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[腺苷-5'-三磷酸水解能量对氢键的激发作用]

[Excitation of the hydrogen bond by the energy of hydrolysis of adenosine-5'-triphosphate].

作者信息

Bespalova S V, Tolpygo K B

机构信息

Donetsk State University, Ukraine.

出版信息

Biofizika. 1998 May-Jun;43(3):484-9.

PMID:9702342
Abstract

The model of muscle contraction suggested in [1] is based on the hypothesis that the first step of the conversion of chemical energy delta E (which is stored in adenosine-5'-triphosphate) is the excitation of the hydrogen bond in the actin-myosin system with a simultaneous hydrolysis of the adenosine-5'-triphosphate molecule. As a consequence, the potential barrier is decreased, and the break of the macroergic bond adenosine-5'-triphosphate-phosphate is facilitated. With the delta E value exceeding the excitation energy of the H-bond, this process represents an exothermic reaction. A simple model of this process is constructed, and its probability depending on temperature and the mutual position of the H-bond and the adenosine-5'-triphosphate molecule is estimated.

摘要

文献[1]中提出的肌肉收缩模型基于这样一个假设:化学能ΔE(储存在腺苷-5'-三磷酸中)转化的第一步是肌动蛋白-肌球蛋白系统中氢键的激发,同时伴随着腺苷-5'-三磷酸分子的水解。因此,势垒降低,高能键腺苷-5'-三磷酸-磷酸的断裂变得更容易。当ΔE值超过氢键的激发能时,这个过程是一个放热反应。构建了这个过程的一个简单模型,并估计了其概率与温度以及氢键和腺苷-5'-三磷酸分子相互位置的关系。

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