témavezető: Fábián István
helyszín (magyar oldal): University of Debrecen, Faculty of Science and Technology, Department of Inorganic Analytical Chemistry D 504, D-509, D-524 laboratories helyszín rövidítés: D-524
A kutatási téma leírása:
Proteins are the most common and effective metal binding sites in living systems. They are built from amino acids and the donor groups of the side chains of amino acids make a significant contribution to the metal binding. [1] Several metal ions coordinated to the side chains of amino acid residues can promote acid-base and redox reactions. In order to achieve deeper insight into the mechanism of enzyme catalyzed reactions and determine the fine-tuning effects of the side chain donor groups, the investigation of short peptides and its small molecule moieties with redox active metal ions (such as copper, iron, nickel) is indispensable.
However, the number of possible ligands mimicking the active site of enzymes is infinite, therefore the model systems need to be selected carefully. Our primary goal is to clarify how the reaction rate and the mechanism of the catalytic reactions of biological relevance can be influenced by the coordination mode and the stability of metal complexes.
pH-potentiometry, UV-Vis, CD, EPR and NMR spectroscopic methods are useful tools to study the interactions between metal ions and ligands. In some cases, the possible structures of the complexes formed in aqueous solutions will be calculated by DFT method while the vertical transitions of the UV-vis spectra will be predicted by TD-DFT methods. [2] These techniques are completed with fast kinetic studies. Moreover, a custom-made photoreactor offers the possibility to investigate the redox reactions induced by light, while flash-photolytic experiments can be carried out to obtain information on primary intermediates generated by light.
The following projects are currently under investigation in our laboratory: i) Complex formation processes of NiSOD related peptides, [3,4] ii) Transition metal complexes as antioxidant systems [5,6] and iii) Development of new experimental protocol to investigate SOD activity.
References:
[1] I. Sóvágó; K. Várnagy; N. Lihi; Á. Grenács, Coord. Chem. Rev. 2016, 327-328, 43-54.
[2] G. Sciortino, N. Lihi, T. Czine, J-D Maréchal, A. Lledós, E. Garribba, Int. J. Quant. Chem. 2018, 15, e25655.
[3] N. Lihi, G. Csire, B. Szakács, N. V. May, K. Várnagy, I. Sóvágó, I. Fábián, Inorg. Chem. 2019, 58(2), 1414-1424.
[4] G. Csire, A. Kolozsi, T. Gajda, G. Pappalardo, K. Várnagy, I. Sóvágó, I. Fábián, N. Lihi, Dalton Trans. 2019, 48, 6217-6227.
[5] N. Ferenc, B. Gábor, M. Szabó, I. Fábián, New J. Chem. 2017, 41, 9947-9953.
[6] B. Gábor, M. Szabó, G. Lente, I. Fábián, J. Org. Chem. 2016, 81, 5345-5353.
előírt nyelvtudás: angol felvehető hallgatók száma: 1
Jelentkezési határidő: 2023-01-16
2024. IV. 17. ODT ülés Az ODT következő ülésére 2024. június 14-én, pénteken 10.00 órakor kerül sor a Semmelweis Egyetem Szenátusi termében (Bp. Üllői út 26. I. emelet).
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