Researcher Portfolio
Kahnt, Jörg
Core Facility Mass Spectrometry and Proteomics, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society
Researcher Profile
Position: Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society
Position: Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society
Position: Core Facility Mass Spectrometry and Proteomics, Max Planck Institute for Terrestrial Microbiology, Max Planck Society
Researcher ID: https://pure.mpg.de/cone/persons/resource/persons254414
Publications
(1 - 25 of 89)
: Yilmaz, S., Kanis, B., Hogers, R. A., Benito-Vaquerizo, S., Kahnt, J., Glatter, T., Dronsella, B., Erb, T. J., Suarez-Diez, M., & Claassens, N. J. (2025). System-level characterization of engineered and evolved formatotrophic E. coli strains. Synthetic and Systems Biotechnology. doi:10.1016/j.synbio.2025.03.001. [PubMan] : He, H., Gómez-Coronado, P. A., Zarzycki, J., Barthel, S., Kahnt, J., Claus, P., Klein, M., Klose, M., de Crécy-Lagard, V., Schindler, D., Paczia, N., Glatter, T., & Erb, T. J. (2024). Adaptive laboratory evolution recruits the promiscuity of succinate semialdehyde dehydrogenase to repair different metabolic deficiencies. Nature Communications, 15(1): 8898. doi:10.1038/s41467-024-53156-x. [PubMan] : Gemmecker, Y., Winiarska, A., Hege, D., Kahnt, J., Seubert, A., Szaleniec, M., & Heider, J. (2024). A pH-dependent shift of redox cofactor specificity in a benzyl alcohol dehydrogenase of aromatoleum aromaticum EbN1. Applied Microbiology and Biotechnology, 108: 410. doi:10.1007/s00253-024-13225-z. [PubMan] : Aziz, I., Kayastha, K., Kaltwasser, S., Vonck, J., Welsch, S., Murphy, B. J., Kahnt, J., Wu, D., Wagner, T., Shima, S., & Ermler, U. (2024). Structural and mechanistic basis of the central energy-converting methyltransferase complex of methanogenesis. Proceedings of the National Academy of Sciences of the United States of America, 121(14): e2315568121. doi:10.1073/pnas.2315568121. [PubMan] : Nomura, S., Paczia, N., Kahnt, J., & Shima, S. (2024). Isolation of an H2-dependent electron-bifurcating CO2-reducing megacomplex with MvhB polyferredoxin from Methanothermobacter marburgensis. The FEBS Journal, 291(11), 2449-2460. doi:10.1111/febs.17115. [PubMan] : Wimmi, S., Balinovic, A., Brianceau, C. F., Pintor, K. L., Vielhauer, J., Turkowyd, B., Helbig, C., Fleck, M., Langenfeld, K., Kahnt, J., Glatter, T., Endesfelder, U., & Diepold, A. (2024). Cytosolic sorting platform complexes shuttle type III secretion system effectors to the injectisome in Yersinia enterocolitica. Nature Microbiology, 9, 185-199. doi:10.1038/s41564-023-01545-1. [PubMan] : Han, W., Meißner, E.-M., Neunteibl, S., Gunther, M., Kahnt, J., Dolga, A., Xie, C., Plesnila, N., Zhu, C., Blomgren, K., & Culmsee, C. (2023). Dying transplanted neural stem cells mediate survival bystander effects in the injured brain. Cell Death and Disease, 14(3): 173. doi:10.1038/s41419-023-05698-z. [PubMan] : Dinarieva, T. Y., Klimko, A. I., Kahnt, J., Cherdyntseva, T. A., & Netrusov, A. I. (2023). Adaptation of Lacticaseibacillus rhamnosus CM MSU 529 to aerobic growth: A proteomic approach. Microorganisms, 11(2): 313. doi:10.3390/microorganisms11020313. [PubMan] : Arriaza-Gallardo, F. J., Schaupp, S., Zheng, Y.-C., Abdul-Halim, M. F., Hui-Jie, P., Kahnt, J., Angelidou, G., Paczia, N., Hu, X., Costa, K., & Shima, S. (2022). The function of two radical-SAM enzymes, HcgA and HcgG, in the biosynthesis of the [Fe]-hydrogenase cofactor. Angewandte Chemie, International Edition in English, 61(50): e202213239. doi:10.1002/anie.202213239. [PubMan] : Khera, R., Mehdipour, A. R., Bolla, J. R., Kahnt, J., Welsch, S., Ermler, U., Münke, C., Robinson, C. V., Hummer, G., Xie, H., & Michel, H. (2022). Cryo-EM structures of pentameric autoinducer-2 exporter from Escherichia coli reveal its transport mechanism. The EMBO Journal, e109990. doi:10.15252/embj.2021109990. [PubMan] : Schaupp, S., Arriaza Gallardo, F. J., Pan, H. J., Kahnt, J., Angelidou, G., Paczia, N., Costa, K., Hu, X., & Shima, S. (2022). In vitro biosynthesis of the [Fe]-hydrogenase cofactor verifies the proposed biosynthetic precursors. Angewandte Chemie, International Edition in English, 61(22): e202200994. doi:10.1002/anie.202200994. [PubMan] : Lemaire, O. N., Müller, M.-C., Kahnt, J., & Wagner, T. (2021). Structural rearrangements of a dodecameric ketol-acid reductoisomerase isolated from a marine thermophilic methanogen. Biomolecules, 11(11): 1679. doi:10.3390/biom11111679. [PubMan] : Krink, N., Löchner, A., Anders, A., Kahnt, J., Rensing, S., Hochberg, G. K. A., & Sourjik, V. (2021). Construction of multicellular yeast networks using the communication toolkit with variable specificity and attenuation. bioRxiv: the preprint server for biology, 2021.09.27.462023. [PubMan] : Hahn, C. J., Lemaire, O. N., Kahnt, J., Engilberge, S., Wegener, G., & Wagner, T. (2021). Crystal structure of a key enzyme for anaerobic ethane activation. Science, 373(6550), 118-121. doi:10.1126/science.abg1765. [PubMan] : Watanabe, T., Pfeil-Gardiner, O., Kahnt, J., Koch, J., Shima, S., & Murphy, B. J. (2021). Three-megadalton complex of methanogenic electron-bifurcating and CO2-fixing enzymes. Science, 373(6559), 1151-1155. doi:10.1126/science.abg5550. [PubMan] : Teteneva, N. A., Mart'yanov V, S., Esteban Lopéz, M., Kahnt, J., Glatter, T., Netrusov I, A., Plakunov, V. K., & Sourjik, V. (2020). Multiple Drug-Induced Stress Responses Inhibit Formation of Escherichia coli Biofilms. APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 86(21): e01113-20. doi:10.1128/AEM.01113-20. [PubMan] : Dell'Aquila, G., Zauner, S., Heimerl, T., Kahnt, J., Samel-Gondesen, V., Runge, S., Hempel, F., & Maier, U. G. (2020). Mobilization and Cellular Distribution of Phosphate in the DiatomPhaeodactylum tricornutum. FRONTIERS IN PLANT SCIENCE, 11: 579. doi:10.3389/fpls.2020.00579. [PubMan] : Stehlik, T., Kremp, M., Kahnt, J., Boelker, M., & Freitag, J. (2020). Peroxisomal targeting of a protein phosphatase type 2C via mitochondrial transit. NATURE COMMUNICATIONS, 11(1). doi:10.1038/s41467-020-16146-3. [PubMan] : Dell’Aquila, G., Zauner, S., Heimerl, T., Kahnt, J., Samel-Gondesen, V., Runge, S., Hempel, F., & Maier, U. G. (2020). Mobilization and Cellular Distribution of Phosphate in the Diatom Phaeodactylum tricornutum. Frontiers in Plant Science. doi:10.3389/fpls.2020.00579. [PubMan] : Schmitt, G., Saft, M., Arndt, F., Kahnt, J., & Heider, J. (2019). Two Different Quinohemoprotein Amine Dehydrogenases Initiate Anaerobic Degradation of Aromatic Amines in Aromatoleum aromaticum EbN1. JOURNAL OF BACTERIOLOGY, 201(16): e00281. doi:10.1128/JB.00281-19. [PubMan] : Watanabe, T., Wagner, T., Huang, G., Kahnt, J., Ataka, K., Ermler, U., & Shima, S. (2019). The Bacterial [Fe]‐Hydrogenase Paralog HmdII Uses Tetrahydrofolate Derivatives as Substrates. Angewandte Chemie International Edition in English, 58(11), 3506-3510. doi:10.1002/anie.201813465. [PubMan] : Pauls, D., Hamarat, Y., Trufasu, L., Schendzielorz, T. M., Gramlich, G., Kahnt, J., Vanselow, J. T., Schlosser, A., & Wegener, C. (2019). Drosophila carboxypeptidase D (SILVER) is a key enzyme in neuropeptide processing required to maintain locomotor activity levels and survival rate. EUROPEAN JOURNAL OF NEUROSCIENCE, 50(9), 3502-3519. doi:10.1111/ejn.14516. [PubMan] : Arndt, F., Schmitt, G., Winiarska, A., Saft, M., Seubert, A., Kahnt, J., & Heider, J. (2019). Characterization of an Aldehyde Oxidoreductase From the Mesophilic Bacterium Aromatoleum aromaticum EbN1, a Member of a New Subfamily of Tungsten-Containing Enzymes. FRONTIERS IN MICROBIOLOGY, 10: 71. doi:10.3389/fmicb.2019.00071. [PubMan] : Berhardsgrütter, I., Vögeli, B., Wagner, T., Peter, D., Cortina, N. S., Kahnt, J., Bange, G., Engilberge, S., Girard, E., Riobe, F., Maury, O., Shima, S., Zarzycki, J., & Erb, T. J. (2018). The multicatalytic compartment of propionyl-CoA synthase sequesters a toxic metabolite. NATURE CHEMICAL BIOLOGY, 14(12), 1127. doi:10.1038/s41589-018-0153-x. [PubMan] : Ma, L., Wang, L., Trippel, C., Mendoza-Mendoza, A., Ullmann, S., Moretti, M., Carsten, A., Kahnt, J., Reissmann, S., Zechmann, B., Bange, G., & Kahmann, R. (2018). The Ustilago maydis repetitive effector Rsp3 blocks the antifungal activity of mannose-binding maize proteins. NATURE COMMUNICATIONS, 9: 1711. doi:10.1038/s41467-018-04149-0. [PubMan]