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
Mazzei, L., Cirri, D., Cianci, M., Messori, L., Ciurli, S. (2021). Kinetic and structural analysis of the inactivation of urease by mixed-ligand phosphine halide Ag(I) complexes. JOURNAL OF INORGANIC BIOCHEMISTRY, 218, 1-9 [10.1016/j.jinorgbio.2021.111375].
Kinetic and structural analysis of the inactivation of urease by mixed-ligand phosphine halide Ag(I) complexes
Luca Mazzei
;Stefano Ciurli
2021
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| File | Dimensione | Formato | |
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Paper_AgP_REV (1).docx
Open Access dal 30/01/2023
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