Synthesis, structures and urease inhibition studies of copper(II) and nickel(II) complexes with bidentate N,O-donor Schiff base ligands

Dong, Xiongwei; Li, Yuguang; Li, Zuowen; Cui, Yuming; Zhu, Hai‐Liang

doi:10.1016/j.jinorgbio.2011.12.006

Cited by 78 publications

(13 citation statements)

References 48 publications

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“…The results indicate that the inhibitory efficiency of the complex towards urease may be influenced by the transition metal and ligands, and the inhibitory activity probably is due to strong Lewis acid properties of copper ions and the ligands strengthen the inhibitory activity of the complexes. The results are in accord with those reported previously, where some Cu(II) complexes have stronger urease inhibitory activities to urease than their parent ligands and metal ion, with IC 50 ranging from 1 to 50 μM [15,28,[35][36][37][38][39]. Compared with the data reported before, the complexes reported in this study exhibit fairly strong inhibitory activity to urease and may be used as urease inhibitors.…”

Section: Resultssupporting

confidence: 92%

Synthesis, structure, and urease inhibitory activities of three binuclear copper(II) complexes with protocatechuic acid derivative

Sheng

Zhou

Sun

et al. 2014

Journal of Coordination Chemistry

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3), with a ligand derived from protocatechuic acid (HL 1 = C 9 H 8 O 4 =2,3-dihydrobenzo[b][1,4]-dioxine-6-carboxylic acid, L 2 = C 7 H 9 N=o-toluidine, L 3 = C 6 H 16 N 2 =N,N-diethylethylenediamine) were synthesized and characterized by C, H, and N elemental analysis and single-crystal X-ray diffraction, which revealed that the three complexes have similar binuclear structures. Complexes 1 and 3 crystallized in triclinic space group P-1 and 2 in orthorhombic space group P2 1 2 1 2 1 . The urease inhibitory activities of the three complexes were tested. All three complexes showed strong inhibitory activity against jack bean urease with an IC 50 value of 6.8, 5.5, and 3.5 μM compared with the acetohydroxamic acid (IC 50 = 7.5 μM), which was a positive control.

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Section: Resultssupporting

confidence: 92%

Synthesis, structure, and urease inhibitory activities of three binuclear copper(II) complexes with protocatechuic acid derivative

Sheng

Zhou

Sun

et al. 2014

Journal of Coordination Chemistry

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“…Urease inhibitors contain two general classifications, including pure organic based compounds and organic compounds, in ligation with transition metals, as some transition metals themselves possess a slight urease inhibition potential [11]. The literature survey showed excellent urease inhibition potential for candidates exhibiting hydroxamic acids, phosphoramides, and thiols’ skeleton [12]. Compounds with thiol functional groups inhibit urease competitively in their thiolate anion form, R-S − [13].…”

Section: Introductionmentioning

confidence: 99%

Symmetrical Heterocyclic Cage Skeleton: Synthesis, Urease Inhibition Activity, Kinetic Mechanistic Insight, and Molecular Docking Analyses

et al. 2019

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The present study focuses on the design and synthesis of a cage-like organic skeleton containing two triazole rings jointed via imine linkage. These molecules can act as urease inhibitors. The in-vitro urease inhibition screening results showed that the combination of the two triazole skeleton in the cage-like morphology exhibited comparable urease inhibition activity to that of the reference thiourea while the metallic complexation, especially with copper, nickel, and palladium, showed excellent activity results with IC50 values of 0.94 ± 0.13, 3.71 ± 0.61, and 7.64 ± 1.21 (3a–c), and 1.20 ± 0.52, 3.93 ± 0.45, and 12.87 ± 2.11 µM (4a–c). However, the rest of compounds among the targeted series exhibited a low to moderate enzyme inhibition potential. To better understand the compounds’ underlying mechanisms of the inhibitory effect (3a and 4a) and their most active metal complexes (3b and 4b), we performed an enzymatic kinetic analysis using the Lineweaver–Burk plot in the presence of different concentrations of inhibitors to represent the non-competitive inhibition nature of the compounds, 3a, 4a, and 4b, while mixed type inhibition was represented by the compound, 3b. Moreover, molecular docking confirmed the binding interactive behavior of 3a within the active site of the target protein.

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“…The enzyme is widely distributed in nature and is found in a variety of plants, algae, fungi, bacteria and soil [1-3]. Thus, urease plays an important role in the nitrogen metabolism of many microorganism and plants [4,5]. Despite the great importance of urease in biotechnology and medicine and also continuous interest in many laboratories [6-11], the mechanisms of hydrolysis of the metal active site of the enzyme have not been studied in detail [12].…”

Section: Introductionmentioning

confidence: 99%

Kinetics and mechanism of jack bean urease inhibition by Hg2+

Chen

Liu

et al. 2012

Chemistry Central Journal

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BackgroundJack bean urease (EC 3.5.1.5) is a metalloenzyme, which catalyzes the hydrolysis of urea to produce ammonia and carbon dioxide. The heavy metal ions are common inhibitors to control the rate of the enzymatic urea hydrolysis, which take the Hg2+ as the representative. Hg2+ affects the enzyme activity causing loss of the biological function of the enzyme, which threatens the survival of many microorganism and plants. However, inhibitory kinetics of urease by the low concentration Hg2+ has not been explored fully. In this study, the inhibitory effect of the low concentration Hg2+ on jack bean urease was investigated in order to elucidate the mechanism of Hg2+ inhibition.ResultsAccording to the kinetic parameters for the enzyme obtained from Lineweaver–Burk plot, it is shown that the Km is equal to 4.6±0.3 mM and Vm is equal to 29.8±1.7 μmol NH3/min mg. The results show that the inhibition of jack bean urease by Hg2+ at low concentration is a reversible reaction. Equilibrium constants have been determined for Hg2+ binding with the enzyme or the enzyme-substrate complexes (Ki =0.012 μM). The results show that the Hg2+ is a noncompetitive inhibitor. In addition, the kinetics of enzyme inhibition by the low concentration Hg2+ has been studied using the kinetic method of the substrate reaction. The results suggest that the enzyme first reversibly and quickly binds Hg2+ and then undergoes a slow reversible course to inactivation. Furthermore, the rate constant of the forward reactions (k+0) is much larger than the rate constant of the reverse reactions (k-0). By combining with the fact that the enzyme activity is almost completely lost at high concentration, the enzyme is completely inactivated when the Hg2+ concentration is high enough.ConclusionsThese results suggest that Hg2+ has great impacts on the urease activity and the established inhibition kinetics model is suitable.

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Synthesis, structures and urease inhibition studies of copper(II) and nickel(II) complexes with bidentate N,O-donor Schiff base ligands

Cited by 78 publications

References 48 publications

Synthesis, structure, and urease inhibitory activities of three binuclear copper(II) complexes with protocatechuic acid derivative

Synthesis, structure, and urease inhibitory activities of three binuclear copper(II) complexes with protocatechuic acid derivative

Symmetrical Heterocyclic Cage Skeleton: Synthesis, Urease Inhibition Activity, Kinetic Mechanistic Insight, and Molecular Docking Analyses

Kinetics and mechanism of jack bean urease inhibition by Hg2+

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