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首页> 外文期刊>Spectrochimica acta, Part A. Molecular and biomolecular spectroscopy >Comparison of energy interaction parameters for the complexation of Pr(III) with glutathione reduced (GSH) in absence and presence of Zn(II) in aqueous and aquated organic solvents using 4f-4f transition spectra as PROBE
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Comparison of energy interaction parameters for the complexation of Pr(III) with glutathione reduced (GSH) in absence and presence of Zn(II) in aqueous and aquated organic solvents using 4f-4f transition spectra as PROBE

机译:使用4f-4f跃迁谱作为PROBE,比较在水和水合有机溶剂中不存在和存在Zn(II)时Pr(III)与谷胱甘肽还原(GSH)络合的能量相互作用参数

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摘要

The coordination chemistry of glutathione reduced (GSH) is of great importance as it acts as excellent model system for the binding of metal ions. The GSH complexation with metal ions is involved in the toxicology of different metal ions. Its coordination behaviour for soft metal ions and hard metal ions is found different because of the structure of GSH and its different potential binding sites. In our work we have studied two chemically dissimilar metal ions viz. Pr(III), which prefer hard donor site like carboxylic groups and Zn(II) the soft metal ion which prefer peptide-NH and sulphydryl groups. The absorption difference and comparative absorption spectroscopy involving 4f-4f transitions of the heterobimetallic Complexation of GSH with Pr(III) and Zn(11) has been explored in aqueous and aquated organic solvents. The variation in the energy parameters like Slater-Condon (F-K), Racah (E-K) and Lande (xi(4f)) Nephelauxetic parameter (beta) and bonding parameter (b(1/2)) are computed to explain the nature of complexation. (c) 2004 Elsevier B.V. All rights reserved.
机译:谷胱甘肽还原(GSH)的配位化学非常重要,因为它是结合金属离子的出色模型系统。 GSH与金属离子的络合涉及不同金属离子的毒理学。由于GSH的结构及其潜在的结合位点不同,发现其对软金属离子和硬金属离子的配位行为不同。在我们的工作中,我们研究了两种化学不同的金属离子,即。 Pr(III),它更喜欢硬的供体位点,例如羧基; Zn(II),它是柔软的金属离子,它们更喜欢肽-NH和巯基。在含水和水合有机溶剂中,研究了GSH与Pr(III)和Zn(11)的异双金属络合物的4f-4f跃迁的吸收差异和比较吸收光谱。计算能量参数的变化,例如Slater-Condon(FK),Racah(EK)和Lande(xi(4f))肾上腺素参数(beta)和键合参数(b(1/2)),以解释络合的性质。 (c)2004 Elsevier B.V.保留所有权利。

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