Morita, Iori, Faraone, Adriana, Salvisberg, Elias, Zhang, Kailin, Jakob, Roman P., Maier, Timm, & Ward, Thomas R. (2024). Directed Evolution of an Artificial Hydroxylase Based on a Thermostable Human Carbonic Anhydrase Protein [Journal-article]. ACS Catalysis, 14, 17171–17179. https://doi.org/10.1021/acscatal.4c04163

Vornholt, Tobias, Leiss-Maier, Florian, Jeong, Woo Jae, Zeymer, Cathleen, Song, Woon Ju, Roelfes, Gerard, & Ward, Thomas R. (2024). Artificial metalloenzymes [Journal-article]. Nature Reviews Methods Primers, 4. https://doi.org/10.1038/s43586-024-00356-w

Mukherjee, Manjistha, Waser, Valerie, Morris, Elinor F., Igareta, Nico V., Follmer, Alec H., Jakob, Roman P., Maier, Timm, Üzümcü, Dilbirin, & Ward, Thomas R. (2024). Artificial Peroxidase Based on the Biotin–Streptavidin Technology that Rivals the Efficiency of Natural Peroxidases. ACS Catalysis, 14(21), 16266–16276. https://doi.org/10.1021/acscatal.4c03208

Renno, Giacomo, Chen, Dongping, Zhang, Qing‐Xia, Gomila, Rosa M., Frontera, Antonio, Sakai, Naomi, Ward, Thomas R., & Matile, Stefan. (2024). Pnictogen‐Bonding Enzymes [Journal-article]. Angewandte Chemie International Edition, 63(45). https://doi.org/10.1002/anie.202411347

Yu, Kun, & Ward, Thomas R. (2024). C–H functionalization reactions catalyzed by artificial metalloenzymes [Journal-article]. Journal of Inorganic Biochemistry, 258. https://doi.org/10.1016/j.jinorgbio.2024.112621

Morita, Iori, & Ward, Thomas R. (2024). Recent advances in the design and optimization of artificial metalloenzymes [Journal-article]. Current Opinion in Chemical Biology, 81. https://doi.org/10.1016/j.cbpa.2024.102508

Zhang, Xiang, Chen, Dongping, Stropp, Julian, Tachibana, Ryo, Zou, Zhi, Klose, Daniel, & Ward, Thomas R. (2024). Repurposing myoglobin into an abiological asymmetric ketoreductase [Journal-article]. Chem, 10(8), 2577–2589. https://doi.org/10.1016/j.chempr.2024.06.010

Zou, Zhi, Higginson, Bradley, & Ward, Thomas R. (2024). Creation and optimization of artificial metalloenzymes: Harnessing the power of directed evolution and beyond [Journal-article]. Chem, 10(8), 2373–2389. https://doi.org/10.1016/j.chempr.2024.07.007

Chen, Dongping, Zhang, Xiang, Vorobieva, Anastassia Andreevna, Tachibana, Ryo, Stein, Alina, Jakob, Roman P., Zou, Zhi, Graf, Damian Alexander, Li, Ang, Maier, Timm, Correia, Bruno E., & Ward, Thomas R. (2024). An evolved artificial radical cyclase enables the construction of bicyclic terpenoid scaffolds via an H-atom transfer pathway [Journal-article]. Nature Chemistry, 16(10), 1656–1664. https://doi.org/10.1038/s41557-024-01562-5

Zou, Zhi, Wu, Shuke, Gerngross, Daniel, Lozhkin, Boris, Chen, Dongping, Tachibana, Ryo, & Ward, Thomas R. (2024). Combining an artificial metathase with a fatty acid decarboxylase in a whole cell for cycloalkene synthesis [Journal-article]. Nature Synthesis, 3, 1113–1123. https://doi.org/10.1038/s44160-024-00575-9

Baiyoumy, Alain, Vinck, Robin, & Ward, Thomas R. (2024). The Two Janus Faces of CpRu‐Based Deallylation Catalysts and Their Application for in Cellulo Prodrug Uncaging [Journal-article]. Helvetica Chimica Acta, 107(7). https://doi.org/10.1002/hlca.202400053

Vornholt, Tobias, Mutný, Mojmír, Schmidt, Gregor W., Schellhaas, Christian, Tachibana, Ryo, Panke, Sven, Ward, Thomas R., Krause, Andreas, & Jeschek, Markus. (2024). Enhanced Sequence-Activity Mapping and Evolution of Artificial Metalloenzymes by Active Learning [Journal-article]. ACS Central Science, 10(7), 1357–1370. https://doi.org/10.1021/acscentsci.4c00258

Yu, Kun, Tachibana, Ryo, Rumo, Corentin, Igareta, Nico V., Zhang, Kailin, & Ward, Thomas R. (2024). Artificial Metalloenzyme‐Catalyzed Enantioselective Carboamination of Alkenes [Journal-article]. ChemCatChem, 16(17). https://doi.org/10.1002/cctc.202400365

Burgener, Simon, Zhang, Xiang, & Ward, Thomas R. (2024). Artificial Metalloenzymes for Enantioselective Catalysis. In Cossy, Janine (ed.), Comprehensive Chirality (pp. 71–110). Elsevier. https://doi.org/10.1016/b978-0-32-390644-9.00082-2

Hua, Yong, Zou, Zhi, Prescimone, Alessandro, Ward, Thomas R, Mayor, Marcel, & Köhler, Valentin. (2024). NSPs: chromogenic linkers for fast, selective, and irreversible cysteine modification [Journal-article]. Chemical Science, 15(28), 10997–11004. https://doi.org/10.1039/d4sc01710b

Yu, K., Zhang, K., Jakob, R. P., Maier, T., & Ward, T. R. (2024). An artificial nickel chlorinase based on the biotin–streptavidin technology [Journal-article]. Chemical Communications, 60, 1944–1947. https://doi.org/10.1039/d3cc05847f

Burgener, Simon, Dačević, Bratislav, Zhang, Xiang, & Ward, Thomas R. (2023). Binding Interactions and Inhibition Mechanisms of Gold Complexes in Thiamine Diphosphate-Dependent Enzymes [Journal-article]. Biochemistry, 62(22), 3303–3311. https://doi.org/10.1021/acs.biochem.3c00376

Vornholt, Tobias, Jončev, Zlatko, Sabatino, Valerio, Panke, Sven, Ward, Thomas R., Sparr, Christof, & Jeschek, Markus. (2023). An Artificial Metalloenzyme for Atroposelective Metathesis** [Journal-article]. ChemCatChem, 15(23). https://doi.org/10.1002/cctc.202301113

Hua, Yong, Zou, Zhi, Prescimone, Alessandro, Ward, Thomas R., Mayor, Marcel, & Köhler, Valentin. (2023). Click, Lock & Dye: a chromogenic handle for selective cysteine modification [Posted-content]. In Chemrxiv. Cambridge University Press. https://doi.org/10.26434/chemrxiv-2023-83gph

Mukherjee, Manjistha, Waser, Valerie, Igareta, Nico V., Follmer, Alec H., jakob, Roman P., Maier, Timm, Üzümcü, Dilbirin, & Ward, Thomas R. (2023). An Artificial Peroxidase based on the Biotin-Streptavidin Technology that Rivals the Efficiency of Natural Peroxidases [Posted-content]. In ChemRxiv. Cambridge University Press. https://doi.org/10.26434/chemrxiv-2023-s830k

Tachibana, Ryo, Zhang, Kailin, Zou, Zhi, Burgener, Simon, & Ward, Thomas R. (2023). A Customized Bayesian Algorithm to Optimize Enzyme-Catalyzed Reactions [Journal-article]. ACS Sustainable Chemistry & Engineering, 11(33), 12336–12344. https://doi.org/10.1021/acssuschemeng.3c02402

Beweries, Torsten, Buchmeiser, Michael R., Bugden, Frances E., Champness, Neil R., Chanbasha, Basheer, Costas, Miquel, Echeverria, Jorge, Eisenstein, Odile, Ferguson, Calum, Goodall, Joe C., Gramage-Doria, Rafael, Greenhalgh, Mark, Gyton, Matthew, Ham, Rens, Kennepohl, Pierre, Lewandowski, Bartosz, Liu, Wei-Chun, Macgregor, Stuart A., Mahmudov, Kamran T., et al. (2023). Make - underpinning concepts of the synthesis of systems where non-covalent interactions are important: general discussion. Faraday Discussions, 244, 434–454. https://doi.org/10.1039/d3fd90012f

Beweries, Torsten, Buchmeiser, Michael R. R., Champness, Neil R. R., Costas, Miquel, Duhme-Klair, Anne, Echeverria, Jorge, Eisenstein, Odile, Ferguson, Calum T. J., Goodall, Joe C. C., Gramage-Doria, Rafael, Gyton, Matthew, Ham, Rens, Herres-Pawlis, Sonja, Johnson, Chloe L. L., Kennepohl, Pierre, Lewandowski, Bartosz, Linnebank, Pim R. R., Macgregor, Stuart A. A., Mahmudov, Kamran T. T., et al. (2023). Manipulate - techniques to manipulate the surroundings of a synthetic catalyst to control activity and selectivity: general discussion. Faraday Discussions, 244, 96–118. https://doi.org/10.1039/d3fd90013d

Chanbasha, Basheer, Costas, Miquel, Echeverria, Jorge, Eisenstein, Odile, Greenhalgh, Mark, Kennepohl, Pierre, Kirrander, Adam, Linnebank, Pim R. R., Macgregor, Stuart A. A., Mahmudov, Kamran T. T., Martin-Fernandez, Carlos, Meeus, Eva, Perutz, Robin N., Poater, Albert N., Morris, Josh, Reek, Joost N. H., Rouse, Ian, Toste, Dean, Trujillo, Cristina, et al. (2023). Model - state-of-the-art modelling and computational analysis of reactive sites: general discussion. Faraday Discussions, 244, 336–355. https://doi.org/10.1039/d3fd90015k

Igareta, Nico V., Tachibana, Ryo, Spiess, Daniel C., Peterson, Ryan L., & Ward, Thomas R. (2023). Spiers Memorial Lecture: Shielding the active site: a streptavidin superoxide-dismutase chimera as a host protein for asymmetric transfer hydrogenation. FARADAY DISCUSSIONS, 244, 9–20. https://doi.org/10.1039/d3fd00034f

Meeus, Eva J., Igareta, Nico V., Morita, Iori, Ward, Thomas R., de Bruin, Bas, & Reek, Joost N. H. (2023). A Co(TAML)-based artificial metalloenzyme for asymmetric radical-type oxygen atom transfer catalysis [Journal-article]. Chemical Communications, 59(98), 14567–14570. https://doi.org/10.1039/d3cc04723g

Wang, Weijin, Tachibana, Ryo, Zou, Zhi, Chen, Dongping, Zhang, Xiang, Lau, Kelvin, Pojer, Florence, Ward, Thomas R., & Hu, Xile. (2023). Manganese Transfer Hydrogenases Based on the Biotin-Streptavidin Technology. Angewandte Chemie International Edition, e202311896. https://doi.org/10.1002/anie.202311896

Ward, Thomas R., & Copéret, Christophe. (2023). Introduction: Bridging the Gaps: Learning from Catalysis across Boundaries. Chemical Reviews, 123(9), 5221–5224. https://doi.org/10.1021/acs.chemrev.3c00029

Waser, Valerie, Mukherjee, Manjistha, Tachibana, Ryo, Igareta, Nico V., & Ward, Thomas R. (2023). An Artificial [Fe₄S₄]-Containing Metalloenzyme for the Reduction of CO₂ to Hydrocarbons. Journal of the American Chemical Society, 145(27), 14823–14830. https://doi.org/10.1021/jacs.3c03546

Waser, Valerie, & Ward, Thomas R. (2023). Aqueous stability and redox chemistry of synthetic [Fe₄S₄] clusters. Coordination chemistry reviews, 495, 215377. https://doi.org/10.1016/j.ccr.2023.215377

Yu, Kun, Zou, Zhi, Igareta, Nico V., Tachibana, Ryo, Bechter, Julia, Köhler, Valentin, Chen, Dongping, & Ward, Thomas R. (2023). Artificial Metalloenzyme-Catalyzed Enantioselective Amidation via Nitrene Insertion in Unactivated C(sp³)-H Bonds. Journal of the American Chemical Society, 145(30), 16621–16629. https://doi.org/10.1021/jacs.3c03969

Burgener, Simon, & Ward, Thomas R. (2022). Dihydrogen-dependent carbon dioxide reductase: Hardwired for CO₂ reduction. Chem Catalysis, 2(10), 2427–2429. https://doi.org/10.1016/j.checat.2022.09.031

Hirschi, Stephan, Ward, Thomas R., Meier, Wolfgang P., Müller, Daniel J., & Fotiadis, Dimitrios. (2022). Synthetic Biology: Bottom-Up Assembly of Molecular Systems. Chemical Reviews, 122(21), 16294–16328. https://doi.org/10.1021/acs.chemrev.2c00339

Rumo, Corentin, Stein, Alina, Klehr, Juliane, Tachibana, Ryo, Prescimone, Alessandro, Haussinger, Daniel, & Ward, Thomas R. (2022). An Artificial Metalloenzyme Based on a Copper Heteroscorpionate Enables sp³ C-H Functionalization via Intramolecular Carbene Insertion. Journal of the American Chemical Society, 144(26), 11676–11684. https://doi.org/10.1021/jacs.2c03311

Schreier, Mirjam R., Guo, Xingwei, Pfund, Björn, Okamoto, Yasunori, Ward, Thomas R., Kerzig, Christoph, & Wenger, Oliver S. (2022). Water-Soluble Tris(cyclometalated) Iridium(III) Complexes for Aqueous Electron and Energy Transfer Photochemistry. Accounts of Chemical Research, 55(9), 1290–1300. https://doi.org/10.1021/acs.accounts.2c00075

Stein, Alina, Liang, Alexandria Deliz, Sahin, Reyhan, & Ward, Thomas R. (2022). Incorporation of metal-chelating unnatural amino acids into halotag for allylic deamination. Journal of Organometallic Chemistry, 962, 122272. https://doi.org/10.1016/j.jorganchem.2022.122272

Vallapurackal, Jaicy, Stucki, Ariane, Liang, Alexandria Deliz, Klehr, Juliane, Dittrich, Petra S., & Ward, Thomas R. (2022). Ultrahigh-Throughput Screening of an Artificial Metalloenzyme using Double Emulsions. Angewandte Chemie International Edition, 61(48), e202207328. https://doi.org/10.1002/anie.202207328

Baiyoumy, Alain, Vallapurackal, Jaicy, Schwizer, Fabian, Heinisch, Tillmann, Kardashliev, Tsvetan, Held, Martin, Panke, Sven, & Ward, Thomas R. (2021). Directed Evolution of a Surface-Displayed Artificial Allylic Deallylase Relying on a GFP Reporter Protein. ACS Catalysis, 11(17), 10705–10712. https://doi.org/10.1021/acscatal.1c02405

Christoffel, Fadri, Igareta, Nico, Pellizzoni, Michela M., Tiessler-Sala, Laura, Lozhkin, Boris, Spiess, Daniel C., Lledos, Agusti, Marechal, Jean-Didier, Peterson, Ryan L., & Ward, Thomas R. (2021). Design and evolution of chimeric streptavidin for protein-enabled dual gold catalysis. Nature Catalysis, 4(8), 643–+. https://doi.org/10.1038/s41929-021-00651-9

Di Leone, Stefano, Vallapurackal, Jaicy, Yorulmaz Avsar, Saziye, Kyropolou, Myrto, Ward, Thomas R., Palivan, Cornelia G., & Meier, Wolfgang. (2021). Expanding the Potential of the Solvent-Assisted Method to Create Bio-Interfaces from Amphiphilic Block Copolymers. Biomacromolecules, 22(7), 3005–3016. https://doi.org/10.1021/acs.biomac.1c00424

Fischer, Sandro, Ward, Thomas R., & Liang, Alexandria D. (2021). Engineering a Metathesis-Catalyzing Artificial Metalloenzyme Based on HaloTag. ACS Catalysis, 11(10), 6343–6347. https://doi.org/10.1021/acscatal.1c01470

Lozhkin, Boris, & Ward, Thomas R. (2021). A Close-to-Aromatize Approach for the Late-Stage Functionalization through Ring Closing Metathesis. Helvetica Chimica Acta, 104(5), e2100024. https://doi.org/10.1002/hlca.202100024

Lozhkin, Boris, & Ward, Thomas R. (2021). Bioorthogonal strategies for the in vivo synthesis or release of drugs. Bioorganic & medicinal chemistry, 45, 116310. https://doi.org/10.1016/j.bmc.2021.116310

Miró-Vinyals, Carla, Stein, Alina, Fischer, Sandro, Ward, Thomas R., & Deliz Liang, Alexandria. (2021). HaloTag Engineering for Enhanced Fluorogenicity and Kinetics with a Styrylpyridium Dye. ChemBioChem, 22(24), 3398–3401. https://doi.org/10.1002/cbic.202100424

Stein, Alina, Chen, Dongping, Igareta, Nico V., Cotelle, Yoann, Rebelein, Johannes G., & Ward, Thomas R. (2021). A Dual Anchoring Strategy for the Directed Evolution of Improved Artificial Transfer Hydrogenases Based on Carbonic Anhydrase. ACS Central Science, 7(11), 1874–1884. https://doi.org/10.1021/acscentsci.1c00825

Stucki, Ariane, Vallapurackal, Jaicy, Ward, Thomas R., & Dittrich, Petra S. (2021). Droplet Microfluidics and Directed Evolution of Enzymes: an Intertwined Journey. Angewandte Chemie International Edition, 60(46), 24368–24387. https://doi.org/10.1002/anie.202016154

Vornholt, Tobias, Christoffel, Fadri, Pellizzoni, Michela M., Panke, Sven, Ward, Thomas R., & Jeschek, Markus. (2021). Systematic engineering of artificial metalloenzymes for new-to-nature reactions. Science Advances, 7(4), eabe4208. https://doi.org/10.1126/sciadv.abe4208

Bullock, R. Morris, Chen, Jingguang G., Gagliardi, Laura, Chirik, Paul J., Farha, Omar K., Hendon, Christopher H., Jones, Christopher W., Keith, John A., Klosin, Jerzy, Minteer, Shelley D., Morris, Robert H., Radosevich, Alexander T., Rauchfuss, Thomas B., Strotman, Neil A., Vojvodic, Aleksandra, Ward, Thomas R., Yang, Jenny Y., & Surendranath, Yogesh. (2020). Using nature’s blueprint to expand catalysis with Earth-abundant metals. Science, 369(6505), 3183. https://doi.org/10.1126/science.abc3183

Davis, Holly Jane, Häussinger, Daniel, Ward, Thomas R., & Okamoto, Yasunori. (2020). A visible-light promoted amine oxidation catalyzed by a Cp*Ir complex. ChemCatChem, 12(18), 4512–4516. https://doi.org/10.1002/cctc.202000488

Miller, Kelsey R., Paretsky, Jonathan D., Follmer, Alec H., Heinisch, Tillmann, Mittra, Kaustuv, Gul, Sheraz, Kim, In-Sik, Fuller, Franklin D., Batyuk, Alexander, Sutherlin, Kyle D., Brewster, Aaron S., Bhowmick, Asmit, Sauter, Nicholas K., Kern, Jan, Yano, Junko, Green, Michael T., Ward, Thomas R., & Borovik, A. S. (2020). Artificial Iron Proteins: Modeling the Active Sites in Non-Heme Dioxygenases. Inorganic Chemistry, 59(9), 6000–6009. https://doi.org/10.1021/acs.inorgchem.9b03791

Sabatino, Valerio, Staub, Dario, & Ward, Thomas R. (2020). Synthesis of N-Substituted Indoles via Aqueous Ring-Closing Metathesis. Catalysis Letters, 151(1), 17–17. https://doi.org/10.1007/s10562-020-03271-3

Samanta, Avik, Sabatino, Valerio, Ward, Thomas R., & Walther, Andreas. (2020). Functional and morphological adaptation in DNA protocells via signal processing prompted by artificial metalloenzymes. Nature Nanotechnology, 15(11), 914–921. https://doi.org/10.1038/s41565-020-0761-y

Serrano-Plana, Joan, Rumo, Corentin, Rebelein, Johannes G., Peterson, Ryan L., Barnet, Maxime, & Ward, Thomas R. (2020). Enantioselective Hydroxylation of Benzylic C(sp; 3; )-H Bonds by an Artificial Iron Hydroxylase Based on the Biotin-Streptavidin Technology. Journal of the American Chemical Society, 142(24), 10617–10623. https://doi.org/10.1021/jacs.0c02788

Klehr, Juliane, Zhao, Jingming, Kron, Amanda Santos, Ward, Thomas R., & Köhler, Valentin. (2020). Streptavidin (Sav)-Based Artificial Metalloenzymes: Cofactor Design Considerations and Large-Scale Expression of Host Protein Variants. In Iranzo O., Roque A. (Ed.), Peptide and Protein Engineering (pp. 213–235). Humana. https://doi.org/10.1007/978-1-0716-0720-6_12

Bartolami, Eline, Basagiannis, Dimitris, Zong, Lili, Martinent, Remi, Okamoto, Yasunori, Laurent, Quentin, Ward, Thomas R., Gonzalez-Gaitan, Marcos, Sakai, Naomi, & Matile, Stefan. (2019). Diselenolane-Mediated Cellular Uptake: Efficient Cytosolic Delivery of Probes, Peptides, Proteins, Artificial Metalloenzymes and Protein-Coated Quantum Dots. Chemistry - A European Journal, 25(16), 4047–4051. https://doi.org/10.1002/chem.201805900

Cheng, Yangyang, Zong, Lili, Lopez-Andarias, Javier, Bartolami, Eline, Okamoto, Yasunori, Ward, Thomas R., Sakai, Naomi, & Matile, Stefan. (2019). Cell-Penetrating Dynamic-Covalent Benzopolysulfane Networks. Angewandte Chemie International Edition, 58(28), 9522–9526. https://doi.org/10.1002/anie.201905003

Davis, Holly J., & Ward, Thomas R. (2019). Artificial Metalloenzymes: Challenges and Opportunities. ACS Central Science, 5(7), 1120–1136. https://doi.org/10.1021/acscentsci.9b00397

Guo, Xingwei, Okamoto, Yasunori, Schreier, Mirjam R., Ward, Thomas R., & Wenger, Oliver S. (2019). Reductive Amination and Enantioselective Amine Synthesis by Photoredox Catalysis. European Journal of Organic Chemistry. https://doi.org/10.1002/ejoc.201900777

Hartwig, John F., & Ward, Thomas R. (2019). New “Cats” in the House: Chemistry Meets Biology in Artificial Metalloenzymes and Repurposed Metalloenzymes. Accounts of Chemical Research, 52(5), 1145. https://doi.org/10.1021/acs.accounts.9b00154

Liang, Alexandria Deliz, Serrano-Plana, Joan, Peterson, Ryan L., & Ward, Thomas R. (2019). Artificial Metalloenzymes Based on the Biotin-Streptavidin Technology: Enzymatic Cascades and Directed Evolution. Accounts of Chemical Research, 52(3), 585–595. https://doi.org/10.1021/acs.accounts.8b00618

Rebelein, Johannes G., Cotelle, Yoann, Garabedian, Brett, & Ward, Thomas R. (2019). Chemical Optimization of Whole-Cell Transfer Hydrogenation Using Carbonic Anhydrase as Host Protein. ACS Catalysis, 9(5), 4173–4178. https://doi.org/10.1021/acscatal.9b01006

Sabatino, Valerio, Rebelein, Johannes G., & Ward, Thomas R. (2019). “Close-to-Release”: Spontaneous Bioorthogonal Uncaging Resulting from Ring-Closing Metathesis. Journal of the American Chemical Society, 141(43), 17048–17052. https://doi.org/10.1021/jacs.9b07193

Sabatino, Valerio, & Ward, Thomas R. (2019). Aqueous olefin metathesis: recent developments and applications. Beilstein Journal of Organic Chemistry, 15, 445–468. https://doi.org/10.3762/bjoc.15.39

Wu, Shuke, Zhou, Yi, Gerngross, Daniel, Jeschek, Markus, & Ward, Thomas R. (2019). Chemo-enzymatic cascades to produce cycloalkenes from bio-based resources. Nature Communications, 10(1), 5060. https://doi.org/10.1038/s41467-019-13071-y

Wu, Shuke, Zhou, Yi, Rebelein, Johannes G., Kuhn, Miriam, Mallin, Hendrik, Zhao, Jingming, Igareta, Nico V., & Ward, Thomas R. (2019). Breaking Symmetry: Engineering Single-Chain Dimeric Streptavidin as Host for Artificial Metalloenzymes. Journal of the American Chemical Society, 141(40), 15869–15878. https://doi.org/10.1021/jacs.9b06923

Christoffel, Fadri, & Ward, Thomas R. (2018). Palladium-Catalyzed Heck Cross-Coupling Reactions in Water: A Comprehensive Review. Catalysis Letters, 148(2), 489–511. https://doi.org/10.1007/s10562-017-2285-0

Guo, Xingwei, Okamoto, Yasunori, Schreier, Mirjam R., Ward, Thomas R., & Wenger, Oliver S. (2018). Enantioselective Synthesis of Amines by Combining Photoredox and Enzymatic Catalysis in a Cyclic Reaction Network. Chemical Science, 9, 5052–5056. https://doi.org/10.1039/c8sc01561a

Heinisch, Tillmann, Schwizer, Fabian, Garabedian, Brett, Csibra, Eszter, Jeschek, Markus, Vallapurackal, Jaicy, Pinheiro, Vitor B., Marlière, Philippe, Panke, Sven, & Ward, Thomas R. (2018). E. coli surface display of streptavidin for directed evolution of an allylic deallylase. Chemical Science, 9(24), 5383–5388. https://doi.org/10.1039/c8sc00484f

Hestericová, Martina, Heinisch, Tillman, Alonso-Cotchico, Lur, Maréchal, Jean-Didier, Vidossich, Pietro, & Ward, Thomas R. (2018). Directed Evolution of an Artificial Imine Reductase. Angewandte Chemie - International Edition, 57(7), 1863–1868. https://doi.org/10.1002/anie.201711016

Hestericova, Martina, Heinisch, Tillmann, Lenz, Markus, & Ward, Thomas R. (2018). Ferritin encapsulation of artificial metalloenzymes: engineering a tertiary coordination sphere for an artificial transfer hydrogenase. Dalton transactions, 47(32), 10837–10841. https://doi.org/10.1039/c8dt02224k

Jeschek, Markus, Panke, Sven, & Ward, Thomas R. (2018). Artificial Metalloenzymes on the Verge of New-to-Nature Metabolism. Trends in Biotechnology, 36(1), 60–72. https://doi.org/10.1016/j.tibtech.2017.10.003

Keller, Sascha G., Probst, Benjamin, Heinisch, Tillmann, Alberto, Roger, & Ward, Thomas R. (2018). Photo-Driven Hydrogen Evolution by an Artificial Hydrogenase Utilizing the Biotin-Streptavidin Technology. Helvetica Chimica Acta, 101(4), e1800036. https://doi.org/10.1002/hlca.201800036

Mallin, Hendrik, & Ward, Thomas R. (2018). Streptavidin-Enzyme Linked Aggregates for the One-Step Assembly and Purification of Enzyme Cascades. ChemCatChem, 10(13), 2810–2816. https://doi.org/10.1002/cctc.201800162

Mann, Samuel, Heinisch, Tillmann, Ward, Thomas R., & Borovik, A. S. (2018). Coordination chemistry within a protein host: regulation of the secondary coordination sphere. Chemical Communications, 54(35), 4413–4416. https://doi.org/10.1039/c8cc01931b

Okamoto, Yasunori, Kojima, Ryosuke, Schwizer, Fabian, Bartolami, Eline, Heinisch, Tillmann, Matile, Stefan, Fussenegger, Martin, & Ward, Thomas R. (2018). A cell-penetrating artificial metalloenzyme regulates a gene switch in a designer mammalian cell. Nature Communications, 9, 1943. https://doi.org/10.1038/s41467-018-04440-0

Pellizzoni, Michela M., Schwizer, Fabian, Wood, Christopher W., Sabatino, Valerio, Cotelle, Yoann, Matile, Stefan, Woolfson , Derek N., & Ward, Thomas R. (2018). Chimeric Streptavidins as Host Proteins for Artificial Metalloenzymes. ACS Catalysis, 8(2), 1476–1484. https://doi.org/10.1021/acscatal.7b03773

Rebelein, Johannes G., & Ward, Thomas R. (2018). In vivo catalyzed new-to-nature reactions. Current Opinion in Biotechnology, 53, 106–114. https://doi.org/10.1016/j.copbio.2017.12.008

Schwizer, Fabian, Okamoto, Yasunori, Heinisch, Tillmann, Gu, Yifan, Pellizzoni, Michela M., Lebrun, Vincent, Reuter, Raphael, Köhler, Valentin, Lewis, Jared C., & Ward, Thomas R. (2018). Artificial Metalloenzymes: Reaction Scope and Optimization Strategies. Chemical Reviews, 118(1), 142–231. https://doi.org/10.1021/acs.chemrev.7b00014

Szponarski, Mathieu, Schwizer, Fabian, Ward, Thomas R., & Gademann, Karl. (2018). On-cell catalysis by surface engineering of live cells with an artificial metalloenzyme. Communications Chemistry, 1(84), 1–10. https://doi.org/10.1038/s42004-018-0087-y

Zhao, Jingming, Bachmann, Daniel G., Lenz, Markus, Gillingham, Dennis G., & Ward, Thomas R. (2018). An artificial metalloenzyme for carbene transfer based on a biotinylated dirhodium anchored within streptavidin. Catalysis science & technology, 8(9), 2294–2298. https://doi.org/10.1039/c8cy00646f

Zhao, Jingming, Rebelein, Johannes G., Mallin, Hendrik, Trindler, Christian, Pellizzoni, Michela M., & Ward, Thomas R. (2018). Genetic Engineering of an Artificial Metalloenzyme for Transfer Hydrogenation of a Self-Immolative Substrate in Escherichia coli’s Periplasm. Journal of American Chemical Society, 140(41), 13171–13175. https://doi.org/10.1021/jacs.8b07189

Jeschek, Markus, Bahls, Maximilian O., Schneider, Veronika, Marlière, Philippe, Ward, Thomas R., & Panke, Sven. (2017). Biotin-independent strains of Escherichia coli for enhanced streptavidin production. Metabolic Engineering, 40, 33–40. https://doi.org/10.1016/j.ymben.2016.12.013

Keller, Sascha G., Pannwitz, Andrea, Mallin, Hendrik, Wenger, Oliver S., & Ward, Thomas R. (2017). Streptavidin as a Scaffold for Light-Induced Long-Lived Charge Separation. Chemistry - A European Journal, 23(71), 18019–18024. https://doi.org/10.1002/chem.201703885

Liu, Le, Cotelle, Yoann, Klehr, Juliane, Sakai, Naomi, Ward, Thomas R., & Matile, Stefan. (2017). Anion-ÏEuro catalysis: Bicyclic products with four contiguous stereogenic centers from otherwise elusive diastereospecific domino reactions on ÏEuro-acidic surfaces. Chemical Science, 8(5), 3770–3774. https://doi.org/10.1039/c7sc00525c

Mann, Samuel, Heinisch, Tillmann, Ward, Thomas R., & Borovik, A. S. (2017). Peroxide Activation Regulated by Hydrogen Bonds within Artificial Cu Proteins. Journal of the American Chemical Society, 139(48), 17289–17292. https://doi.org/10.1021/jacs.7b10452

Okamoto, Yasunori, & Ward, Thomas R. (2017). Cross-Regulation of an Artificial Metalloenzyme. Angewandte Chemie International Edition, 56(34), 10156–10160. https://doi.org/10.1002/anie.201702181

Okamoto, Yasunori, & Ward, Thomas R. (2017). Transfer Hydrogenation Catalyzed by Organometallic Complexes using NADH as Reductant in a Biochemical Context. Biochemistry, 56(40), 5223–5224. https://doi.org/10.1021/acs.biochem.7b00809

Seck, Charlotte, Mbaye, Diagne M., Coufourier, Sébastien, Lator, Alexis, Lohier, Jean-François, Poater, Albert, Ward, Thomas R., Gaillard, Sylvain, & Renaud, Jean-Luc. (2017). Alkylation of Ketones Catalyzed by Bifunctional Iron Complexes: From Mechanistic Understanding to Application. ChemCatChem, 9(23), 4410–4416. https://doi.org/10.1002/cctc.201701241

Okamoto, Yasunori, & Ward, Thomas R. (2017). Supramolecular Enzyme Mimics. In Atwood Ed., J. (Ed.), Comprehensive Supramolecular Chemistry II (II, Vol. 4, pp. 459–510). Elsevier. https://doi.org/10.1016/b978-0-12-409547-2.12551-x

Trindler, Christian, & Ward, Thomas R. (2017). Artificial Metalloenzymes. In Poli, Rinaldo (Ed.), Effects of Nanoconfinement on Catalysis: Vol. Fundamental and Applied Catalysis (pp. 49–82). Springer. https://doi.org/10.1007/978-3-319-50207-6_3

Chatterjee, Anamitra, Mallin, Hendrik, Klehr, Juliane, Vallapurackal, Jaicy, Finke, Aaron D., Vera, Laura, Marsh, May, & Ward, Thomas R. (2016). An Enantioselective Artificial Suzukiase Based on the Biotin-Streptavidin Technology. Chemical Science, 7(1), 673–677. https://doi.org/10.1039/c5sc03116h

Chatterjee, Anamitra, & Ward, Thomas R. (2016). Recent Advances in the Palladium Catalyzed Suzuki-Miyaura Cross-Coupling Reaction in Water. Catalysis Letters, 146(4), 820–840. https://doi.org/10.1007/s10562-016-1707-8

Cotelle, Yoann, Benz, Sebastian, Avestro, Alyssa-Jennifer, Ward, Thomas R., Sakai, Naomi, & Matile, Stefan. (2016). Anion-π Catalysis of Enolate Chemistry: Rigidified Leonard Turns as a General Tool to Run Reactions on Aromatic Surfaces. Angewandte Chemie International Edition, 55(13), 4275–4279. https://doi.org/10.1002/ange.201600831

Cotelle, Yoann, Chuard, Nicolas, Lascano, Santiago, Lebrun, Vincent, Wehlauch, Robin, Bohni, Nadine, Loercher, Samuel, Postupalenko, Viktoriia, Reddy, Sai T., Meier, Wolfgang, Palivan, Cornelia G., Gademann, Karl, Ward, Thomas R., & Matile, Stefan. (2016). Interfacing Functional Systems. Chimia, 70(6), 418–423. https://doi.org/10.2533/chimia.2016.418

Cotelle, Yoann, Lebrun, Vincent, Sakai, Naomi, Ward, Thomas R., & Matile, Stefan. (2016). Anion-π Enzymes. ACS Central Science, 2(6), 388–393. https://doi.org/10.1021/acscentsci.6b00097

Heinisch, Tillmann, & Ward, Thomas R. (2016). Artificial Metalloenzymes Based on the Biotin-Streptavidin Technology: Challenges and Opportunities. Accounts of Chemical Research, 49(9), 1711–1721. https://doi.org/10.1021/acs.accounts.6b00235

Hestericová, Martina, Correro, M Rita, Lenz, Markus, Corvini, Philippe F-X, Shahgaldian, Patrick, & Ward, Thomas R. (2016). Immobilization of an Artificial Imine Reductase within Silica Nanoparticles Improves its Performance. Chemical Communications, 52(60), 9462–9465. https://doi.org/10.1039/c6cc04604e

Hyster, Todd K., & Ward, Thomas R. (2016). Genetic Optimization of Metalloenzymes: Enhancing Enzymes for Non-Natural Reactions. Angewandte Chemie International Edition, 55(26), 7344–7357. https://doi.org/10.1002/anie.201508816

Jeschek, Markus, Panke, Sven, & Ward, Thomas R. (2016). Periplasmic Screening for Artificial Metalloenzymes. Methods in enzymology, 580, 539–556. https://doi.org/10.1016/bs.mie.2016.05.037

Jeschek, Markus, Reuter, Raphael, Heinisch, Tillmann, Trindler, Christian, Klehr, Juliane, Panke, Sven, & Ward, Thomas R. (2016). Directed evolution of artificial metalloenzymes for in vivo metathesis. Nature, 537(7622), 661–665. https://doi.org/10.1038/nature19114