TY - JOUR AU - Karner, Victoria AU - Jancsó, Attila AU - Hemmingsen, Lars TI - Probing the Bioinorganic Chemistry of Cu(I) with 111Ag Perturbed Angular Correlation (PAC) Spectroscopy JF - INORGANICS J2 - INORGANICS VL - 11 PY - 2023 IS - 10 PG - 13 SN - 2304-6740 DO - 10.3390/inorganics11100375 UR - https://m2.mtmt.hu/api/publication/34409105 ID - 34409105 AB - The two most common oxidation states of copper in biochemistry are Cu(II) and Cu(I), and while Cu(II) lends itself to spectroscopic interrogation, Cu(I) is silent in most techniques. Ag(I) and Cu(I) are both closed-shell d10 monovalent ions, and to some extent share ligand and coordination geometry preferences. Therefore, Ag(I) may be applied to explore Cu(I) binding sites in biomolecules. Here, we review applications of 111Ag perturbed angular correlation (PAC) of γ-ray spectroscopy aimed to elucidate the chemistry of Cu(I) in biological systems. Examples span from small blue copper proteins such as plastocyanin and azurin (electron transport) over hemocyanin (oxygen transport) to CueR and BxmR (metal-ion-sensing proteins). Finally, possible future applications are discussed. 111Ag is a radionuclide which undergoes β-decay to 111Cd, and it is a γ-γ cascade of the 111Cd daughter nucleus, which is used in PAC measurements. 111Ag PAC spectroscopy may provide information on the coordination environment of Ag(I) and on the structural relaxation occurring upon the essentially instantaneous change from Ag(I) to Cd(II). LA - English DB - MTMT ER - TY - JOUR AU - Nafaee, Zeyad Hasan Abdullah AU - Egyed, Viktória AU - Jancsó, Attila AU - Tóth, Annamária AU - Gerami, Adeleh Mokhles AU - Dang, Thanh Thien AU - Heiniger-Schell, Juliana AU - Hemmingsen, Lars AU - Hunyadi-Gulyás Éva, Csilla AU - Peintler, Gábor AU - Gyurcsik, Béla TI - Revisiting the hydrolysis of ampicillin catalyzed by Temoneira-1 β-lactamase, and the effect of Ni(II), Cd(II) and Hg(II) JF - PROTEIN SCIENCE J2 - PROTEIN SCI VL - 32 PY - 2023 IS - 12 PG - 20 SN - 0961-8368 DO - 10.1002/pro.4809 UR - https://m2.mtmt.hu/api/publication/34393301 ID - 34393301 AB - Abstract ?-Lactamases grant resistance to bacteria against ?-lactam antibiotics. The active center of TEM-1 ?-lactamase accommodates a Ser-Xaa-Xaa-Lys motif. TEM-1 ?-lactamase is not a metalloenzyme but it possesses several putative metal ion binding sites. The sites composed of His residue pairs chelate borderline transition metal ions such as Ni(II). In addition, there are many sulfur-containing donor groups that can coordinate soft metal ions such as Hg(II). Cd(II) may bind to both types of the above listed donor groups. No significant change was observed in the circular dichroism spectra of TEM-1 ?-lactamase on increasing the metal ion content of the samples, with the exception of Hg(II) inducing a small change in the secondary structure of the protein. A weak nonspecific binding of Hg(II) was proven by mass spectrometry and 119mHg perturbed angular correlation spectroscopy. The hydrolytic process of ampicillin catalyzed by TEM-1 ?-lactamase was described by the kinetic analysis of the set of full catalytic progress curves, where the slow, yet observable conversion of the primary reaction product into a second one, identified as ampilloic acid by mass spectrometry, needed also to be considered in the applied model. Ni(II) and Cd(II) slightly promoted the catalytic activity of the enzyme while Hg(II) exerted a noticeable inhibitory effect. Hg(II) and Ni(II), applied at 10??M concentration, inhibited the growth of E. coli BL21(DE3) in M9 minimal medium in the absence of ampicillin, but addition of the antibiotic could neutralize this toxic effect by complexing the metal ions. LA - English DB - MTMT ER - TY - JOUR AU - Szekeres, Levente István AU - Maldivi, Pascale AU - Lebrun, Colette AU - Gateau, Christelle AU - Mesterházy, Edit AU - Delangle, Pascale AU - Jancsó, Attila TI - Tristhiolato Pseudopeptides Bind Arsenic(III) in an AsS 3 Coordination Environment Imitating Metalloid Binding Sites in Proteins JF - INORGANIC CHEMISTRY J2 - INORG CHEM VL - 62 PY - 2023 IS - 17 SP - 6817 EP - 6824 PG - 8 SN - 0020-1669 DO - 10.1021/acs.inorgchem.3c00563 UR - https://m2.mtmt.hu/api/publication/33767799 ID - 33767799 AB - The AsIII binding of two NTA-based tripodal pseudopeptides, possessing three cysteine (ligand L1) or D- penicillamine residues (ligand L2) as potential coordinating groups for soft semimetals or metal ions, was studied by experimental (UV, CD, NMR, and ESI-MS) and theoretical (DFT) methods. All of the experimental data, obtained with the variation of the AsIII:ligand concentration ratios or pH values in some instances, evidence the exclusive formation of species with an AsS3-type coordination mode. The UV-monitored titration of the ligands with arsenous acid at pH = 7.0 provided an absorbance data set that allowed for the determination of apparent stability constants of the forming species. The obtained stabilities (logK ' = 5.26 (AsL1) and logK ' = 3.04 (AsL2)) reflect high affinities, especially for the sterically less restricted cysteine derivative. DFT calculated structures correlate well with the spectroscopic results and, in line with the 1H NMR data, indicate a preference for the all-endo conformers resembling the AsIII environment at the semimetal binding sites in various metalloproteins. LA - English DB - MTMT ER - TY - JOUR AU - Balogh, Ria Katalin AU - Gyurcsik, Béla AU - Jensen, Mikael AU - Thulstrup, Peter W. AU - Köster, Ulli AU - Christensen, Niels Johan AU - Jensen, Marianne L. AU - Hunyadi-Gulyás Éva, Csilla AU - Hemmingsen, Lars AU - Jancsó, Attila TI - Tying Up a Loose End: On the Role of the C‐Terminal CCHHRAG Fragment of the Metalloregulator CueR JF - CHEMBIOCHEM J2 - CHEMBIOCHEM VL - 23 PY - 2022 IS - 16 PG - 8 SN - 1439-4227 DO - 10.1002/cbic.202200290 UR - https://m2.mtmt.hu/api/publication/32924475 ID - 32924475 LA - English DB - MTMT ER - TY - JOUR AU - McFadden, Ryan M. L. AU - Szunyogh, Dániel AU - Bravo-Frank, Nicholas AU - Chatzichristos, Aris AU - Dehn, Martin H. AU - Fujimoto, Derek AU - Jancsó, Attila AU - Johannsen, Silke AU - Kálomista, Ildikó AU - Karner, Victoria L. AU - Kiefl, Robert F. AU - Larsen, Flemming H. AU - Lassen, Jens AU - Levy, C. D. Philip AU - Li, Ruohong AU - McKenzie, Iain AU - McPhee, Hannah AU - Morris, Gerald D. AU - Pearson, Matthew R. AU - Sauer, Stephan P. A. AU - Sigel, Roland K. O. AU - Thulstrup, Peter W. AU - MacFarlane, W. Andrew AU - Hemmingsen, Lars AU - Stachura, Monika TI - Magnesium(II)‐ATP Complexes in 1‐Ethyl‐3‐Methylimidazolium Acetate Solutions Characterized by 31Mg β‐Radiation‐Detected NMR Spectroscopy JF - ANGEWANDTE CHEMIE-INTERNATIONAL EDITION J2 - ANGEW CHEM INT EDIT VL - 61 PY - 2022 IS - 35 PG - 8 SN - 1433-7851 DO - 10.1002/anie.202207137 UR - https://m2.mtmt.hu/api/publication/32924465 ID - 32924465 LA - English DB - MTMT ER - TY - CHAP AU - Csomos, Attila AU - Kontra, Bence AU - Kovács, Ervin AU - Tóth, Annamária AU - Galbács, Gábor AU - Sajdik, Kadosa AU - Jancsó, Attila AU - Mucsi, Zoltán ED - Demetrio, Milea TI - Metal ion binding and Ca2+-promoted fluorescence of bis(diethylamino)xanthene-labelled BAPTA analogues T2 - ISMEC 2021 International Symposium on Thermodynamics of Metal Complexes PB - ISMEC Group CY - Online kiadás T3 - ISMEC GROUP SERIES, ISSN 2239-2459 ; 10. PY - 2021 PG - 2 UR - https://m2.mtmt.hu/api/publication/32685955 ID - 32685955 LA - English DB - MTMT ER - TY - GEN AU - Tóth, Annamária AU - Csomos, Attila AU - Kontra, Bence AU - Kovács, Ervin AU - Galbács, Gábor AU - Mucsi, Zoltán AU - Jancsó, Attila TI - Ca2+-érzékelőkben potenciálisan alkalmazható módosított BAPTA származékok Ca2+ - és Mg2+ -kötő sajátságai PY - 2021 UR - https://m2.mtmt.hu/api/publication/32685853 ID - 32685853 AB - Az idegkutatásokban gyakran alkalmazott fluoreszcens Ca2+-indikátorok jelentős hányada a fluoreszcens molekularészük mellett kelátor egységként a BAPTA-t (1,2-bisz(oaminofenoxy) etán-N,N,N',N'-tetraecetsav), ill. annak szubsztituált származékait tartalmazza [1]. Munkánk során a BAPTA linker szakaszában módosított két származékáa (RBP, MBP) Ca2+- és Mg2+-ionokkal alkotott rendszereinek pH- és fémion-ligandum aránytól függő speciációs viszonyait, illetve a képződő komplexek stabilitását tanulmányoztuk, valamint hasonlítottuk össze az alap vegyület Ca2+- és Mg2+-ionokkal történő kölcsönhatásával. A vizsgált rendszerekben kizárólag mono-komplexek képződnek, azonban a Ca2+, illetve a Mg2+ komplexek stabiltásai között, továbbá a három vegyület Ca2+-ion szelektivitásában is komoly különbségeket tapasztaltunk. Az egyensúlyi vizsgálatok mellett az előadásban bemutatjuk a kelátorok és tetrametil rodamin fluorofór hozzájuk történő kapcsolásával felépített érzékelő vegyületek Ca2+-ion affinitásával, illetve a fémionok „turn on” hatásával kapcsolatos eddigi eredményeinket is. [1] R.Y. Tsien, Biochemistry, 1980, 19, 2396-2404. LA - Hungarian DB - MTMT ER - TY - JOUR AU - Kovács, Ervin AU - Cseri, Levente AU - Jancsó, Attila AU - Terényi, Ferenc AU - Fülöp, Anna AU - Rózsa J., Balázs AU - Galbács, Gábor AU - Mucsi, Zoltán TI - Synthesis and Fluorescence Mechanism of the Aminoimidazolone Analogues of the Green Fluorescent Protein: Towards Advanced Dyes with Enhanced Stokes Shift, Quantum Yield and Two-Photon Absorption JF - EUROPEAN JOURNAL OF ORGANIC CHEMISTRY J2 - EUR J ORG CHEM VL - 2021 PY - 2021 IS - 41 SP - 5649 EP - 5660 PG - 12 SN - 1434-193X DO - 10.1002/ejoc.202101173 UR - https://m2.mtmt.hu/api/publication/32399352 ID - 32399352 N1 - Department of Chemistry, Femtonics Inc., Tűzoltó u. 58, Budapest, 1094, Hungary Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Magyar tudósok körútja 2, Budapest, 1117, Hungary Department of Chemical Engineering & Analytical Science, The University of Manchester, The Mill, Sackville Street, Manchester, M1 3BB, United Kingdom Department of Inorganic and Analytical Chemistry, University of Szeged, Dóm tér 8, Szeged, 6720, Hungary Two-Photon Measurement Technology Research Group, The Faculty of Information Technology, Pázmány Péter Catholic University, Práter u. 50/A, Budapest, 1083, Hungary Laboratory of 3D Functional Imaging of Neuronal Networks and Dendritic Integration, Institute of Experimental Medicine, Szigony utca 43, Budapest, 1083, Hungary Institute of Chemistry, Faculty of Materials Science and Engineering, University of Miskolc, Egyetem út 1, Miskolc, 3515, Hungary Export Date: 18 January 2022 CODEN: EJOCF Correspondence Address: Kovács, E.; Department of Chemistry, Tűzoltó u. 58, Hungary; email: kovacs.ervin@ttk.hu Correspondence Address: Mucsi, Z.; Department of Chemistry, Tűzoltó u. 58, Hungary; email: zmucsi@femtonics.eu Funding details: 2018‐1.1.2‐KFI‐2018‐00097, 2018‐1.3.1‐VKE‐2018‐00032 Funding details: Hungarian Scientific Research Fund, OTKA, PD128612 Funding details: Magyar Tudományos Akadémia, MTA, BO/799/21/7 Funding details: Nemzeti Kutatási, Fejlesztési és Innovaciós Alap, NKFIA Funding details: Innovációs és Technológiai Minisztérium Funding text 1: This project was supported by National Research, Development and Innovation Fund of Hungary, financed under the [2018‐1.1.2‐KFI‐2018‐00097; 2018‐1.3.1‐VKE‐2018‐00032; OTKA PD128612] funding scheme. The authors are grateful for the Bolyai Research Scholarship of the Hungarian Academy of Sciences (BO/799/21/7) and the ÚNKP‐21‐5 new National Excellence Program of the Ministry for Innovation and Technology from the Source of the National Research, Development and Innovation Fund. AB - Novel small-molecular analogues the green fluorescence protein (GFP) chromophore are synthesised to expand and improve this fluorophore family and to deepen the understanding of their fluorescence mechanism. The introduction of an aminophenyl substituent and the repositioning of the hydroxyl group to enable strong intramolecular hydrogen bonding, not only enhances fluorescence emission, but also results in an increased Stokes shift and a considerable red shift. Experimental and computational results describe a dual fluorescence involving both excited-state intramolecular proton transfer and internal charge transfer (ESIPT?ICT) mechanism. The further improvement of the photophysical properties via the systematic variation of dialkylamino substituents at a single position of the chromophore led to a two-orders of magnitude enhancement in the quantum yields. In addition, the novel compounds also have significant two-photon absorption, which widens the possibilities for applications in the field of bioimaging. LA - English DB - MTMT ER - TY - JOUR AU - Csomos, Attila AU - Kontra, Bence AU - Jancsó, Attila AU - Galbács, Gábor AU - Deme, Ruth AU - Kele, Zoltán AU - Rózsa J., Balázs AU - Kovács, Ervin AU - Mucsi, Zoltán TI - A comprehensive study of the Ca2+ ion binding of fluorescently labelled BAPTA analogues JF - EUROPEAN JOURNAL OF ORGANIC CHEMISTRY J2 - EUR J ORG CHEM VL - 2021 PY - 2021 IS - 37 SP - 5248 EP - 5261 PG - 17 SN - 1434-193X DO - 10.1002/ejoc.202100948 UR - https://m2.mtmt.hu/api/publication/32187933 ID - 32187933 AB - Since its development, the ionophore BAPTA (1,2?bis(2?aminophenoxy)-ethane?N,N,N?,N??tetraacetic acid) has been used unchanged in calcium sensing applications. In this work we present a comprehensive experimental and theoretical study of novel alterations in the structure of BAPTA, with a focus on the systematic modification of the chain connecting the two aromatic rings of the molecule (denoted as ?linker?). A bis-(diethylamino)xantene fluorophore was also attached to the structures in a fixed position and the structure-fluorescence response relationship of these molecules was investigated in addition. The effect of the length of the linker, the number of O atoms in this chain and even the removal of one of the rings was tested; these all proved to significantly alter the characteristics of the compounds. For example, it was found that the second aromatic ring of BAPTA is not essential for the turn-on of the fluorescence. We also demonstrated that successful sensing can be realized even by replacing the chain with a single oxygen atom, which suggests the availability of a new calcium binding mode of the chelator. The reliable turn-on characteristic, the steep Ca 2+ fluorescence titration curve and the intense fluorescence emission combine to make this compound a prospective candidate as a calcium sensing molecular probe in diagnostic neurobiological applications. LA - English DB - MTMT ER - TY - JOUR AU - May, Nóra Veronika AU - Jancsó, Attila AU - Enyedy, Éva Anna TI - Binding Models of Copper(II) Thiosemicarbazone Complexes with Human Serum Albumin: A Speciation Study JF - MOLECULES J2 - MOLECULES VL - 26 PY - 2021 IS - 9 PG - 15 SN - 1420-3049 DO - 10.3390/molecules26092711 UR - https://m2.mtmt.hu/api/publication/32000256 ID - 32000256 N1 - Cited By :7 Export Date: 18 September 2023 CODEN: MOLEF Correspondence Address: Enyedy, É.A.; Department of Inorganic and Analytical Chemistry, Dóm tér 7, Hungary; email: enyedy@chem.u-szeged.hu Chemicals/CAS: copper, 15158-11-9, 7440-50-8; human serum albumin, 9048-49-1; 3-aminopyridine-2-carboxaldehyde thiosemicarbazone; aspartyl-alanyl-histidyl-lysine; Copper; Oligopeptides; Pyridines; Serum Albumin, Human; Solutions; Thiosemicarbazones Funding details: Emberi Eroforrások Minisztériuma, EMMI, TKP-2020 Funding details: National Research, Development and Innovation Office, FK124240 Funding text 1: Funding: This research was funded by National Research, Development, and Innovation Office-NKFIA through projects FK124240 and Ministry of Human Capacities through project Hungary grant TKP-2020. LA - English DB - MTMT ER -