Dr. Christina Römelt - Computational Chemistry & Chemical Synthesis
- Dr. Christina Römelt
- Group leader
- Computational Chemistry & Chemical Synthesis
- Inorganic Spectroscopy
- +49 (0)208 306 - 3694
- christina.roemelt(at)cec.mpg.de
- Room: 512
Vita
| Studies (Chemistry) | University of Bonn (2003-2008) |
| Diploma (organic Chemistry) | University of Bonn (2008) |
| Dr. rer. nat. (organic Chemistry) | University of Bonn (2008-2010), University of Mainz (2010-2013) |
| Research project | Novartis, Basel (2013) |
| Scientific staff | MPI CEC (2014-2017) |
| Group leader | Computational Chemistry & Chemical Synthesis, MPI CEC (since 2017) |
Publications
Full publications list | ORCID
Selected MPI CEC publications
- Roemelt, C., Peredkov, S., Neese, F., Roemelt, M. and DeBeer, S. (2024). Valence-to-core X-ray emission spectroscopy of transition metal tetrahalides: mechanisms governing intensities. Phys. Chem. Chem. Phys. 26, 19960-19975. Doi: https://doi.org/10.1039/D4CP00967C
- Tarrago, M., Römelt, C., Nehrkorn, J., Schnegg, A., Neese, F., Bill, E., Ye, S. (2021). Experimental and Theoretical Evidence for an Unusual Almost Triply Degenerate Electronic Ground State of Ferrous Tetraphenylporphyrin. Inorganic chemistry. doi:10.1021/acs.inorgchem.1c00031.
- Berkefeld, A., Roemelt, M., Römelt, C., Schubert, H., Jeschke, G. (2020). Modulating Effect of Ligand Charge on the Electronic Properties of 2Ni–2S Structures and Implications for Biological 2M–2S Sites Inorganic Chemistry 59(23),17234–17243. https://doi.org/10.1021/acs.inorgchem.0c02467
- Römelt, C., Weyhermüller, T., Wieghardt, K. (2019). Structural characteristics of redox-active pyridine-1,6-diimine complexes: Electronic structures and ligand oxidation levels Coordination Chemistry Reviews 380, 287-317. https://doi.org/10.1016/j.ccr.2018.09.018
- Wang, M., Römelt, C., Weyhermüller, T., Wieghardt, K. (2019). Coordination Modes, Oxidation, and Protonation Levels of 2,6-Pyridinediimine and 2,2′:6′,2′́-Terpyridine Ligands in New Complexes of Cobalt, Zirconium, and Ruthenium. An Experimental and Density Functional Theory Computational Study Inorganic Chemistry 58(1), 121 132. https://doi.org/10.1021/acs.inorgchem.8b01949
- Römelt, C., Ye, S., Bill, E., Weyhermuller, T., van Gastel, M., Neese, F. (2018). Electronic Structure and Spin Multiplicity of Iron Tetraphenylporphyrins in Their Reduced States as Determined by a Combination of Resonance Raman Spectroscopy and Quantum Chemistry Inorganic Chemistry 57(4), 2141-2148. https://doi.org/10.1021/acs.inorgchem.7b03018
- Römelt, C., Song, J.S., Tarrago, M., Rees, J.A., van Gastel, M., Weyhermüller, T., DeBeer, S., Bill, E., Neese, F., Ye, S. (2017). Electronic Structure of a Formal Iron(0), Porphyrin Complex Relevant to CO2 Reduction Inorganic Chemistry 56(8), 4745-4750. https://doi.org/10.1021/acs.inorgchem.7b00401
Computational Chemistry & Chemical Synthesis
Quantum mechanics / molecular mechanics investigation of nitrogenase
Within the field of computational chemistry, our research group focuses on the calculation of electronic structures and spectroscopic properties of transition metal species. Our main project, in collaboration with the Sengupta group, is centered around the iron protein of the nitrogenase enzyme.
Nitrogenase is known to very efficiently catalyze the conversion of dinitrogen into ammonia, whereas the full catalytic cycle has yet not been completely understood. The iron protein (FeP) of nitrogenase is known to initiate the catalytic cycle of the nitrogenase active site via bonding interactions and electron transfer reactions from its [4Fe4S]n+ cluster and the associated ADP-ATP binding / ATP hydrolysis. FeP has been isolated without bound nucleotides as well as with one or two ADP/ATP bound, respectively. By investigating the influence of the nature of the bound nucleotide (induced geometric and electronic changes within the protein as a function of the nucleotide) as well as oxidation and spin state of the [4Fe4S] cluster on the spectral properties of the FeP (XAS, NRVS, Mössbauer), we hope to shed light on the steps which precede the initial electron transfer to the nitrogenase active site.
In addition to the iron protein, qm/mm computational studies on the Fe-only nitrogenases are topic of our future research, where the aim of this project is to unravel the reaction mechanism and identify intermediates of the catalytic cycle of the active site cofactor during CO2 reduction.
Electronic structure and spectroscopy of transition metal complexes
In collaboration with external experimental research groups as well as internal groups, our group uses computational chemistry (DFT and higher level theory) to investigate the electronic structures and spectroscopic properties of transition metal complexes. By providing insight into ground state electronic configurations as well as proposed intermediates and their respective spectroscopic properties (XAS, XES, (Resonance)-Raman, Mössbauer..) we aim to support our research collaborators in elucidating catalytic cycles and their active species.
Recently, our study on X-ray emission spectroscopy[2] of transition metal halides gave insight into trends and intensity mechanisms which govern the valence-to-core features of transition metal halides, providing a guideline on how to identify the factors which dictate the observed intensity trends.
Chemical Synthesis
Fe(IV)oxo complexes have previously been synthesized in our group[1] and investigated regarding their spin state behavior using resonant inelastic x-ray scattering experiments. These complexes will further be used for time resolved x-ray experiments. Thus, preparation and purification of this class of compounds in large amounts has been the main focus of the synthetic staff of our group. For future synthesis projects, close collaboration with the Gomez Castillo group is envisioned, frequently providing transition metal complexes to be investigated via time resolved spectroscopy.