Thomas R. Ward - NCCR MSE

Thomas R. Ward

Department of Chemistry, University of Basel

Director of NCCR Molecular Systems Engineering

Project Leader

Publications

A. D. Liang, J. Serrano-Plana, R. L. Peterson, T. R. Ward “Artificial Metalloenzymes Based on the Biotin–Streptavidin Technology: Enzymatic Cascades and Directed Evolution“ Acc. Chem. Res. 2019. [DOI]
M. Szponarski, F. Schwizer, T. R. Ward, K. Gademann “On-cell catalysis by surface engineering of live cells with an artificial metalloenzyme“ Commun. Chem. 2018. [DOI]
J. Zhao, J. G. Rebelein, H. Mallin, C. Trindler, M. M. Pellizzoni, T. R. Ward “Genetic Engineering of an Artificial Metalloenzyme for Transfer Hydrogenation of a Self-Immolative Substrate in Escherichia coli’s Periplasm“ J. Am. Chem. Soc. 2018. [DOI]
M. Hestericová, T. Heinisch, M. Lenz, T. R. Ward “Ferritin Encapsulation of Artificial Metalloenzymes: Engineering a Tertiary Coordination Sphere for an Artificial Transfer Hydrogenase“ Dalton Trans. 2018. [DOI]
X. Guo, Y. Okamoto, M. R. Schreier, T. R. WardO. Wenger “Enantioselective synthesis of amines by combining photoredox and enzymatic catalysis in a cyclic reaction network“ Chem. Sci. 2018. [DOI]
Y. Okamoto, R. Kojima, F. Schwizer, E. Bartolami, T. Heinisch, S. MatileM. FusseneggerT. R. Ward “A cell-penetrating artificial metalloenzyme regulates a gene switch in a designer mammalian cell“ Nat. Commun. 2018. [DOI]
J. Zhao, D. G. Bachmann, M. Lenz, D. G. Gillingham, T. R. Ward “An artificial metalloenzyme for carbene transfer based on a biotinylated dirhodium anchored within streptavidin“ Catal. Sci. Technol. 2018. [DOI]
S. G. Keller, B. Probst, T. Heinisch, R. Alberto, T. R. Ward “Photo‐Driven Hydrogen Evolution by an Artificial Hydrogenase Utilizing the Biotin‐Streptavidin Technology“ Helv. Chim. Acta 2018. [DOI]
H. Mallin, T. R. Ward “Streptavidin‐Enzyme Linked Aggregates for the One‐Step Assembly and Purification of Enzyme Cascades“ ChemCatChem 2018. [DOI]
J. G. Rebelein, T. R. Ward “In vivo catalyzed new-to-nature reactions“ Curr. Opin. Biotechnol. 2018. [DOI]
M. M. Pellizzoni, F. Schwizer, C. W. Wood, V. Sabatino, Y. Cotelle, S. Matile, D. N. Woolfson, T. R. Ward “Chimeric Streptavidins as Host Proteins for Artificial Metalloenzymes“ ACS Catal. 2018. [DOI]
T. Heinisch, F. Schwizer, B. Garabedian, E. Csibra, M. Jeschek, J. Vallapurackal, V. B. Pinheiro, P. Marlière, S. PankeT. R. Ward “E. coli surface display of streptavidin for directed evolution of an allylic deallylase“ Chem. Sci. 2018, 9(24):5383-5388. [DOI]
M. JeschekS. PankeT. R. Ward “Artificial Metalloenzymes on the Verge of New-to-Nature Metabolism“ Trends Biotechnol. 2017. [DOI]
S. G. Keller, A. Pannwitz, H. Mallin, O. WengerT. R. Ward “Streptavidin as a Scaffold for Light-Induced Long-Lived Charge Separation“ Chem. Eur. J. 2017. [DOI]
F. Schwizer, Y. Okamoto, T. Heinisch, Y. Gu, M. M. Pellizzoni, V. Lebrun, R. Reuter, V. Köhler, J. C. Lewis, T. R. Ward “Artificial Metalloenzymes: Reaction Scope and Optimization Strategies“ Chem. Rev. 2017. [DOI]
Y. OkamotoT. R. Ward “Cross-Regulation of an Artificial Metalloenzyme“ Angew. Chem. Int. Ed. 2017. [DOI]
L. Liu, Y. Cotelle, J. Klehr, N. Sakai, T. R. WardS. Matile “Anion-π catalysis: bicyclic products with four contiguous stereogenic centers from otherwise elusive diastereospecific domino reactions on π-acidic surfaces“ Chem. Sci. 2017, 8:3770-74. [DOI]
M. Jeschek, M. O. Bahls, V. Schneider, P. Marlière, T. R. WardS. Panke “Biotin-independent Strains of Escherichia coli for Enhanced Streptavidin Production“ Metab. Eng. 2017, 40:33-40. [DOI]
Z. Liu, V. Lebrun, T. Kitanosono, H. Mallin, V. Köhler, D. Häussinger, D. Hilvert, S. Kobayashi, T. R. Ward “Upregulation of an Artificial Zymogen by Proteolysis“ Angew. Chem. Int. Ed. 2016, 55:11587-90. [DOI]
M. Jeschek, R. Reuter, T. Heinisch, C. Trindler, J. Klehr, S. PankeT. R. Ward “Directed evolution of artificial metalloenzymes for in vivo metathesis“ Nature 2016, doi:10.1038/nature19114. [DOI] [More Information]
M. Hestericová, M. R. Correro, M. Lenz, P. F. Corvini, P. Shahgaldian, T. R. Ward “Immobilization of an artificial imine reductase within silica nanoparticles improves its performance“ Chem. Commun. 2016, 52:9462-65. [DOI]
S. G. Keller, A. Pannwitz, F. Schwizer, J. Klehr, O. WengerT. R. Ward “Light-driven electron injection from a biotinylated triarylamine donor to [Ru (diimine) 3] 2+-labeled streptavidin“ Org. Biomol. Chem. 2016, 14:7197-201. [DOI]
Y. OkamotoT. R. WardO. Wenger “From Photodriven Charge Accumulation to Fueling Enzyme Cascades in Molecular Factories“ Chimia 2016, 6:395. [DOI]
Y. Cotelle, N. Chuard, S. Lascano, V. Lebrun, R. Wehlauch, N. Bohni, S. Lörcher, V. Postupalenko, S. ReddyW. MeierC. G. Palivan, K. Gademann, T. R. WardS. Matile “Interfacing Functional Systems“ Chimia 2016, 6:418. [DOI]
P. Rottmann, T. R. WardS. Panke “Compartmentalization – A Prerequisite for Maintaining and Changing an Identity“ Chimia 2016, 6:428
M. JeschekS. PankeT. R. Ward “Chapter Twenty-Three-Periplasmic Screening for Artificial Metalloenzymes“ Methods Enzymol. 2016, 580:539-56. [DOI]
E. A. Miłopolska, M. Kuss-Petermann, M. Neuburger, O. WengerT. R. Ward “N-Heterocyclic carbene ligands bearing a naphthoquinone appendage: Synthesis and coordination chemistry“ Polyhedron 2016, 103:261-66. [DOI]
Y. Cotelle, V. Lebrun, N. Sakai, T. R. WardS. Matile “Anion‑π Enzymes“ ACS Cent. Sci. 2016:DOI: 10.1021/acscentsci.6b00097. [DOI] [More Information]
Y. Okamoto, V. Köhler, C. E. Paul, F. Hollmann, T. R. Ward “Efficient In Situ Regeneration of NADH Mimics by an Artificial Metalloenzyme“ ACS Catal. 2016, 6:3553. [DOI]
Y. Okamoto, V. Köhler, T. R. Ward “An NAD(P)H-Dependent Artificial Transfer Hydrogenase for Multienzymatic Cascades“ J. Am. Chem. Soc. 2016, 138:5781. [DOI]
H. Mallin, M. Hestericová, R. Reuter, T. R. Ward “Library design and screening protocol for artificial metalloenzymes based on the biotin-streptavidin technology“ Nat. Protoc. 2016, 11:835. [DOI]
Y. Cotelle, S. Benz, A. Avestro, T. R. Ward, N. Sakai, S. Matile “Anion-π Catalysis of Enolate Chemistry: Rigidified Leonard Turns as a General Motif to Run Reactions on Aromatic Surfaces“ Angew. Chem. Int. Ed. 2016, 55:4275. [DOI]
T. Heinisch, M. Pellizzoni, M. Dürrenberger, C. E. Tinberg, V. Köhler, J. Klehr, D. Häussinger, D. Baker, T. R. Ward “Improving the Catalytic Performance of an Artificial Metalloenzyme by Computational Design“ J. Am. Chem. Soc. 2016, 137:10414. [DOI]
A. Chatterjee, H. Mallin, J. Klehr, J. Vallapurackal, A. D. Finke, L. Vera, M. Marsh, T. R. Ward “An enantioselective artificial Suzukiase based on the biotin–streptavidin technology “ Chem. Sci. 2016, 7:673. [DOI]
R. Reuter, T. R. Ward “Profluorescent substrates for the screening of olefin metathesis catalysts“ Beilstein J. Org. Chem. 2015, 11:1886-92. [DOI]
T. Heinisch, T. R. Ward “Latest Developments in Metalloenzyme Design and Repurposing“ Eur. J. Inorg. Chem. 2015, 2015:3406-18. [DOI]
J. Zhao, A. Kajetanowicz, T. R. Ward “Carbonic anhydrase II as host protein for the creation of a biocompatible artificial metathesase“ Org. Biomol. Chem. 2015, 13:5652-55. [DOI]
N. Fujieda, J. Schätti, E. Stuttfeld, K. Ohkubo, T. Maier, S. Fukuzumi, T. R. Ward “Enzyme repurposing of a hydrolase as an emergent peroxidase upon metal binding“ Chem. Sci. 2015, 6:4060. [DOI]
T. Quinto, D. Haussinger, V. Kohler, T. R. Ward “Artificial metalloenzymes for the diastereoselective reduction of NAD(+) to NAD(2)H“ Org. Biomol. Chem. 2015, 13:357-60. [DOI]