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Foto: Maciej Szaleniec
  • Investigation of enzymatic substrates spectrum and analysis of reaction products with LC-MS and GC-MS methods.

  • The study of enzyme reaction mechanisms with steady-state and pre-steady state kinetics 

  • Investigation of enzyme's thermodynamics using isothermal titration calorimetry (ITC).

  • Enzyme inhibition and deactivation study

  • Reaction engineering of enzymatic systems

  • Quantum chemical modeling of reaction pathways of enzymes

  • Modeling of quantitative structure-activity relationships (QSAR) of catalytic activity with Multiple Linear Regression (MLR) and Artificial Neural Network (ANN) methods.

  • Enzyme production in recombinant bacterial systems

  • FPLC and electrophoresis techniques for enzyme purification.

  • Investigation of enzyme activities towards different substrates with spectroscopic and HPLC-based activity assays. Rapid mixing stopped-flow kinetic measurements of half-cycle redox reactions.

  • Experiments with isotope-labeled substrates for determination of isotope kinetic effect. 

  • LC-MS and GC-MS for separation of reaction's products.

  • Isothermal titration calorimetry for investigation of thermodynamics of enzyme reaction.

  • Molecular dynamic (MD) simulations of enzyme-substrate complexes

  • Quantum chemical modeling of cluster model of enzyme active sites and verification of hypothetical reaction mechanism with various substrates.

  • QM:MM modeling of enzyme reactions

  • Prediction of biological activity with ANN and QSAR equations based on quantum chemical parameters.

Prof. Maciej Szaleniec

Head of JLBEC

Member of the ICSC since: October, 2002
Phone: +48 12 6395 101,
Room: 203, 223, 226
E-mail:

maciej.szaleniec@ikifp.edu.pl

Methods:

Research Topics:

ORCID: 0000-0002-7650-9263

Selected papers:

  • A. Winiarska, F. Ramrez-Amador, D. Hege, Y. Gemmecker, S. Prinz, G. Hochberg, J. Heider, M. Szaleniec, J. Michael Schuller, “A bacterial tungsten-containing aldehyde oxidoreductase forms an enzymatic decorated protein nanowire”, Science Adv. 9 (2023) eadg6689.

  • P. Wojcik, M. Glanowski, B. Mrugala, M. Procner, O. Zastawny, M. Flejszar, K. Kurpiewska, E. Niedzialkowska, W. Minor, M. Oszajca, A. J. Bojarski, A. Wojtkiewicz, M. Szaleniec, “Structure, Mutagenesis, and QM:MM Modeling of 3-Ketosteroid Δ1-Dehydrogenase from Sterolibacterium denitrificans ─ The Role of a New Putative Membrane-Associated Domain and Proton-Relay System in Catalysis”, Biochemistry 62 (2023) 808-823

  • A. Winiarska, D. Hege, Y. Gemmecker, J. Kryściak-Czerwenka, A. Seubert, J. Heider, M. Szaleniec, "Tungsten Enzyme Using Hydrogen as an Electron Donor to Reduce Carboxylic Acids and NAD+", ACS Catalysis, 2022, 12 (14), 8707-8717

  • I. Salii, M. Szaleniec, A. Alhaj Zein, D. Seyhan, A. Sekuła, K. Schühle, I. Kaplieva-Dudek, U. Linne, R. U. Meckenstock, J. Heider, "Determinants for Substrate Recognition in the Glycyl Radical Enzyme Benzylsuccinate Synthase Revealed by Targeted Mutagenesis", ACS Catalysis, 11 (2021) 3361-3370

  • M. Glanowski, P. Wójcik, M. Procner, T. Borowski, D. Lupa, P. Mielczarek, M. Oszajca, K. Świderek, V. Moliner, A.J. Bojarski, M. Szaleniec, "Enzymatic Δ1‑Dehydrogenation of 3‑Ketosteroids - Reconciliation of Kinetic Isotope Effects with the Reaction Mechanism", ACS Catal.,  11 (2021) 8211–8225 

  • P. Wójcik, M. Glanowski, A. M. Wojtkiewicz, A. Rohman, M. Szaleniec, "Universal capability of 3‑ketosteroid Δ1‑dehydrogenases to catalyze Δ1‑dehydrogenation of C17‑substituted steroids", Microb. Cell Fact., 20 (2021) 119

  • M. Glanowski, P. Wójcik, M. Procner, T. Borowski, D. Lupa, P. Mielczarek, M. Oszajca, K. Świderek, V. Moliner, A.J. Bojarski, M. Szaleniec, "Enzymatic Δ1‑Dehydrogenation of 3‑Ketosteroids - Reconciliation of Kinetic Isotope Effects with the Reaction Mechanism", ACS Catal., 10.1021/acscatal.1c01479

  • P. Borowiecki, N. Telatycka, M. Tataruch, A. Żądło‐Dobrowolska, T. Reiter, K. Schühle, J. Heider, M. Szaleniec, W. Kroutil, "Biocatalytic Asymmetric Reduction of γ‐Keto Esters to Access Optically Active γ‐Aryl‐γ‐butyrolactones", Adv. Synth. Catal., 362 (2020) 2012

  • A. M. Wojtkiewicz, P. Wójcik, M. Procner, M. Flejszar, M. Oszajca, M. Hochołowski, M. Tataruch, B. Mrugała, T. Janeczko, M. Szaleniec, "The efficient Δ1-dehydrogenation of a wide spectrum of 3-ketosteroids in a broad pH range by 3-ketosteroid dehydrogenase from Sterolibacterium denitrificans", J. Steroid Biochem. Mol. Biol., 202 (2020) 105731

  • K. Sofińska, A. M. Wojtkiewicz, P. Wójcik, O. Zastawny, M. Guzik, A. Winiarska, P. Waligórski, M. Cieśla, J. Barbasz, M. Szaleniec, "Investigation of quaternary structure of aggregating 3-ketosteroid dehydrogenase from Sterolibacterium denitrificans: In the pursuit of consensus of various biophysical techniques", Biochim. Biophys. Acta-Gen. Subj., 1863 (2019) 1027-1039

  • J. Szaleniec, A. Gibała, M. Pobiega, S. Parasion, J. Składzień, P. Stręk, T. Gosiewski, M. Szaleniec, "Exacerbations of Chronic Rhinosinusitis— Microbiology and Perspectives of Phage Therapy", Antibiotics, 8 (2019) 175

  • P. Kalimuthu, A. M. Wojtkiewicz, M. Szaleniec, P. V. Bernhardt, "Electrocatalytic Hydroxylation of Sterols by Steroid C25 Dehydrogenase from Sterolibacterium denitrificans", Chem. Eur. J., 24 (30) (2018) 7710-7717

  • M. Szaleniec, A. M. Wojtkiewicz, R. Bernhardt, T. Borowski, M. Donova, "Bacterial steroid hydroxylases: enzyme classes, their functions and comparison of their catalytic mechanisms", Appl. Microbiol. Biotechnol., 102(19) (2018) 8153-8171

  • A. Rugor, M. Tataruch, J. Staroń, A. Dudzik, E. Niedzialkowska, P. Nowak, A. Hogendorf, A. Michalik-Zym, D. B. Napruszewska, A. Jarzębski, K. Szymańska, W. Białas, M. Szaleniec, "Regioselective hydroxylation of cholecalciferol, cholesterol and other sterol derivatives by steroid C25 dehydrogenase", Appl. Microbiol. Biotechnol., 101 (2017) 1163-1174

  • A. Rugor, A. Wójcik-Augustyn, E. Niedzialkowska, S. Mordalski, J. Staroń A. Bojarski, M. Szaleniec, "Reaction mechanism of sterol hydroxylation by steroid C25 dehydrogenase – homology model, reactivity and isoenzymatic diversity", J. Inorg. Biochem., 173 (2017) 28–43

  • R. Rabus, M. Boll, J. Heider, R. U. Meckenstock, W. Buckel, O. Einsle, U. Ermler, B. T. Golding, R. P. Gunsalus, P. M. H. Kroneck, M. Krüger, T. Lueders, B. M. Martins, F. Musat, H. H. Richnow, B. Schink, J. Seifert, M. Szaleniec, T. Treude, G. M. Ullman, "Anaerobic Microbial Degradation of Hydrocarbons: From Enzymatic Reactions to the Environment.", J. Mol. Microbiol. Biotechnol., 26 (2016) 5-28

  • A. Dudzik, W. Snoch, P. Borowiecki, J. Opalinska-Piskorz, M. Witko, J. Heider, M. Szaleniec, "Asymmetric reduction of ketones and β-keto esters by (S)-1-phenylethanol dehydrogenase from denitrifying bacterium Aromatoleum aromaticum", App. Microbiol. Biotechnol., 99 (2015) 5055-5069

  • M. Szaleniec, A. Dudzik, B. Kozik, T. Borowski, J. Heider, M. Witko, "Mechanistic basis for the Enantioselectivity of the Anaerobic Hydroxylation of Alkylaromatic compounds by Ethylbenzene Dehydrogenase", J. Inorg. Biochem., 139 (2014) 9–20

  • D. H. Knack, J. L. Marshall, G. P. Harlow, A. Dudzik, M. Szaleniec, S-Y. Liu, J. Heider, "BN/CC isosteric compounds as new class of enzyme inhibitors: N- and B-ethyl-1,2-azaborine inhibit ethylbenzene hydroxylation as non-convertible substrate analogs", Angew. Chem. Int. Ed., 52 (2013) 2599 –2601

  • M. Szaleniec, T. Borowski, K. Schühle, M. Witko, J. Heider, "Ab inito modeling of ethylbenzene dehydrogenase reaction mechanism", J. Am. Chem. Soc., 132 (2010) 6014-6024

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