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[利用三重态交换失活现象研究蛋白质的结构和电子传导性]

[Use of triplet state exchange disactivation phenomenon for the study of structure and electron conductivity of proteins].

作者信息

Kotel'nikov A I, Fogel' V R, Likhtenshteĭn G I, Postnikova G B, Shliapnikova E A

出版信息

Mol Biol (Mosk). 1981 Mar-Apr;15(2):281-9.

PMID:6264283
Abstract

A method for studying protein structure and estimating its electron conducting properties is proposed. The method is based on the kinetic recording of exchange quenching triplet labels and probes phosphorescence by chromophores or paramagnetic centres. It is shown that different types of exchange interactions (spin exchange, exchange energy transfer) between centres with distance R are described approximately by an equation (I = I0 exp-2R/L) where L changes from 0.7 A (absence of electron coupling--system of type I) to 6.5 A (strong electron coupling--system of type II). I (sec-1) corresponds to exchange energy transfer rate constant or exchange integral in the case of spin exchange. Life-times of excited triplet state eosin-isotiocionate labels connected with the terminal NH2-groups of the following preparations were measured by the method of kinetic phosphorescence decay recording: human oxyhemoglobin, methemoglobin, F- and CN-methemoglobin, metmyoglobin, F- and CN-metmyoglobins. The influence of lysozyme of the nitroxyl spin label bound to His-15 group on the phosphorescence spectrum was investigated. The analysis of our and literature data on the exchange interactions between the centres localized on the protein with known structure (hemoglobin, myoglobin, lysozyme, carboangidrase, bacterial ferredoxin) permit us to conclude that in the examined cases the experimental values correspond to model systems of type I and are different from the dependence in systems of type II by 5--15 order. This allows us to use equation (I) for estimation of the distances between the centres on proteins.

摘要

提出了一种研究蛋白质结构并估计其电子传导性质的方法。该方法基于对交换猝灭三重态标记以及发色团或顺磁中心对探针磷光的动力学记录。结果表明,距离为R的中心之间不同类型的交换相互作用(自旋交换、交换能量转移)大约由方程(I = I0 exp-2R/L)描述,其中L从0.7埃(不存在电子耦合——I型系统)变化到6.5埃(强电子耦合——II型系统)。I(秒-1)在自旋交换的情况下对应于交换能量转移速率常数或交换积分。通过动力学磷光衰减记录法测量了与以下制剂末端NH2基团相连的激发三重态曙红-异硫氰酸酯标记的寿命:人氧合血红蛋白、高铁血红蛋白、F-和CN-高铁血红蛋白、肌红蛋白、F-和CN-肌红蛋白。研究了与His-15基团结合的硝酰自旋标记的溶菌酶对磷光光谱的影响。对我们自己以及文献中关于位于具有已知结构的蛋白质(血红蛋白、肌红蛋白、溶菌酶、碳酸酐酶、细菌铁氧化还原蛋白)上的中心之间交换相互作用的数据进行分析后,我们可以得出结论,在所研究的案例中,实验值对应于I型模型系统,并且与II型系统中的依赖性相差5 - 15个数量级。这使我们能够使用方程(I)来估计蛋白质上中心之间的距离。

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Mol Biol (Mosk). 1981 Mar-Apr;15(2):281-9.
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