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首页> 外文会议>Conference on Optical Technologies in Biophysics and Medicine IV; Oct 1-4, 2002; Saratov, Russia >Electrostatic interactions in catalytic centers of F_1-ATPase
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Electrostatic interactions in catalytic centers of F_1-ATPase

机译：F_1-ATPase催化中心的静电相互作用

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摘要

F_1-ATPase is one of the most important enzymes of membrane bioenergetics. F_1 -ATPase is the constituent complex that provides the ATP formation from ADP and inorganic phosphate (P_i) at the expense of energy of electrochemical gradient of hydrogen ions generated across the energy transducing mitochondrial, chloroplast or bacterial membrane. F_1-ATPase is a reversible molecular machine that can work as a proton pump due to energy released in the course of ATP hydrolysis (ATPase reaction). The unusual feature of this enzyme is that it operates as a rotary molecular motor. Recently, using the fluorescence microscopy method for the real time visualization of molecular mobility of individual molecules, it was demonstrated directly that the ATP hydrolysis by F_1-ATPase is accompanied by unidirectional rotations of mobile subunits (rotor) of F_1F_0-ATP synthase. In this work, we calculated the contribution of electrostatic interactions between charged groups of a substrate (MgATP), products molecules (MgADP and P_i) and charged amino acid residuals of ATPase molecule to the energy changes associated with the substrate binding and their chemical transformations in the catalytic centers located at the interface of α and β subunits of the enzyme (oligomer complex α_3β_3γ of bovine mitochondria ATPase). A catalytic cycle of ATP hydrolysis considered in our work includes conformaftional changes of α and β subunits caused by unidirectional rotations of an eccentric γ subunit. The knowledge of energy characteristics and force field in catalytic center of an enzyme in different conformational states may be important for further simulation dynamic properties of ATP synthase complex.
机译：F_1-ATPase是膜生物能最重要的酶之一。 F_1 -ATPase是一种组成复合物，它以跨能量转换线粒体，叶绿体或细菌膜产生的氢离子的电化学梯度能量为代价，由ADP和无机磷酸盐（P_i）提供了ATP的形成。 F_1-ATPase是一种可逆分子机器，由于在ATP水解（ATPase反应）过程中释放的能量，可以充当质子泵。这种酶的不寻常特征是它可以作为旋转分子马达运行。最近，使用荧光显微镜法实时观察单个分子的分子迁移率，直接证明了F_1-ATPase水解ATP伴随着F_1F_0-ATP合酶的移动亚基（转子）的单向旋转。在这项工作中，我们计算了底物的带电基团（MgATP），产物分子（MgADP和P_i）以及ATPase分子的带电氨基酸残基之间的静电相互作用对与底物结合及其化学转化相关的能量变化的贡献。催化中心位于酶的α和β亚基（牛线粒体ATPase的低聚物复合物α_3β_3γ）的界面上。我们工作中考虑的ATP水解的催化循环包括由偏心γ亚基的单向旋转引起的α和β亚基的构象变化。了解不同构象状态下酶催化中心的能量特征和力场对于进一步模拟ATP合酶复合物的动力学性质可能很重要。

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