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Redox potentials elucidate the electron transfer pathway of NAD+-dependent formate dehydrogenases,
B. R. Duffus, M. Gauglitz, C. Teutloff, S. Leimkühler,
Journal of Inorganic Biochemistry
2024,
253,
112487–0,
10.1016/j.jinorgbio.2024.112487
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Coupling of the Catalytic Reactions of Formate Dehydrogenase and Hydrogenase in Solution: Insights from in situ IR Spectroscopy and Computations,
A. F. T. Waffo, M. Wu‐Lu, S. Katz, S. Frielingsdorf, B. R. Duffus, J. Liedtke, S. Leimkühler, O. Lenz, K. Laun, M. A. Mroginski, I. Zebger,
ChemCatChem
2024,
10.1002/cctc.202400794
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Discovery of the Lanthipeptide Curvocidin and Structural Insights into its Trifunctional Synthetase CuvL,
A. Sigurdsson, B. M. Martins, S. A. Düttmann, M. Jasyk, B. Dimos‐Röhl, F. Schöpf, M. Gemander, C. H. Knittel, R. Schnegotzki, B. Schmid, S. Kosol, L. Pommerening, M. Gonzáles‐Viegaz, M. Seidel, M. Hügelland, S. Leimkühler, H. Dobbek, A. Mainz, R. D. Süssmuth,
Angewandte Chemie International Edition
2023,
62,
1–11,
10.1002/anie.202302490
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Changing the Electron Acceptor Specificity of Rhodobacter capsulatus Formate Dehydrogenase from NAD+ to NADP+,
H. Kumar, S. Leimkühler,
International Journal of Molecular Sciences
2023,
24,
16067–0,
10.3390/ijms242216067
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Metal-Containing Formate Dehydrogenases, a Personal View,
S. Leimkühler,
Molecules
2023,
28,
5338–0,
10.3390/molecules28145338
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The Mechanism of Metal-Containing Formate Dehydrogenases Revisited: The Formation of Bicarbonate as Product Intermediate Provides Evidence for an Oxygen Atom Transfer Mechanism,
H. Kumar, M. Khosraneh, S. S. M. Bandaru, C. Schulzke, S. Leimkühler,
Molecules
2023,
28,
1537–0,
10.3390/molecules28041537
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Infrared Spectroscopy Elucidates the Inhibitor Binding Sites in a Metal‐Dependent Formate Dehydrogenase,
K. Laun, B. R. Duffus, S. Wahlefeld, S. Katz, D. Belger, P. Hildebrandt, M. A. Mroginski, S. Leimkühler, I. Zebger,
Chemistry – A European Journal
2022,
28,
10.1002/chem.202201091
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A Minimal Light‐Driven System to Study the Enzymatic CO Reduction of Formate Dehydrogenase,
K. Laun, B. R. Duffus, H. Kumar, J. H. Oudsen, C. Karafoulidi‐Retsou, A. Tadjoung Waffo, P. Hildebrandt, K. Hoang Ly, S. Leimkühler, S. Katz, I. Zebger,
ChemCatChem
2022,
14,
10.1002/cctc.202201067
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A hydrogen-driven biocatalytic approach to recycling synthetic analogues of NAD(P)H,
H. A. Reeve, J. Nicholson, F. Altaf, T. H. Lonsdale, J. Preissler, L. Lauterbach, O. Lenz, S. Leimkühler, F. Hollmann, C. E. Paul, K. A. Vincent,
Chemical Communications
2022,
58,
10540–10543,
10.1039/d2cc02411j
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Second and Outer Coordination Sphere Effects in Nitrogenase, Hydrogenase, Formate Dehydrogenase, and CO Dehydrogenase,
S. T. Stripp, B. R. Duffus, V. Fourmond, C. Léger, S. Leimkühler, S. Hirota, Y. Hu, A. Jasniewski, H. Ogata, M. W. Ribbe,
Chemical Reviews
2022,
122,
11900–11973,
10.1021/acs.chemrev.1c00914
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The Role of the Nucleotides in the Insertion of the bis-Molybdopterin Guanine Dinucleotide Cofactor into apo-Molybdoenzymes,
K. Tiedemann, C. Iobbi-Nivol, S. Leimkühler,
Molecules
2022,
27,
2993–0,
10.3390/molecules27092993
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Electrochemical Trimethylamine N-Oxide Biosensor with Enzyme-Based Oxygen-Scavenging Membrane for Long-Term Operation under Ambient Air,
A. F. T. Waffo, B. Mitrova, K. Tiedemann, C. Iobbi-Nivol, S. Leimkühler, U. Wollenberger,
Biosensors
2021,
11,
98–0,
10.3390/bios11040098
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Voltammetry and Single‐Molecule In Situ Scanning Tunnelling Microscopy of the Redox Metalloenzyme Human Sulfite Oxidase,
J. Yan, E. E. Frøkjær, C. Engelbrekt, S. Leimkühler, J. Ulstrup, U. Wollenberger, X. Xiao, J. Zhang,
ChemElectroChem
2021,
8,
164–171,
10.1002/celc.202001258
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Cryo-EM structures reveal intricate Fe-S cluster arrangement and charging in Rhodobacter capsulatus formate dehydrogenase,
C. Radon, G. Mittelstädt, B. R. Duffus, J. Bürger, T. Hartmann, T. Mielke, C. Teutloff, S. Leimkühler, P. Wendler,
Nature Communications
2020,
11,
10.1038/s41467-020-15614-0
