@article{MTMT:34409105,
	title = {Probing the Bioinorganic Chemistry of Cu(I) with 111Ag Perturbed Angular Correlation (PAC) Spectroscopy},
	url = {https://m2.mtmt.hu/api/publication/34409105},
	author = {Karner, Victoria and Jancsó, Attila and Hemmingsen, Lars},
	doi = {10.3390/inorganics11100375},
	journal-iso = {INORGANICS},
	journal = {INORGANICS},
	volume = {11},
	unique-id = {34409105},
	abstract = {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).},
	year = {2023},
	eissn = {2304-6740},
	orcid-numbers = {Karner, Victoria/0000-0002-2915-2652; Jancsó, Attila/0000-0003-2362-0758; Hemmingsen, Lars/0000-0002-1823-3035}
}

@article{MTMT:34393301,
	title = {Revisiting the hydrolysis of ampicillin catalyzed by Temoneira-1 β-lactamase, and the effect of Ni(II), Cd(II) and Hg(II)},
	url = {https://m2.mtmt.hu/api/publication/34393301},
	author = {Nafaee, Zeyad Hasan Abdullah and Egyed, Viktória and Jancsó, Attila and Tóth, Annamária and Gerami, Adeleh Mokhles and Dang, Thanh Thien and Heiniger-Schell, Juliana and Hemmingsen, Lars and Hunyadi-Gulyás Éva, Csilla and Peintler, Gábor and Gyurcsik, Béla},
	doi = {10.1002/pro.4809},
	journal-iso = {PROTEIN SCI},
	journal = {PROTEIN SCIENCE},
	volume = {32},
	unique-id = {34393301},
	issn = {0961-8368},
	abstract = {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.},
	keywords = {Mass spectrometry; Circular Dichroism; Reaction kinetics; 199mHg perturbed angular correlation spectroscopy of γ-rays; TEM-1 β-lactamase; toxic metal binding},
	year = {2023},
	eissn = {1469-896X},
	orcid-numbers = {Jancsó, Attila/0000-0003-2362-0758; Peintler, Gábor/0000-0001-5171-5346; Gyurcsik, Béla/0000-0003-1894-7414}
}

@article{MTMT:33767799,
	title = {Tristhiolato Pseudopeptides Bind Arsenic(III) in an AsS 3 Coordination Environment Imitating Metalloid Binding Sites in Proteins},
	url = {https://m2.mtmt.hu/api/publication/33767799},
	author = {Szekeres, Levente István and Maldivi, Pascale and Lebrun, Colette and Gateau, Christelle and Mesterházy, Edit and Delangle, Pascale and Jancsó, Attila},
	doi = {10.1021/acs.inorgchem.3c00563},
	journal-iso = {INORG CHEM},
	journal = {INORGANIC CHEMISTRY},
	volume = {62},
	unique-id = {33767799},
	issn = {0020-1669},
	abstract = {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.},
	year = {2023},
	eissn = {1520-510X},
	pages = {6817-6824},
	orcid-numbers = {Maldivi, Pascale/0000-0003-2008-1090; Mesterházy, Edit/0000-0003-0856-6685; Delangle, Pascale/0000-0002-8546-9080; Jancsó, Attila/0000-0003-2362-0758}
}

@article{MTMT:32924475,
	title = {Tying Up a Loose End: On the Role of the C‐Terminal CCHHRAG Fragment of the Metalloregulator CueR},
	url = {https://m2.mtmt.hu/api/publication/32924475},
	author = {Balogh, Ria Katalin and Gyurcsik, Béla and Jensen, Mikael and Thulstrup, Peter W. and Köster, Ulli and Christensen, Niels Johan and Jensen, Marianne L. and Hunyadi-Gulyás Éva, Csilla and Hemmingsen, Lars and Jancsó, Attila},
	doi = {10.1002/cbic.202200290},
	journal-iso = {CHEMBIOCHEM},
	journal = {CHEMBIOCHEM},
	volume = {23},
	unique-id = {32924475},
	issn = {1439-4227},
	year = {2022},
	eissn = {1439-7633},
	orcid-numbers = {Gyurcsik, Béla/0000-0003-1894-7414; Jancsó, Attila/0000-0003-2362-0758}
}

@article{MTMT:32924465,
	title = {Magnesium(II)‐ATP Complexes in 1‐Ethyl‐3‐Methylimidazolium Acetate Solutions Characterized by 31Mg β‐Radiation‐Detected NMR Spectroscopy},
	url = {https://m2.mtmt.hu/api/publication/32924465},
	author = {McFadden, Ryan M. L. and Szunyogh, Dániel and Bravo-Frank, Nicholas and Chatzichristos, Aris and Dehn, Martin H. and Fujimoto, Derek and Jancsó, Attila and Johannsen, Silke and Kálomista, Ildikó and Karner, Victoria L. and Kiefl, Robert F. and Larsen, Flemming H. and Lassen, Jens and Levy, C. D. Philip and Li, Ruohong and McKenzie, Iain and McPhee, Hannah and Morris, Gerald D. and Pearson, Matthew R. and Sauer, Stephan P. A. and Sigel, Roland K. O. and Thulstrup, Peter W. and MacFarlane, W. Andrew and Hemmingsen, Lars and Stachura, Monika},
	doi = {10.1002/anie.202207137},
	journal-iso = {ANGEW CHEM INT EDIT},
	journal = {ANGEWANDTE CHEMIE-INTERNATIONAL EDITION},
	volume = {61},
	unique-id = {32924465},
	issn = {1433-7851},
	year = {2022},
	eissn = {1521-3773},
	orcid-numbers = {Jancsó, Attila/0000-0003-2362-0758}
}

@{MTMT:32685955,
	title = {Metal ion binding and Ca2+-promoted fluorescence of bis(diethylamino)xanthene-labelled BAPTA analogues},
	url = {https://m2.mtmt.hu/api/publication/32685955},
	author = {Csomos, Attila and Kontra, Bence and Kovács, Ervin and Tóth, Annamária and Galbács, Gábor and Sajdik, Kadosa and Jancsó, Attila and Mucsi, Zoltán},
	booktitle = {ISMEC 2021 International Symposium on Thermodynamics of Metal Complexes},
	unique-id = {32685955},
	year = {2021},
	orcid-numbers = {Kovács, Ervin/0000-0002-3939-6925; Galbács, Gábor/0000-0002-1799-5329; Jancsó, Attila/0000-0003-2362-0758}
}

@misc{MTMT:32685853,
	title = {Ca2+-érzékelőkben potenciálisan alkalmazható módosított BAPTA származékok Ca2+ - és Mg2+ -kötő sajátságai},
	url = {https://m2.mtmt.hu/api/publication/32685853},
	author = {Tóth, Annamária and Csomos, Attila and Kontra, Bence and Kovács, Ervin and Galbács, Gábor and Mucsi, Zoltán and Jancsó, Attila},
	unique-id = {32685853},
	abstract = {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.},
	year = {2021},
	orcid-numbers = {Kontra, Bence/0000-0001-8293-3637; Kovács, Ervin/0000-0002-3939-6925; Galbács, Gábor/0000-0002-1799-5329; Mucsi, Zoltán/0000-0003-3224-8847; Jancsó, Attila/0000-0003-2362-0758}
}

@article{MTMT:32399352,
	title = {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},
	url = {https://m2.mtmt.hu/api/publication/32399352},
	author = {Kovács, Ervin and Cseri, Levente and Jancsó, Attila and Terényi, Ferenc and Fülöp, Anna and Rózsa J., Balázs and Galbács, Gábor and Mucsi, Zoltán},
	doi = {10.1002/ejoc.202101173},
	journal-iso = {EUR J ORG CHEM},
	journal = {EUROPEAN JOURNAL OF ORGANIC CHEMISTRY},
	volume = {2021},
	unique-id = {32399352},
	issn = {1434-193X},
	abstract = {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.},
	keywords = {ESIPTFluorescenceGFP analoguesStokes shiftTwo-photon fluorescence},
	year = {2021},
	eissn = {1099-0690},
	pages = {5649-5660},
	orcid-numbers = {Kovács, Ervin/0000-0002-3939-6925; Jancsó, Attila/0000-0003-2362-0758; Galbács, Gábor/0000-0002-1799-5329; Mucsi, Zoltán/0000-0003-3224-8847}
}

@article{MTMT:32187933,
	title = {A comprehensive study of the Ca2+ ion binding of fluorescently labelled BAPTA analogues},
	url = {https://m2.mtmt.hu/api/publication/32187933},
	author = {Csomos, Attila and Kontra, Bence and Jancsó, Attila and Galbács, Gábor and Deme, Ruth and Kele, Zoltán and Rózsa J., Balázs and Kovács, Ervin and Mucsi, Zoltán},
	doi = {10.1002/ejoc.202100948},
	journal-iso = {EUR J ORG CHEM},
	journal = {EUROPEAN JOURNAL OF ORGANIC CHEMISTRY},
	volume = {2021},
	unique-id = {32187933},
	issn = {1434-193X},
	abstract = {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.},
	keywords = {Calcium ChelatesDensity functional calculationsDyesFluorescent probes},
	year = {2021},
	eissn = {1099-0690},
	pages = {5248-5261},
	orcid-numbers = {Kontra, Bence/0000-0001-8293-3637; Jancsó, Attila/0000-0003-2362-0758; Galbács, Gábor/0000-0002-1799-5329; Deme, Ruth/0000-0002-0798-6912; Kele, Zoltán/0000-0002-4401-0302; Kovács, Ervin/0000-0002-3939-6925; Mucsi, Zoltán/0000-0003-3224-8847}
}

@article{MTMT:32000256,
	title = {Binding Models of Copper(II) Thiosemicarbazone Complexes with Human Serum Albumin: A Speciation Study},
	url = {https://m2.mtmt.hu/api/publication/32000256},
	author = {May, Nóra Veronika and Jancsó, Attila and Enyedy, Éva Anna},
	doi = {10.3390/molecules26092711},
	journal-iso = {MOLECULES},
	journal = {MOLECULES},
	volume = {26},
	unique-id = {32000256},
	issn = {1420-3049},
	year = {2021},
	eissn = {1420-3049},
	orcid-numbers = {May, Nóra Veronika/0000-0003-4770-4681; Jancsó, Attila/0000-0003-2362-0758; Enyedy, Éva Anna/0000-0002-8058-8128}
}