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UniSysCat Publications

  • Conformational and mechanical stability of the isolated large subunit of membrane-bound [NiFe]-hydrogenase from Cupriavidus necator, J. Dragelj, C. Karafoulidi-Retsou, S. Katz, O. Lenz, I. Zebger, G. Caserta, S. Sacquin-Mora, M. A. Mroginski, Frontiers in Microbiology 2023, 13, 10.3389/fmicb.2022.1073315
  • Stepwise assembly of the active site of [NiFe]-hydrogenase, G. Caserta, S. Hartmann, C. Van Stappen, C. Karafoulidi-Retsou, C. Lorent, S. Yelin, M. Keck, J. Schoknecht, I. Sergueev, Y. Yoda, P. Hildebrandt, C. Limberg, S. DeBeer, I. Zebger, S. Frielingsdorf, O. Lenz, Nature Chemical Biology 2023, 10.1038/s41589-022-01226-w
  • Structural Determinants of the Catalytic Ni -L Intermediate of [NiFe]-Hydrogenase, A. F. T. Waffo, C. Lorent, S. Katz, J. Schoknecht, O. Lenz, I. Zebger, G. Caserta, Journal of the American Chemical Society 2023, 145, 13674–13685, 10.1021/jacs.3c01625
  • Immobilization of O -tolerant [NiFe] hydrogenase from on Tin-rich Indium Oxide Alters the Catalytic Bias from H Oxidation to Proton Reduction, V. Davis, N. Heidary, A. Guiet, K. H. Ly, M. Zerball, C. Schulz, N. Michael, R. von Klitzing, P. Hildebrandt, S. Frielingsdorf, O. Lenz, I. Zebger, A. Fischer, ACS Catalysis 2023, 13, 6312–6327, 10.1021/acscatal.2c06334
  • Stepwise conversion of the Cys [4Fe-3S] to a Cys [4Fe-4S] cluster and its impact on oxygen tolerance of [NiFe]-hydrogenase, A. Schmidt, J. Kalms, C. Lorent, S. Katz, S. Frielingsdorf, R. M. Evans, J. Fritsch, E. Siebert, C. Teutloff, F. A. Armstrong, I. Zebger, O. Lenz, P. Scheerer, Chemical Science 2023, 10.1039/D3SC03739H
  • Reversible Glutamate Coordination to High-Valent Nickel Protects the Active Site of a [NiFe] Hydrogenase from Oxygen, C. J. Kulka-Peschke, A. C. Schulz, C. Lorent, Y. Rippers, S. Wahlefeld, J. Preissler, C. Schulz, C. Wiemann, C. C. M. Bernitzky, C. Karafoulidi-Retsou, S. L. D. Wrathall, B. Procacci, H. Matsuura, G. M. Greetham, C. Teutloff, L. Lauterbach, Y. Higuchi, M. Ishii, N. T. Hunt, O. Lenz, I. Zebger, M. Horch, Journal of the American Chemical Society 2022, 144, 17022–17032, 10.1021/jacs.2c06400
  • High-Yield Production of Catalytically Active Regulatory [NiFe]-Hydrogenase From Cupriavidus necator in Escherichia coli, Q. Fan, G. Caserta, C. Lorent, I. Zebger, P. Neubauer, O. Lenz, M. Gimpel, Frontiers in Microbiology 2022, 13, 10.3389/fmicb.2022.894375
  • 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
  • Exploring Structure and Function of Redox Intermediates in [NiFe]‐Hydrogenases by an Advanced Experimental Approach for Solvated, Lyophilized and Crystallized Metalloenzymes, C. Lorent, V. Pelmenschikov, S. Frielingsdorf, J. Schoknecht, G. Caserta, Y. Yoda, H. Wang, K. Tamasaku, O. Lenz, S. P. Cramer, M. Horch, L. Lauterbach, I. Zebger, Angewandte Chemie International Edition 2021, 60, 15854–15862, 10.1002/anie.202100451
  • Resonance Raman spectroscopic analysis of the iron–sulfur cluster redox chain of the membrane‐bound [NiFe]‐hydrogenase, E. Siebert, A. Schmidt, S. Frielingsdorf, J. Kalms, U. Kuhlmann, O. Lenz, P. Scheerer, I. Zebger, P. Hildebrandt, Journal of Raman Spectroscopy 2021, 10.1002/jrs.6163
  • Hydroxy-bridged resting states of a [NiFe]-hydrogenase unraveled by cryogenic vibrational spectroscopy and DFT computations, G. Caserta, V. Pelmenschikov, C. Lorent, A. F. Tadjoung Waffo, S. Katz, L. Lauterbach, J. Schoknecht, H. Wang, Y. Yoda, K. Tamasaku, M. Kaupp, P. Hildebrandt, O. Lenz, S. P. Cramer, I. Zebger, Chemical Science 2021, 12, 2189–2197, 10.1039/D0SC05022A
  • Optimization of Culture Conditions for Oxygen-Tolerant Regulatory [NiFe]-Hydrogenase Production from Ralstonia eutropha H16 in Escherichia coli, Q. Fan, G. Caserta, C. Lorent, O. Lenz, P. Neubauer, M. Gimpel, Microorganisms 2021, 9, 1195–0, 10.3390/microorganisms9061195
  • Electrografted Interfaces on Metal Oxide Electrodes for Enzyme Immobilization and Bioelectrocatalysis, T. G. A. A. Harris, N. Heidary, S. Frielingsdorf, S. Rauwerdink, A. Tahraoui, O. Lenz, I. Zebger, A. Fischer, ChemElectroChem 2021, 8, 1329–1336, 10.1002/celc.202100020
  • Bringing biocatalytic deuteration into the toolbox of asymmetric isotopic labelling techniques, J. S. Rowbotham, M. A. Ramirez, O. Lenz, H. A. Reeve, K. A. Vincent, Nature Communications 2020, 11, 10.1038/s41467-020-15310-z
  • Phosphoglycolate salvage in a chemolithoautotroph using the Calvin cycle, N. J. Claassens, G. Scarinci, A. Fischer, A. I. Flamholz, W. Newell, S. Frielingsdorf, O. Lenz, A. Bar-Even, Proceedings of the National Academy of Sciences 2020, 117, 22452–22461, 10.1073/pnas.2012288117
  • Dihydrogen‐Driven NADPH Recycling in Imine Reduction and P450‐Catalyzed Oxidations Mediated by an Engineered O ‐Tolerant Hydrogenase, J. Preissler, H. A. Reeve, T. Zhu, J. Nicholson, K. Urata, L. Lauterbach, L. L. Wong, K. A. Vincent, O. Lenz, ChemCatChem 2020, 10.1002/cctc.202000763
  • The large subunit of the regulatory [NiFe]-hydrogenase from – a minimal hydrogenase?, G. Caserta, C. Lorent, A. Ciaccafava, M. Keck, R. Breglia, C. Greco, C. Limberg, P. Hildebrandt, S. P. Cramer, I. Zebger, O. Lenz, Chemical Science 2020, 11, 5453–5465, 10.1039/D0SC01369B
  • A membrane‐bound [NiFe]‐hydrogenase large subunit precursor whose C‐terminal extension is not essential for cofactor incorporation but guarantees optimal maturation, S. Hartmann, S. Frielingsdorf, G. Caserta, O. Lenz, MicrobiologyOpen 2020, 9, 1197–1206, 10.1002/mbo3.1029
  • In Vitro Assembly as a Tool to Investigate Catalytic Intermediates of [NiFe]-Hydrogenase, G. Caserta, C. Lorent, V. Pelmenschikov, J. Schoknecht, Y. Yoda, P. Hildebrandt, S. P. Cramer, I. Zebger, O. Lenz, ACS Catalysis 2020, 10, 13890–13894, 10.1021/acscatal.0c04079
  • Hydrogen Development, U. P. Apfel, W. Weigand, M. Horch, I. Zebger, O. Lenz, T. Fujishiro in Bioorganometallic Chemistry (Hrsg.: Wolfgang Weigand, Ulf-Peter Apfel), De Gruyter, 2020, 13–136, ISBN: 9783110496505
  • Understanding the structure and dynamics of hydrogenases by ultrafast and two-dimensional infrared spectroscopy, M. Horch, J. Schoknecht, S. L. D. Wrathall, G. M. Greetham, O. Lenz, N. T. Hunt, Chemical Science 2019, 10, 8981–8989, 10.1039/C9SC02851J
  • Formyltetrahydrofolate Decarbonylase Synthesizes the Active Site CO Ligand of O -Tolerant [NiFe] Hydrogenase, A. C. Schulz, S. Frielingsdorf, P. Pommerening, L. Lauterbach, G. Bistoni, F. Neese, M. Oestreich, O. Lenz, Journal of the American Chemical Society 2019, 142, 1457–1464, 10.1021/jacs.9b11506
  • Discriminating changes in intracellular NADH/NAD+ levels due to anoxicity and H2 supply in R. eutropha cells using the Frex fluorescence sensor, S. Wilkening, F. J. Schmitt, O. Lenz, I. Zebger, M. Horch, T. Friedrich, Biochimica et Biophysica Acta (BBA) - Bioenergetics 2019, 1860, 148062–0, 10.1016/j.bbabio.2019.148062