Study on the Interaction of Pentachlorophenol with Urease in Aqueous Solution by Multiple Spectroscopic Techniques

Wang, Yan-Qing; Zhang, Gencheng; Zhang, Hongmei

doi:10.1007/s10953-011-9664-8

Cited by 14 publications

(6 citation statements)

References 27 publications

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“…The binding constant (K b ) expresses the strength of interaction between a ligand and a due protein and for the case of lichen metabolites it was found that the interaction between (R)-(+)-UA (1) and urease was stronger than that of (S)-(-)-UA (2) and FPA (3) ( Table 2). The K b values for lichen compounds 1-3 toward urease were in the same Please do not adjust margins Please do not adjust margins range of those reported for the interaction between pentachlorophenol (3.85×10 3 M -1 at 32 o C), 26 K 2 Cr 2 O 7 (1.96×10 4 M -1 at 29 o C) 31 and Cu(II) (3.89×10 5 M -1 at 37 o C for [Cu(II)] < 16 µM) 32 and jack bean urease. However, these authors did not evaluate the potential of pentachlorophenol, K 2 Cr 2 O 7 and Cu(II) as urease inhibitors.…”

Section: Interaction Between Lichen Secondary Metabolites and Jack Besupporting

confidence: 72%

In vitroinhibition ofHelicobacter pyloriand interaction studies of lichen natural products with jack bean urease

et al. 2018

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Section: Interaction Between Lichen Secondary Metabolites and Jack Besupporting

confidence: 72%

In vitroinhibition ofHelicobacter pyloriand interaction studies of lichen natural products with jack bean urease

et al. 2018

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“…3(b), fluorescence peaks from tryptophan residues had l max(ex) /l max(em) = 280 nm/340 nm, ΔF = 2881. 80 nm) changed, it was presumed that the conformation of pepsin was changed (18,19). 3c).…”

Section: Resultsmentioning

confidence: 99%

“…350 nm) and Stokes shift (60 nm ! 80 nm) changed, it was presumed that the conformation of pepsin was changed (18,19).…”

Section: Resultsmentioning

confidence: 99%

Fluorescence spectroscopic analysis on interaction of fleroxacin with pepsin

et al. 2013

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The interaction between fleroxacin (FLX) and pepsin was investigated by spectrofluorimetry. The effects of FLX on pepsin showed that the microenvironment of tryptophan residues and molecular conformation of pepsin were changed based on fluorescence quenching and synchronous fluorescence spectroscopy in combination with three-dimensional fluorescence spectroscopy. Static quenching was suggested and it was proved that the fluorescence quenching of pepsin by FLX was related to the formation of a new complex and a non-radiation energy transfer. The quenching constants KSV , binding constants K and binding sites n were calculated at different temperatures. The molecular interaction distance (r = 6.71) and energy transfer efficiency (E = 0.216) between pepsin and FLX were obtained according to the Forster mechanism of non-radiation energy transfer. Hydrophobic and electrostatic interaction played a major role in FLX-pepsin association. In addition, the hydrophobic interaction and binding free energy were further tested by molecular modeling study.

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“…This intensity decrease was accompanied by a large shift and apparent splitting of the maximum emission wavelength from 357 nm to 380 nm and 323 nm in the presence of 30.00 × 10 −6 M concentrations of 2,4-DNP. The large displacement of the maximum emission wavelength could be due to the hydrophilic or hydrophobic character of the compounds [ 22 , 23 ], thus the theoretical logP was calculated using the specialized Quantitative Structure-Activity Relationship (QSAR) module of the software HyperChem 7.5. Tryptophan has a logP equal to 0.06, 2,4-DNP 1.67 and 2,4-DNP:Tryp complex 0.65.…”

Section: Resultsmentioning

confidence: 99%

Quenching of Tryptophan Fluorescence in the Presence of 2,4-DNP, 2,6-DNP, 2,4-DNA and DNOC and Their Mechanism of Toxicity

2013

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Although they are widely used as insecticides, acaricides and fungicides in the agriculture or as raw materials in the dye industry, dinitrophenols (DNPs) are extremely noxious, death cases having been registered. These compounds produce cataracts, lower leucocyte levels, disturb the general metabolism and can cause cancer. It is also assumed that DNPs hinder the proton translocation through the mitochondrial inner membrane and therefore inhibit oxidative phosphorylation. Their fluorescence quenching properties can help understand and explain their toxicity. Fluorescence quenching of tryptophan was tested using different dinitrophenols such as 2,4-dinitrophenol (2,4-DNP), 4,6-dinitro-orthocresol (DNOC), 2-[(2,4-dinitrophenyl)amino]acetic acid (GlyDNP), 2-(1-methyl-heptyl)-4.6-dinitrophenyl crotonate (Karathan), 2-amino-5-[(1-((carboxymethyl)amino)-3-((2,4-dinitrophenyl)thio)-1-oxopropan-2-yl)amino]-5-oxopentanoic acid (SDN GSH), 2,4-dinitroanisole (2,4-DNA) and 2,4-dinitrobenzoic acid (2,4-DNB). 2,4-DNP and DNOC showed the highest tryptophan fluorescence quenching constant values, these being also the most toxic compounds. The electronic chemical potential value of the most stable complex of 2,4-DNP-with tryptophan is higher than the values of the electronic chemical potentials of complexes corresponding to the derivatives.

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Study on the Interaction of Pentachlorophenol with Urease in Aqueous Solution by Multiple Spectroscopic Techniques

Cited by 14 publications

References 27 publications

In vitroinhibition ofHelicobacter pyloriand interaction studies of lichen natural products with jack bean urease

In vitroinhibition ofHelicobacter pyloriand interaction studies of lichen natural products with jack bean urease

Fluorescence spectroscopic analysis on interaction of fleroxacin with pepsin

Quenching of Tryptophan Fluorescence in the Presence of 2,4-DNP, 2,6-DNP, 2,4-DNA and DNOC and Their Mechanism of Toxicity

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