T. R. WardImproving the Catalytic Performance of an Artificial Metalloenzyme by Computational Design“ J. Am. Chem. Soc. 137, 10414 (2016). [Link]
A. Chatterjee, H. Mallin, J. Klehr, J. Vallapurackal, A. D. Finke, L. Vera, M. Marsh, T. R. WardAn enantioselective artificial Suzukiase based on the biotin–streptavidin technology “ Chem. Sci. 7, 673 (2016). [Link]
R. Reuter, T. R. WardProfluorescent substrates for the screening of olefin metathesis catalysts“ Beilstein J. Org. Chem. 11, 1886-92 (2015). [Link]
T. Heinisch, T. R. WardLatest Developments in Metalloenzyme Design and Repurposing“ Eur. J. Inorg. Chem. 2015, 3406-18 (2015). [Link]
J. Zhao, A. Kajetanowicz, T. R. WardCarbonic anhydrase II as host protein for the creation of a biocompatible artificial metathesase“ Org. Biomol. Chem. 13, 5652-55 (2015). [Link]
N. Fujieda, J. Schätti, E. Stuttfeld, K. Ohkubo, T. Maier, S. Fukuzumi, T. R. WardEnzyme repurposing of a hydrolase as an emergent peroxidase upon metal binding“ Chem. Sci. 6, 4060 (2015). [Link]
T. Quinto, D. Haussinger, V. Kohler, T. R. WardArtificial metalloenzymes for the diastereoselective reduction of NAD(+) to NAD(2)H“ Org. Biomol. Chem. 13, 357-60 (2015). [Link]