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首页> 外文期刊>Dalton transactions: An international journal of inorganic chemistry >Ferutinin as a Ca2+ complexone: lipid bilayers, conductometry, FT-IR, NMR studies and DFT-B3LYP calculations
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Ferutinin as a Ca2+ complexone: lipid bilayers, conductometry, FT-IR, NMR studies and DFT-B3LYP calculations

机译：Ferutinin作为Ca2 +络合物：脂质双层，电导，FT-IR，NMR研究和DFT-B3LYP计算

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Calcium ionophoretic properties of ferutinin were re-evaluated in solvent-containing bilayer lipid membranes. The slopes of conductance-concentration curves suggest that in the presence of a solvent in the membrane the majority of complexes appear to consist of a single terpenoid molecule bound to one Ca ion. By contrast, the stoichiometry of ferutinin-Ca2+ complexes in acetone determined using the conductometric method was 2 : 1. While the cation-cation selectivity of ferutinin did not change, the cationanion selectivity slightly decreased in solvent containing membranes. FT-IR and NMR data together with DFT calculations at the B3LYP/6-31G(d) level of theory indicate that in the absence of Ca ions ferutinin molecules are hydrogen-bonded at the phenol hydroxyl groups. The variations of absorption assigned to -OH and -C-O stretching mode suggest that ferutinin interacts strongly with Ca ions via the hydroxyl group of ferutinol and carboxyl oxygen of the complex ether bond. The coordination through the carbonyl group of ferutinin was demonstrated by theoretical calculations. Taken together, ferutinin molecules form H-bonded dimers, while complexation of Ca2+ by ferutinin ruptures this hydrogen bond due to spatial re-orientation of the ferutinin molecules from parallel to antiparallel alignment.
机译：在含溶剂的双层脂质膜中重新评估了铁白蛋白的钙离子电性质。电导浓度曲线的斜率表明，在膜中存在溶剂的情况下，大多数复合物似乎由结合到一个Ca离子上的单个萜类分子组成。相比之下，使用电导法测定的丙酮中的Ferutinin-Ca2 +配合物的化学计量比为2：1。尽管Ferutinin的阳离子-阳离子选择性没有变化，但含溶剂的膜中的阳离子阴离子选择性略有下降。 FT-IR和NMR数据以及在理论上B3LYP / 6-31G（d）的DFT计算表明，在不存在Ca离子的情况下，Ferutinin分子氢键合在酚羟基上。分配给-OH和-C-O拉伸模式的吸收变化表明，Ferutinin通过Ferutinol的羟基和复杂醚键的羧基氧与Ca离子强烈相互作用。通过理论计算证明了通过阿魏白蛋白的羰基的配位。总的来说，Ferutinin分子形成H键合的二聚体，而由于Ferutinin分子从平行到反平行排列的空间重新取向，则Ferutinin的Ca2 +络合使氢键断裂。

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