Effect of La3+ on structure and electrochemical reaction of microperoxidase-11 in imitated physiological solution

Huang, Xiaohua; Guo, Shuntang; Zhou, Qing; Lu, Tianhong; Ding, Xifeng

doi:10.1016/j.jelechem.2006.10.017

Cited by 9 publications

(3 citation statements)

References 64 publications

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“…From Fig. 1a-c, it is shown that the peak current (ip) varies with the different scan rate (10-100 mV) and is significantly correlated with the square root of scan rate (v 1/2 ) [31,32]. In Fig.…”

Section: H Nmr Spectramentioning

confidence: 89%

Studies on DNA Interactions and Biological Activities of Lanthanum(III) Complexes with 4-Quinoline Terpyridine and 1,10-Phenanthroline

et al. 2019

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A series of lanthanum(III) complexes [La(4-qtpy)2(NO3)2](NO3) (1), [La(4-qtpy)3(NO3)](NO3)2 (2), [La(4-qtpy)(phen)(NO3)2](NO3) (3) and [La(4-qtpy)(phen)2(NO3)2](NO3) (4) (4-qtpy = 4′-[(4-quinoline)-2,2′;6′,2′′-terpyridine]) were synthesized and characterized. The cyclic voltammetric studies revealed that the complexes 1 and 3 are redox active. UV-visible absorption spectral studies and viscosity measurements revealed that complexes bind to DNA through intercalation. Complexes 1 and 3 have shown the highest binding propensity (Kb = 4.241 + 0.2 × 106 for 1 and 1.492 + 0.2 × 106 for 3). The results of chemical nuclease studies revealed that the complexes 3 and 4 have shown maximum chemical nuclease activity in the presence of H2O2 and the mechanism involves hydroxyl radicals. The antibacterial activities of the complexes 1 to 4 were tested against Gram positive and Gram negative bacteria in which complex 3 shows comparable results with the standard antibiotic tetracycline. The cytotoxic activities of 4-qtpy and complex 4 were done by MTT assay against HeLa cell lines.

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Section: H Nmr Spectramentioning

confidence: 89%

Studies on DNA Interactions and Biological Activities of Lanthanum(III) Complexes with 4-Quinoline Terpyridine and 1,10-Phenanthroline

et al. 2019

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“…Meanwhile, Tb 4d5/2 Table 2). The increase in the average binding energy of O 1s and S 2p3/2 in the Tb III -HRP complex indicated the decrease in the electron density of O 1s and S 2p3/2 in the HRP molecule, while the decrease in the average binding energy of N 1s and Tb 4d5/2 illustrated the increase in the electron density of N 1s and Tb 4d5/2 [14]. Thus, the above results suggested that a coordinate covalent bond between Tb, and O or S is formed.…”

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confidence: 98%

“…Thus, Tb III would first interact with O in the amide groups in the peptide of HRP. In fact, since the heme group and S-atoms are embedded below the molecular surface, Tb III may only interact with amide groups in the peptide of the HRP molecule, inducing the increase in planarity of the porphyrin cycle in the heme group [14]. Then, the increase in planarity of the porphyrin cycle in the heme group would cause an increase in the conjugation between the porphyrin cycle and S [14], leading to a decrease in the electron density of S. The above results indicated that Tb III interacts with HRP by covalent bonds.…”

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confidence: 99%

Inhibition Mechanism of Tb^III on Horseradish Peroxidase Activity

Guo

Zhou

et al. 2008

Chemistry & Biodiversity

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The inhibition mechanism of Tb(III) on horseradish peroxidase (HRP) in vitro was discussed. The results from MALDI-TOF/MS and X-ray photoelectron spectroscopy (XPS) showed that Tb(III) mainly interacts with the O-containing groups of the amides in the polypeptide chains of the HRP molecules and forms the complex of Tb(III)-HRP, and, in the complex, the molar ratio Tb(III)/HRP is 2 : 1. The results from CD and atomic force microscopy (AFM) indicated that the coordination effect between Tb(III) and HRP can lead to the conformation change in the HRP molecule, in which the contents of alpha-helix and beta-sheet conformation in the peptide of the HRP molecules is decreased, and the content of the random coil conformation is increased. Meanwhile, the coordination effect also leads to the decrease in the content of inter- and intrapeptide-chain H-bonds in the HRP molecules, resulting in the HRP molecular looseness and/or aggregation. Thus, the conformation change in the HRP molecules can significantly decrease the electrochemical reaction of HRP and its electrocatalytic activity for the reduction of H2O2.

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Molecular and cellular mechanism of the effect of La(III) on horseradish peroxidase

Wang

Zhou

et al. 2010

J Biol Inorg Chem

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Horseradish is an important economic crop. It contains horseradish peroxidase (HRP) and lots of nutrients, and has specific pungency. Lanthanum is one of the heavy metals in the environment. It can transfer through the food chain to humans. In this paper, the molecular and cellular mechanism of the toxic effects of La(III) on HRP in vivo was investigated with an optimized combination of biophysical, biochemical, and cytobiological methods. It was found that La(III) could interact with O and/or N atoms in the backbone/side chains of the HRP molecule in the cell membrane of horseradish treated with 80 microM La(III), leading to the formation of a new complex of La and HRP (La-HRP). The formation of the La-HRP complex causes the redistribution of the electron densities of atoms in the HRP molecule, especially the decrease in the electron density of the active center, Fe(III), in the heme group of the La-HRP molecule compared with the native HRP molecule in vivo. Therefore, the electron transfer and the activity of HRP in horseradish treated with 80 microM La(III) are obviously decreased compared with those of the native HRP in vivo. This is a possible molecular and cellular mechanism for the toxic effect of La(III) on HRP in vivo. It is suggested that the accumulation of La in the environment, especially the formation of the La-HRP complex in vivo, is harmful to organisms.

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Effect of La3+ on structure and electrochemical reaction of microperoxidase-11 in imitated physiological solution

Cited by 9 publications

References 64 publications

Studies on DNA Interactions and Biological Activities of Lanthanum(III) Complexes with 4-Quinoline Terpyridine and 1,10-Phenanthroline

Studies on DNA Interactions and Biological Activities of Lanthanum(III) Complexes with 4-Quinoline Terpyridine and 1,10-Phenanthroline

Inhibition Mechanism of Tb^III on Horseradish Peroxidase Activity

Molecular and cellular mechanism of the effect of La(III) on horseradish peroxidase

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Effect of La3+ on structure and electrochemical reaction of microperoxidase-11 in imitated physiological solution

Cited by 9 publications

References 64 publications

Studies on DNA Interactions and Biological Activities of Lanthanum(III) Complexes with 4-Quinoline Terpyridine and 1,10-Phenanthroline

Studies on DNA Interactions and Biological Activities of Lanthanum(III) Complexes with 4-Quinoline Terpyridine and 1,10-Phenanthroline

Inhibition Mechanism of TbIII on Horseradish Peroxidase Activity

Molecular and cellular mechanism of the effect of La(III) on horseradish peroxidase

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Inhibition Mechanism of Tb^III on Horseradish Peroxidase Activity