Max Planck Research Group - Magnetische Resonanz Komplexer Materialien und Katalysatoren

Prof. Dr. Thomas Wiegand - Magnetische Resonanz Komplexer Materialien und Katalysatoren

Vita
Diploma Chemistry, Westfälische-Wilhelms Universität Münster, Germany (2010)
PhD Thesis Prof. Hellmut Eckert, Westfälische-Wilhelms Universität Münster, Germany/ Institute of Physical Chemistry (2010-2013)
PostDoc Prof. Hellmut Eckert, Westfälische-Wilhelms Universität Münster, Germany/ Institute of Physical Chemistry (2013-2014)
PostDoc Prof. Beat H. Meier, ETH Zürich, Switzerland/ Laboratory of Physical Chemistry (2014-2020)
Habilitation ETH Zürich, Switzerland/ Laboratory of Physical Chemistry (2019)
Venia Legendi ETH Zürich, Switzerland/ Laboratory of Physical Chemistry (2020)
Oberassistent/Privatdozent ETH Zürich, Switzerland/ Laboratory of Physical Chemistry (2020-2021)
Research Group Leader “Magnetic resonance of complex materials and catalysts”, MPI CEC (since 2021)
W2-Heisenberg-Professor  “Magnetic resonance of complex materials and catalysts”, MPI CEC/RWTH Aachen (since 2021)

 

Gruppenmitglieder

Laborkoordination

Dr. Riza Dervisoglu

PhD Studierende

Leeroy Hendrickx
Koen Linssen
Sven Moos
Publications

Full publications list​​​​​​​ | ORCID | Researcher ID / Publons

  • Silva, I. d. A., Bartalucci, E., Bolm, C.,  Wiegand, T. (2023). Opportunities and Challenges in Applying Solid-State NMR Spectroscopy in Organic Mechanochemistry. ADVANCED MATERIALS. doi:10.1002/adma.202304092.
  • Sodreau, A., Zahedi, H. G., Dervisoglu, R., Kang, L., Menten, J., Zenner, J., Terefenko, N., DeBeer, S., Wiegand, T., Bordet, A.,  Leitner, W. (2023). A Simple and Versatile Approach for the Low-Temperature Synthesis of Transition Metal Phosphide Nanoparticles from Metal Chloride Complexes and P(SiMe3)3. ADVANCED MATERIALS. 2306621 (1-9) doi:10.1002/adma.202306621.
  • Rout, S. K., Cadalbert, R., Schröder, N., Wang, J., Zehnder, J., Gampp, O., Wiegand, T., Güntert, P., Klingler, D., Kreutz, C., Knörlein, A., Hall, J., Greenwald, J.,  Riek, R. (2023). An Analysis of Nucleotide-Amyloid Interactions Reveals Selective Binding to Codon-Sized RNA. Journal of the American Chemical Society, 145(40), 21915-21924. doi:10.1021/jacs.3c06287.
  • Callon, M., Luder, D., Malär, A. A., Wiegand, T., Rimal, V., Lecoq, L., Böckmann, A., Samoson, A.,  Meier, B. H. (2023). High and fast: NMR protein-proton side-chain assignments at 160 kHz and 1.2 GHz. CHEMICAL SCIENCE, 14(39), 10824-10834. doi:10.1039/d3sc03539e.
  • Zhang, Y., El Sayed, S., Kang, L., Sanger, M., Wiegand, T., Jessop, P. G., DeBeer, S., Bordet, A., Leitner, W. (2023). Adaptive Catalysts for the Selective Hydrogenation of Bicyclic Heteroaromatics using Ruthenium Nanoparticles on a CO2-Responsive Support. Angewandte Chemie, International Edition in English, (XX): e202311427, pp. x-xx. doi:10.1002/anie.202311427.
  • Pfister, S., Rabl, J., Wiegand, T., Mattei, S., Malaer, A. A., Lecoq, L., Seitz, S., Bartenschlager, R., Boeckmann, A., Nassal, M., Boehringer, D., Meier, B. H. (2023). Structural conservation of HBV-like capsid proteins over hundreds of millions of years despite the shift from non-enveloped to enveloped life-style. Nature Communications, (14): 1574, pp. 1-15. doi:10.1038/s41467-023-37068-w.
  • Lipinski, W. P. P., Zehnder, J., Abbas, M., Güntert, P., Spruijt, E., Wiegand, T. (2023). Fibrils Emerging from Droplets: Molecular Guiding Principles behind Phase Transitions of a Short Peptide-Based Condensate Studied by Solid-State NMR. Chemistry – A European Journal,(29) e202301159, pp. 1-11. doi:10.1002/chem.202301159.
  • Bartalucci, E., Malär, A. A. A., Mehnert, A., Büning, J. B. K. B., Günzel, L., Icker, M., Börner, M., Wiebeler, C., Meier, B. H. H., Grimme, S., Kersting, B.,  Wiegand, T. (2023). Probing a Hydrogen-pi Interaction Involving a Trapped Water Molecule in the Solid State. Angewandte Chemie, International Edition in English, (62), 1-10,e2022177 . doi:10.1002/anie.202217725.
  • Bartalucci, E., Luder, D. J., Terefenko, N., Malär, A. A., Bolm, C., Ernst, M., Wiegand, T. (2023). The effect of methyl group rotation on H-1-H-1 solid-state NMR spin-diffusion spectra. Physical Chemistry Chemical Physics, (25), 19501-19511. doi:10.1039/d3cp02323k.
  • Bartalucci, E., Schumacher, C., Hendrickx, L., Puccetti, F., d'Anciaes Almeida Silva, I., Dervisoglu, R., Puttreddy, R., Bolm, C., Wiegand, T. (2023). Disentangling the Effect of Pressure and Mixing on a Mechanochemical Bromination Reaction by Solid-State NMR Spectroscopy. Chemistry – A European Journal, e202203466, pp. 1-12. doi:10.1002/chem.202203466.
  • Lacabanne, D., Wiegand, T., Di Cesare, M., Orelle, C., Ernst, M., Jault, J.-M., Meier, B. H., Boeckmann, A. (2022). Solid-State NMR Reveals Asymmetric ATP Hydrolysis in the Multidrug ABC Transporter BmrA. Journal of the American Chemical Society, 144(27), 12431-12442. doi:10.1021/jacs.2c04287.
  • Malär, A. A., Sun, Q., Zehnder, J., Kehr, G., Erker, G.,  Wiegand, T. (2022). Proton-phosphorous connectivities revealed by high-resolution proton-detected solid-state NMR. Physical Chemistry Chemical Physics, 24(13), 7768-7778. doi:10.1039/d2cp00616b.
  • Zehnder, J.; Cadalbert, R.; Yulikov, M.; Künze, G.; Wiegand, T. (2021) Paramagnetic spin labeling of a bacterial DnaB helicase for solid-state NMR, J. Magn. Reson., 332, 107075, DOI:10.1016/j.jmr.2021.107075
  • Malär, A.A., Wili, N., Völker, L.A., Kozlova, M.I., Cadalbert, R., Däpp, A., Weber, M. E., Zehnder, J. ,  Jeschke, G. , Eckert, H. , Böckmann, A. , Klose, D. , Mulkidjanian, A.Y., Meier, B.H. , Wiegand, T. (2021) Spectroscopic glimpses of the transition state of ATP hydrolysis trapped in a bacterial DnaB helicase, Nat. Commun., 12, 5293 doi.org/10.1038/s41467-021-25599-z
  • Chávez, M., Wiegand, T., Malär, A. A., Meier, B. H. , Ernst, M.(2021) Residual Linewidth in Magic-Angle Spinning Proton Solid-State NMR, Magnetic Resonance, 2, 499-509. doi.org/10.5194/mr-2-499-2021
  • Callon, M., Malär, A.A., Pfister, S., Rimal, V., Weber, M. E., Wiegand, T., Zehnder, J., Chavez, M., Deb, R., Däpp, A., Cadalbert, R., Fogeron, M.-L., Zyla, D., Hunkeler, A., Lecoq, L., Torosyan, A., Wang, S., Jonas, S., Glockshuber, R., Ernst, M., Böckmann, A., Meier, B.H. (2021) Biomolecular solid-state NMR spectroscopy at 1200 MHz: the gain in resolution, J. Biomol. NMR, 75, 255-272. doi.org/10.1007/s10858-021-00373-x
  • Malär, A.A,, Völker, L.A.,Cadalbert, R.,  Ernst, M., Böckmann,A, Meier,B.H., Wiegand,T. (2021) Temperature-dependent solid-state NMR proton chemical-shift values and hydrogen bonding, J. Phys. Chem. B, 2021, 125, 6222-6230 doi/pdf/10.1021/acs.jpcb.1c04061
  • Zehnder, J., Cadalbert, R., Terradot, L., Ernst, M., Böckmann, A., Güntert, P., Meier, B.H., Wiegand, T. (2021) Paramagnetic solid-state NMR to localize the metal-ion cofactor in an oligomeric DnaB helicase, Chemistry 27, 7745-7755 doi.org/10.1002/chem.202100462
  • Lecoq, L., Wang, S., Dujardin, M., Zimmermann, P., Schuster, L., Fogeron, M.-L, Briday, M., Schledorn, M., Wiegand, T., Cole, A.L, Montserrat, R., Bressanelli, S., Meier, B.H., Nassal, M., Böckmann A. (2021) A pocket-factor-triggered conformational switch in the hepatitis B virus capsid, PNAS, 118, e2022464118. doi.org/10.1073/pnas.2022464118
  • Kumari, P. , Gosh, D. , Vanas, A. ,. Fleischmann, Y, Wiegand, T. , Jeschke, G. , Riek, R. Eichmann, C.(2021) Structural Insights into α-Synuclein Monomer-Fibril Interactions, PNAS, 118, e2012171118. doi: 10.1073/pnas.2012171118
  • Lacabanne, D.; Boudet, J.; Malär, A. A. ; Wu, P. ; Cadalbert, R. ; Salmon, L.; Allain, F. H.-T. ; Meier, B. H.; Wiegand, T. (2020) Protein side-chain-DNA contacts probed by fast magic-angle spinning NMR. J. Phys. Chem. B (124) 11089-11097 doi.org/10.1021/acs.jpcb.0c08150
  • Wiegand, T.; Malär, A. A.; Cadalbert, R.; Ernst, M.; Böckmann, A.; Meier, B.H. (2020) Asparagine and glutamine side-chains and ladders in HET-s(218-289) amyloid fibrils studied by fast magic-angle spinning NMR. Frontiers Mol. Biosc.(7) 582033 doi.org/10.3389/fmolb.2020.582033
  • Wiegand, T.; Lacabanne, D.; Torosyan, A.; Boudet, J.; Cadalbert, R.; Allain, F. H.-T. ; Meier, B. H.; Böckmann, A. (2020) Sedimentation yields long-term stable protein samples as shown by solid-state NMR. Frontiers Mol. Biosc. (7) 17 DOI: 10.3389/fmolb.2020.00017
  • Wiegand, T.; Schledorn, M.; Malär, A. A. R. Cadalbert, R.; Däpp, A.; Terradot, L.; Meier, B. H.; Böckmann, A. (2020)  Nucleotide binding modes in a motor protein revealed by 31P- and 1H-detected MAS solid-state NMR . ChemBioChem (21) 324-330  DOI: 10.1002/cbic.201900439
  • Torosyan, A; , Wiegand.T ; Schledorn, M.; Klose, D.; Güntert, P.; Böckmann, A.; Meier, B. H. (2019) Including protons in solid-state NMR resonance assignment and secondary structure analysis: The example of RNA polymerase II subunits Rpo4/7. Frontiers Mol. Biosc. (6) 100. doi.org/10.3389/fmolb.2019.00100
  • Malär, A. A.; Smith-Penzel, S.; Camenisch, G.-M. ; Wiegand, T.; Samoson, A.; Böckmann, A.; Ernst, M.; Meier, B. H. (2019) Quantifying NMR Coherent Proton Linewidth in Proteins Under Fast MAS Conditions: A Second Moment Approach, PhysChemChemPhys (21) 18850-18865 doi: 10.1039/c9cp03414e
  • Lacabanne, D.; Orelle, C.; Lecoq, L.; Kunert, B. ; Chuilon, C. ; Wiegand, T.; Ravaud, S.; Jault, J.-M. ; Meier, B. H.; Böckmann, A. (2019) Flexible-to-rigid transition is central for substrate transport in the ABC transporter BmrA from Bacillus subtilis, Commun. Biol. (2) 1-9 doi.org/10.1038/s42003-019-0390-x |
  • Malär, A. A.; Dong, S.; Kehr, G.; Erker, G.; Meier, B. H.; Wiegand T. (2019) Characterization of H2-splitting products of Frustrated Lewis Pairs: Benefit of fast magic-angle spinning. ChemPhysChem, (20) 672-679 doi.org/10.1002/cphc.201900006
  • Wiegand T. ; Cadalbert, R.; Lacabanne, D.;  Timmins, J. ; Terradot, L. ; Böckmann, A.; Meier, B. H. (2019) The conformational changes coupling ATP hydrolysis and translocation in a bacterial DnaB helicase. Nat. Commun. (10) 31 doi:10.1038/s41467-018-07968-3
  • Boudet, J.; Devillier, J.-C. ; Wiegand T.; Salmon, L.; Meier, B. H.; Lipps, G.; Allain, F. H.-T. (2019) A small helical bundle prepares primer synthesis by binding two ATP nucleotides that enhance sequence-specific recognition of the DNA template. Cell, (176) 154-166. doi.org/10.1016/j.cell.2018.11.031

Magnetic resonance of complex materials and catalysts

Molecular-recognition events in biological and chemical sciences probed by solid-state NMR spectroscopy in the Wiegand laboratory. Copyright: AK Wiegand

The Wiegand research group develops and applies Nuclear Magnetic Resonance (NMR) spectroscopy techniques to probe weak chemical interactions in solid-state molecular recognition processes. Molecular recognition plays a fundamental role in many disciplines of life sciences and is essential in biology and chemistry. It is driven by the cooperative interplay of noncovalent interactions (NCIs), such as hydrogen bonds, dispersion or cation-π interactions. Solid-state NMR allows us to shed light on the atomic-level details of molecular recognition in rather diverse fields of biological and chemical sciences. We currently focus in collaboration with our partners on four selected research topics, namely mechanochemically-induced organic reactions, multifunctional heterogeneous catalysts, cellular organization by phase separation and protein-nucleotide binding in ATPases. Our research themes require the continuous further development of the solid-state NMR methodology in concert with computational modelling, particularly focussing on proton-detected solid-state NMR at magic-angle spinning (MAS) frequencies of 100 kHz or even higher as well as paramagnetic NMR spectroscopy in solids.

Probing NCIs by solid-state NMR. The group develops a set of dedicated proton-detected solid-state NMR experiments enabling the detection and quantification of NCIs.[1] Until recently, however, proton-detected solid-state NMR spectra often used to be uninformative due to lack of resolution. However, with the significant line-narrowing achieved with the advent of fast MAS techniques (MAS frequencies larger than 100 kHz) the protons engaged in various types of NCIs can be resolved and identified. We interpret our experimental results in feedback with quantum-chemical calculations on how NMR observables are influenced by NCIs. Current examples comprise lanthanide-π containers that trap small guest molecules.[2]

Probing a hydrogen-π interaction involving a trapped water molecule in a lanthanide-π container by solid-state NMR spectroscopy.[2] Copyright: AK Wiegand

Organic mechanochemistry. Solid-state molecular recognition in mechanochemically-induced organic reactions is a central research topic in the group. Spectroscopic techniques are crucial for shedding light on the mechanisms of such reactions and solid-state NMR offers a variety of opportunities in this research field (for a recent review see [3]). We currently focus on the mechanochemical racemic-phase formation of chiral organic molecules, as well as amino acids.[4] The technique of resonant-acoustic mixing as an alternative tool is further explored in our laboratory.[5] Mechanistically, we explore solid-state NMR to disentangle the various effects affecting mechanochemical reactions.[6] A current application aims at combining the concepts of mechanochemistry and Frustrated Lewis Pair chemistry. Novel insight into mechanochemical reactions is often combined with using the target compounds for NMR methodological work (for recent examples see [7-8]). 

Disentangling various effects occurring during mechanochemical reactions by solid-state NMR spectroscopy focussing on solid-state molecular-recognition processes. Copyright: AK Wiegand

Multifunctional catalysts. We investigate among others supported ionic-liquid phases involving metal(phosphide) nanoparticles. A particular focus lies on probing the conformation of ionic liquids (IL) on such surfaces and to explore the roles of ordering phenomena as well as IL dynamics in catalytic processes. We are establishing homonuclear distance measurements for catalytic materials in the fast MAS regime, particularly for those materials possessing a large chemical-shift anisotropy impairing with accurate distance measurements. In addition, we apply proton-detected solid-state NMR experiments at MAS frequencies >100 kHz using adiabatic pulse schemes to characterize paramagnetic lanthanide complexes, which for instance allows us to probe magnetic susceptibility tensors in the solid state. 

Solid-state NMR to probe ordering phenomena and formic acid stabilization on SILP surfaces. Copyright: AK Wiegand

Cellular organization by phase separation. A central molecular-recognition event the group is focussing on is liquid-liquid phase separation and subsequent liquid-to-solid phase transition of proteins linked with neurodegenerative diseases. Real-time solid-state NMR allowed us to monitor liquid-droplet maturation of the Fused in Sarcoma protein and to follow amyloid fibril formation.[9] Small peptide derivatives designed based on the “sticker-and-spacer” concept have been studied as model systems.[10] 

Figure: Liquid droplet formation and maturation followed by NMR spectroscopy. Copyright: AK Wiegand

ATP-hydrolysis in ATPases. The group explores solid-state NMR spectroscopy to monitor ATP-hydrolysis in various ATPases, in many cases by real-time NMR spectroscopy focussing on the detection of the nucleotide. A particular focus lies on studying protein-nucleotide interactions, e.g. by probing hydrogen bonds. Our current protein systems range from proteins involved in DNA replication[11-12]  to ATPases of relevance in the biogenesis of iron-sulphur clusters. 

Figure: ATP-hydrolysis in SmsCB studied by solid-state NMR. Copyright: AK Wiegand

National and international collaboration partners (selection): Prof. Dr. F. H.-T. Allain (ETH Zürich, Switzerland), Prof. Dr. S. DeBeer (MPI CEC, Germany), Prof. Dr. C. Bolm (RWTH Aachen University, Germany), Dr. Bordet (MPI CEC, Germany), Prof. Dr. M. Ernst (ETH Zürich, Switzerland), Prof. Dr. M. Fyta (RWTH Aachen University), Prof. Dr. B. Kersting (Leipzig University, Germany), Prof. Dr. W. Leitner (MPI CEC, Germany) and Dr. E. Spruijt (Radboud University, Netherlands).

Selected references:

[1] N. Schröder, E. Bartalucci, T. Wiegand, Chemphyschem 2024, 25, e202400537.

[2] E. Bartalucci, A. A. Malär, A. Mehnert, J. B. Kleine Büning, L. Günzel, M. Icker, M. Börner, C. Wiebeler, B. H. Meier, S. Grimme, B. Kersting, T. Wiegand, Angew. Chem. Int. Ed. Engl. 2023, 62, e202217725.

[3] I. D. A. Silva, E. Bartalucci, C. Bolm, T. Wiegand, Adv. Mater. 2023, 35, e2304092.

[4] C. Quaranta, I. d'Anciães Almeida Silva, S. Moos, E. Bartalucci, L. Hendrickx, B. M. D. Fahl, C. Pasqualini, F. Puccetti, M. Zobel, C. Bolm, T. Wiegand, Angew. Chem. Int. Ed. 2024, 63, e202410801.

[5] L. Hendrickx, C. Quaranta, E. Fuchs, M. Plekhanov, M. Zobel, C. Bolm, T. Wiegand, Molecules 2025, 30, 3745.

[6] E. Bartalucci, C. Schumacher, L. Hendrickx, F. Puccetti, I. d'Anciaes Almeida Silva, R. Dervisoglu, R. Puttreddy, C. Bolm, T. Wiegand, Chem. Eur. J. 2023, 29, e202203466.

[7] E. Bartalucci, C. Quaranta, F. Manzoni, I. D. A. Silva, M. Zobel, C. Bolm, M. Ernst, T. Wiegand, Phys. Chem. Chem. Phys. 2025, 27, 5995-6004.

[8] E. Bartalucci, D. J. Luder, N. Terefenko, A. A. Malär, C. Bolm, M. Ernst, T. Wiegand, Phys. Chem. Chem. Phys. 2023, 25, 19501-19511.

[9 L. Emmanouilidis, E. Bartalucci, Y. Kan, M. Ijavi, M. E. Perez, P. Afanasyev, D. Boehringer, J. Zehnder, S. H. Parekh, M. Bonn, T. C. T. Michaels, T. Wiegand, F. H. Allain, Nat. Chem. Biol. 2024, 20, 1044-1052.

[10] W. P. Lipinski, J. Zehnder, M. Abbas, P. Güntert, E. Spruijt, T. Wiegand, Chem. Eur. J. 2023, 29, e202301159.

[11] A. A. Malär, N. Wili, L. A. Völker, M. I. Kozlova, R. Cadalbert, A. Däpp, M. E. Weber, J. Zehnder, G. Jeschke, H. Eckert, A. Böckmann, D. Klose, A. Y. Mulkidjanian, B. H. Meier, T. Wiegand, Nat. Commun. 2021, 12, 5293.

[12] P. Wu, J. Zehnder, N. Schröder, P. E. W. Blümmel, L. Salmon, F. F. Damberger, G. Lipps, F. H. T. Allain, T. Wiegand, J. Am. Chem. Soc. 2024, 146, 9583-9596.