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UniSysCat Publications

  • Expanding the scope of resonance Raman spectroscopy in hydrogenase research: New observable states and reporter vibrations, C. C. M. Bernitzky, G. Caserta, S. Frielingsdorf, J. Schoknecht, A. Schmidt, P. Scheerer, O. Lenz, P. Hildebrandt, C. Lorent, I. Zebger, M. Horch, Journal of Inorganic Biochemistry 2025, 262, 112741–0, 10.1016/j.jinorgbio.2024.112741
  • Trapping of a phenoxyl radical at a non-haem high-spin iron(II) centre, D. Kass, V. A. Larson, T. Corona, U. Kuhlmann, P. Hildebrandt, T. Lohmiller, E. Bill, N. Lehnert, K. Ray, Nature Chemistry 2024, 16, 658–665, 10.1038/s41557-023-01405-9
  • A high-spin alkylperoxo–iron( ) complex with -anionic ligands: implications for the superoxide reductase mechanism, T. Devi, K. Dutta, J. Deutscher, S. Mebs, U. Kuhlmann, M. Haumann, B. Cula, H. Dau, P. Hildebrandt, K. Ray, Chemical Science 2024, 15, 528–533, 10.1039/D3SC05603A
  • A Bioinspired Nonheme Fe –(O )–Cu Complex with an = 1 Ground State, D. Kass, S. Katz, H. Özgen, S. Mebs, M. Haumann, R. García-Serres, H. Dau, P. Hildebrandt, T. Lohmiller, K. Ray, Journal of the American Chemical Society 2024, 146, 24808–24817, 10.1021/jacs.4c04492
  • A bis-Phenolate Carbene-Supported bis-μ-Oxo Iron(IV/IV) Complex with a [Fe (μ-O) Fe ] Diamond Core Derived from Dioxygen Activation, L. Gravogl, D. Kass, O. Pyschny, F. W. Heinemann, M. Haumann, S. Katz, P. Hildebrandt, H. Dau, A. Swain, R. García-Serres, K. Ray, D. Munz, K. Meyer, Journal of the American Chemical Society 2024, 146, 28757–28769, 10.1021/jacs.4c07582
  • Cation Dependence of Enniatin B/Membrane‐Interactions Assessed Using Surface‐Enhanced Infrared Absorption (SEIRA) Spectroscopy, B. D. Gonzalez, E. Forbrig, G. Yao, P. Kielb, M. A. Mroginski, P. Hildebrandt, J. Kozuch, ChemPlusChem 2024, 89, 10.1002/cplu.202400159
  • High Fluorescence of Phytochromes Does Not Require Chromophore Protonation, S. Katz, H. T. Phan, F. Rieder, F. Seifert, M. Pietzsch, J. Laufer, F. J. Schmitt, P. Hildebrandt, Molecules 2024, 29, 4948–0, 10.3390/molecules29204948
  • Hydrogen Bonding and Noncovalent Electric Field Effects in the Photoconversion of a Phytochrome, A. D. Nguyen, N. Michael, L. Sauthof, J. von Sass, O. T. Hoang, A. Schmidt, M. La Greca, R. Schlesinger, N. Budisa, P. Scheerer, M. A. Mroginski, A. Kraskov, P. Hildebrandt, The Journal of Physical Chemistry B 2024, 128, 11644–11657, 10.1021/acs.jpcb.4c06419
  • A New Thiolate‐Bound Dimanganese Cluster as a Structural and Functional Model for Class Ib Ribonucleotide Reductases, B. Battistella, T. Lohmiller, B. Cula, P. Hildebrandt, U. Kuhlmann, H. Dau, S. Mebs, K. Ray, Angewandte Chemie International Edition 2023, 10.1002/anie.202217076
  • 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
  • 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
  • Vibrational Spectroscopy of Phytochromes, P. Hildebrandt, Biomolecules 2023, 13, 1007–0, 10.3390/biom13061007
  • Experimental Assessment of the Electronic and Geometrical Structure of a Near-Infrared Absorbing and Highly Fluorescent Microbial Rhodopsin, M. Broser, T. Andruniów, A. Kraskov, R. Palombo, S. Katz, M. Kloz, J. Dostál, C. Bernardo, J. T. M. Kennis, P. Hegemann, M. Olivucci, P. Hildebrandt, The Journal of Physical Chemistry Letters 2023, 14, 9291–9295, 10.1021/acs.jpclett.3c02167
  • On the Role of a Conserved Tryptophan in the Chromophore Pocket of Cyanobacteriochrome, M. Blain-Hartung, G. Johannes von Sass, J. Plaickner, S. Katz, O. Tu Hoang, M. Andrea Mroginski, N. Esser, N. Budisa, K. T. Forest, P. Hildebrandt, Journal of Molecular Biology 2023, 168227–0, 10.1016/j.jmb.2023.168227
  • Orthogonal translation with 5‐cyanotryptophan as an infrared probe for local structural information, electrostatics, and hydrogen bonding, G. J. von Freiherr Sass, M. Blain‐Hartung, T. Baumann, K. T. Forest, P. Hildebrandt, N. Budisa, Protein Science 2023, 32, 10.1002/pro.4705
  • In Situ Raman Spectroscopy Reveals Cytochrome Redox-Controlled Modulation of Mitochondrial Membrane Permeabilization That Triggers Apoptosis, J. Zhu, J. Zhu, H. Xie, J. Tang, Y. Miao, L. Cai, P. Hildebrandt, X. X. Han, Nano Letters 2023, 24, 370–377, 10.1021/acs.nanolett.3c04129
  • Unusual structures and unknown roles of FeS clusters in metalloenzymes seen from a resonance Raman spectroscopic perspective, G. Caserta, L. Zuccarello, C. Barbosa, C. M. Silveira, E. Moe, S. Katz, P. Hildebrandt, I. Zebger, S. Todorovic, Coordination Chemistry Reviews 2022, 452, 214287–0, 10.1016/j.ccr.2021.214287
  • Ultrafast proton-coupled isomerization in the phototransformation of phytochrome, Y. Yang, T. Stensitzki, L. Sauthof, A. Schmidt, P. Piwowarski, F. Velazquez Escobar, N. Michael, A. D. Nguyen, M. Szczepek, F. N. Brünig, R. R. Netz, M. A. Mroginski, S. Adam, F. Bartl, I. Schapiro, P. Hildebrandt, P. Scheerer, K. Heyne, Nature Chemistry 2022, 14, 823–830, 10.1038/s41557-022-00944-x
  • 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
  • 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
  • The influence of secondary interactions on the [Ni(O2)]+ mediated aldehyde oxidation reactions, B. Battistella, K. Warm, B. Cula, B. Lu, P. Hildebrandt, U. Kuhlmann, H. Dau, S. Mebs, K. Ray, Journal of Inorganic Biochemistry 2022, 227, 111668–0, 10.1016/j.jinorgbio.2021.111668
  • QuasAr Odyssey: the origin of fluorescence and its voltage sensitivity in microbial rhodopsins, A. Silapetere, S. Hwang, Y. Hontani, R. G. Fernandez Lahore, J. Balke, F. V. Escobar, M. Tros, P. E. Konold, R. Matis, R. Croce, P. J. Walla, P. Hildebrandt, U. Alexiev, J. T. M. Kennis, H. Sun, T. Utesch, P. Hegemann, Nature Communications 2022, 13, 10.1038/s41467-022-33084-4
  • Potential Distribution across Model Membranes, T. Utesch, J. Staffa, S. Katz, G. Yao, J. Kozuch, P. Hildebrandt, The Journal of Physical Chemistry B 2022, 126, 7664–7675, 10.1021/acs.jpcb.2c05372
  • Human endonuclease III/NTH1: focusing on the [4Fe–4S] cluster and the N-terminal domain, E. Moe, C. M. Silveira, L. Zuccarello, F. Rollo, M. Stelter, S. De Bonis, C. Kulka-Peschke, S. Katz, P. Hildebrandt, I. Zebger, J. Timmins, S. Todorovic, Chemical Communications 2022, 58, 12568–12571, 10.1039/D2CC03643F
  • Electron transfer between cytochrome c and microsomal monooxygenase generates reactive oxygen species that accelerates apoptosis, H. Xie, L. Song, S. Katz, J. Zhu, Y. Liu, J. Tang, L. Cai, P. Hildebrandt, X. X. Han, Redox Biology 2022, 53, 102340–0, 10.1016/j.redox.2022.102340
  • Evidence of Sulfur Non‐Innocence in [Co (dithiacyclam)] ‐Mediated Catalytic Oxygen Reduction Reactions, B. Battistella, L. Iffland‐Mühlhaus, M. Schütze, B. Cula, U. Kuhlmann, H. Dau, P. Hildebrandt, T. Lohmiller, S. Mebs, U. Apfel, K. Ray, Angewandte Chemie International Edition 2022, 62, 10.1002/anie.202214074
  • Substrate-Dependent Conformational Switch of the Noncubane [4Fe-4S] Cluster in Heterodisulfide Reductase HdrB, V. Pelmenschikov, D. Ferreira, S. S. Venceslau, P. Hildebrandt, I. A. C. Pereira, S. Todorovic, Journal of the American Chemical Society 2022, 145, 7–11, 10.1021/jacs.2c10885
  • 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
  • Local Electric Field Changes during the Photoconversion of the Bathy Phytochrome Agp2, A. Kraskov, J. von Sass, A. D. Nguyen, T. O. Hoang, D. Buhrke, S. Katz, N. Michael, J. Kozuch, I. Zebger, F. Siebert, P. Scheerer, M. A. Mroginski, N. Budisa, P. Hildebrandt, Biochemistry 2021, 60, 2967–2977, 10.1021/acs.biochem.1c00426
  • 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
  • A Resonance Raman Marker Band Characterizes the Slow and Fast Form of Cytochrome Oxidase, F. Kruse, A. D. Nguyen, J. Dragelj, J. Heberle, P. Hildebrandt, M. A. Mroginski, I. M. Weidinger, Journal of the American Chemical Society 2021, 143, 2769–2776, 10.1021/jacs.0c10767
  • Molecular Details on Multiple Cofactor Containing Redox Metalloproteins Revealed by Infrared and Resonance Raman Spectroscopies, C. M. Silveira, L. Zuccarello, C. Barbosa, G. Caserta, I. Zebger, P. Hildebrandt, S. Todorovic, Molecules 2021, 26, 4852–0, 10.3390/molecules26164852
  • Spectroscopic Characterization of a Reactive [Cu (μ‐OH) ] Intermediate in Cu/TEMPO Catalyzed Aerobic Alcohol Oxidation Reaction, K. Warm, G. Tripodi, E. Andris, S. Mebs, U. Kuhlmann, H. Dau, P. Hildebrandt, J. Roithová, K. Ray, Angewandte Chemie International Edition 2021, 60, 23018–23024, 10.1002/anie.202108442
  • A Pseudotetrahedral Terminal Oxoiron(IV) Complex: Mechanistic Promiscuity in C−H Bond Oxidation Reactions, K. Warm, A. Paskin, U. Kuhlmann, E. Bill, M. Swart, M. Haumann, H. Dau, P. Hildebrandt, K. Ray, Angewandte Chemie International Edition 2021, 60, 6752–6756, 10.1002/anie.202015896
  • A bioinspired oxoiron( ) motif supported on a N S macrocyclic ligand, J. Deutscher, P. Gerschel, K. Warm, U. Kuhlmann, S. Mebs, M. Haumann, H. Dau, P. Hildebrandt, U. P. Apfel, K. Ray, Chemical Communications 2021, 57, 2947–2950, 10.1039/d1cc00250c
  • Stable, but still reactive – investigations on the effects of Lewis acid binding on copper nitrene intermediates, K. Warm, I. Monte Pérez, U. Kuhlmann, P. Hildebrandt, E. Farquhar, M. Swart, K. Ray, Zeitschrift für Anorganische und Allgemeine Chemie 2021, 647, 1495–1502, 10.1002/zaac.202100092
  • Stoichiometric Formation of an Oxoiron(IV) Complex by a Soluble Methane Monooxygenase Type Activation of O at an Iron(II)-Cyclam Center, D. Kass, T. Corona, K. Warm, B. Braun-Cula, U. Kuhlmann, E. Bill, S. Mebs, M. Swart, H. Dau, M. Haumann, P. Hildebrandt, K. Ray, Journal of the American Chemical Society 2020, 142, 5924–5928, 10.1021/jacs.9b13756
  • Catalytic dioxygen reduction mediated by a tetranuclear cobalt complex supported on a stannoxane core, A. Chandra, S. Mebs, S. Kundu, U. Kuhlmann, P. Hildebrandt, H. Dau, K. Ray, Dalton Transactions 2020, 49, 6065–6073, 10.1039/d0dt00475h
  • 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
  • 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
  • Immobilized dye-decolorizing peroxidase (DyP) and directed evolution variants for hydrogen peroxide biosensing, C. Barbosa, C. M. Silveira, D. Silva, V. Brissos, P. Hildebrandt, L. O. Martins, S. Todorovic, Biosensors and Bioelectronics 2020, 153, 112055–0, 10.1016/j.bios.2020.112055
  • Gradient metal nanoislands as a unified surface enhanced Raman scattering and surface enhanced infrared absorption platform for analytics, D. Gkogkou, T. Shaykhutdinov, C. Kratz, T. W. H. Oates, P. Hildebrandt, I. M. Weidinger, K. H. Ly, N. Esser, K. Hinrichs, The Analyst 2019, 144, 5271–5276, 10.1039/C9an00839J
  • Influence of Mesityl and Thiophene Peripheral Substituents on Surface Attachment, Redox Chemistry, and ORR Activity of Molecular Iron Porphyrin Catalysts on Electrodes, R. Götz, K. H. Ly, P. Wrzolek, A. Dianat, A. Croy, G. Cuniberti, P. Hildebrandt, M. Schwalbe, I. M. Weidinger, Inorganic Chemistry 2019, 58, 10637–10647, 10.1021/acs.inorgchem.9b00043
  • Accelerated Photo‐Induced Degradation of Benzidine‐ ‐Aminothiophenolate Immobilized at Light‐Enhancing TiO Nanotube Electrodes, C. J. Querebillo, I. H. Öner, P. Hildebrandt, K. H. Ly, I. M. Weidinger, Chemistry – A European Journal 2019, 25, 16048–16053, 10.1002/chem.201902963
  • Probing Structure and Reaction Dynamics of Proteins Using Time-Resolved Resonance Raman Spectroscopy, D. Buhrke, P. Hildebrandt, Chemical Reviews 2019, 120, 3577–3630, 10.1021/acs.chemrev.9b00429
  • Spectroscopic, thermodynamic and computational evidence of the locations of the FADs in the nitrogen fixation-associated electron transfer flavoprotein, N. Mohamed-Raseek, H. D. Duan, P. Hildebrandt, M. A. Mroginski, A. F. Miller, Chemical Science 2019, 10, 7762–7772, 10.1039/c9sc00942f
  • MerMAIDs: a family of metagenomically discovered marine anion-conducting and intensely desensitizing channelrhodopsins, J. Oppermann, P. Fischer, A. Silapetere, B. Liepe, S. Rodriguez-Rozada, J. Flores-Uribe, E. Peter, A. Keidel, J. Vierock, J. Kaufmann, M. Broser, M. Luck, F. Bartl, P. Hildebrandt, J. S. Wiegert, O. Béjà, P. Hegemann, J. Wietek, Nature Communications 2019, 10, 10.1038/s41467-019-11322-6
  • Plasmonic Cu/CuCl/Cu2S/Ag and Cu/CuCl/Cu2S/Au Supports with Peroxidase-Like Activity: Insights from Surface Enhanced Raman Spectroscopy, W. Song, P. Hildebrandt, I. M. Weidinger, Zeitschrift für Physikalische Chemie 2018, 232, 1541–1550, 10.1515/zpch-2018-1126
  • A New Domain of Reactivity for High-Valent Dinuclear [M(μ-O) M′] Complexes in Oxidation Reactions, X. Engelmann, S. Yao, E. R. Farquhar, T. Szilvási, U. Kuhlmann, P. Hildebrandt, M. Driess, K. Ray, Angewandte Chemie 2017, 129, 303–307, 10.1002/ange.201607611