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EnglishSoft metal ions can inactivate urease, a Ni(II)-dependent enzyme whose hydrolytic activity has significant im-plications in agro-environmental science and human health. Kinetic and structural studies of the reaction of Canavalia ensiformis urease (JBU) and Sporosarcina pasteurii urease (SPU) with Ag(I) compounds of general formula [Ag(PEt3)X]4 (X =Cl, Br, I), and with the ionic species [Ag(PEt3)2]NO3, revealed the role of the Ag(I) ion and its ligands in modulating the metal-enzyme interaction. The activity of JBU is obliterated by the [Ag(PEt3) X]4 complexes, with IC50 values in the nanomolar range; the efficiency of the inhibition increases in the Cl
| Titolo: | Kinetic and structural analysis of the inactivation of urease by mixed-ligand phosphine halide Ag(I) complexes | |
| Autore/i: | Luca Mazzei; Damiano Cirri; Michele Cianci; Luigi Messori; Stefano Ciurli | |
| Autore/i Unibo: | ||
| Anno: | 2021 | |
| Rivista: | ||
| Digital Object Identifier (DOI): | http://dx.doi.org/10.1016/j.jinorgbio.2021.111375 | |
| Abstract: | Soft metal ions can inactivate urease, a Ni(II)-dependent enzyme whose hydrolytic activity has significant im-plications in agro-environmental science and human health. Kinetic and structural studies of the reaction of Canavalia ensiformis urease (JBU) and Sporosarcina pasteurii urease (SPU) with Ag(I) compounds of general formula [Ag(PEt3)X]4 (X =Cl, Br, I), and with the ionic species [Ag(PEt3)2]NO3, revealed the role of the Ag(I) ion and its ligands in modulating the metal-enzyme interaction. The activity of JBU is obliterated by the [Ag(PEt3) X]4 complexes, with IC50 values in the nanomolar range; the efficiency of the inhibition increases in the Cl | |
| Data stato definitivo: | 2021-10-25T11:13:45Z | |
| Appare nelle tipologie: | 1.01 Articolo in rivista |
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