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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

What do we do

Our aim is to combine the research potentials of Institute of Catalysis and Surface Chemistry and Institute of Plant Physiology in the field of biochemistry and biotechnology

Our Projects

Laboratory members aplly for new domestic and international projects in order to carry out increasingly advanced research

Join our team

We are open to scientists willing to cooperate on ongoing projects as well as those coming with their own scientific ideas

Contact us

If you are interested in research conducted in our laboratory or have any questions, please do not hesitate and feel free to contact us

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