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首页> 外文期刊>Inorganic Chemistry Communications >Characterisation of a coordinated imidazole as a structural model for superoxide dismutase
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Characterisation of a coordinated imidazole as a structural model for superoxide dismutase

机译:配位咪唑的表征作为超氧化物歧化酶的结构模型

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The copper complex [Cu(HL)](ClO_4)_2 (centor dot) 2H_2O, where HL is N-[2-(4,7-dimethyl-1,4,7-triazacyclonon-1-yl)ethyl]-N-(benzimidazol-2-yl)methanimine, has been prepared and characterized by X-ray crystallography and solution absorption spectroscopy. Deprotonation of the benzimidazole moiety in this complex has been investigated by electronic spectroscopy. The results show a definite shift in #lambda#_(max) for [Cu(HL)]~(2+), at 632-818 nm for the deprotonated [CuL]~+, in acetonitrile. This complex has been synthesized as a structural homologue to half of the enzyme u-Zn superoxide dismutase (SOD) which contains a bridged imidazolate moiety between the two Cu and Zn metal ions.
机译:铜络合物[Cu(HL)](ClO_4)_2(中心点)2H_2O,其中HL为N- [2-(4,7-二甲基-1,4,7-三氮杂环壬-1-基)乙基] -N已经制备了-(苯并咪唑-2-基)甲亚胺,并通过X射线晶体学和溶液吸收光谱对其进行了表征。苯并咪唑部分在该配合物中的去质子化已经通过电子光谱法进行了研究。结果表明,对于[Cu(HL)]〜(2+),去质子化的[CuL]〜+在乙腈中,在#lambda #_(max)中有明确的偏移。该复合物已作为与u-Zn超氧化物歧化酶(SOD)的一半酶的结构同源物合成,该酶在两个Cu和Zn金属离子之间包含桥连的咪唑酸酯部分。

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