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F0F1 - ATP合酶的动力学特性。交替位点模型的理论预测。

Kinetic properties of F0F1-ATPases. Theoretical predictions from alternating-site models.

作者信息

Stein W D, Läuger P

机构信息

Department of Biological Chemistry, Hebrew University, Jerusalem, Israel.

出版信息

Biophys J. 1990 Feb;57(2):255-67. doi: 10.1016/S0006-3495(90)82528-5.

DOI:10.1016/S0006-3495(90)82528-5
PMID:2138501
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1280667/
Abstract

We present an analysis of models based on current structural concepts of the F0F1 synthases, accounting for coupling between proton transport and ATP synthesis. It is assumed that each of the three alpha beta-subunits of the synthase can exist in three different conformational states E, Eo and E*. Proton translocation is coupled to cyclic interconversion of the conformations of the alpha beta-subunits. The conformational changes of these subunits are assumed to be coordinated so that all three interconvert simultaneously, in a rate-limiting transition. Binding and release of the ligands ATP, ADP, Pi, and protons are assumed to be equilibrium steps. In one family of models, interconversion of the alpha beta-subunits of F1 is coupled to the translocation event in F0 acting as a proton carrier. In a second family of models, protons combine with F0F1 and are translocated during the interconversion step in a chemiport. Kinetic tests involving the mutual effects of [ATP], [ADP], H+', and H+" are described, allowing us to make a distinction between the different models and submodels.

摘要

我们基于F0F1合酶当前的结构概念对模型进行了分析,解释了质子转运与ATP合成之间的偶联关系。假定合酶的三个αβ亚基中的每一个都可以存在于三种不同的构象状态E、Eo和E*。质子易位与αβ亚基构象的循环相互转化偶联。假定这些亚基的构象变化是协同的,以便所有三个亚基在限速转变中同时相互转化。配体ATP、ADP、Pi和质子的结合与释放被假定为平衡步骤。在一类模型中,F1的αβ亚基的相互转化与作为质子载体的F0中的易位事件偶联。在另一类模型中,质子与F0F1结合并在化学转运体的相互转化步骤中发生易位。描述了涉及[ATP]、[ADP]、H+'和H+"相互作用的动力学测试,这使我们能够区分不同的模型和子模型。

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引用本文的文献

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Biophysical comparison of ATP synthesis mechanisms shows a kinetic advantage for the rotary process.ATP合成机制的生物物理比较显示了旋转过程的动力学优势。
Proc Natl Acad Sci U S A. 2016 Oct 4;113(40):11220-11225. doi: 10.1073/pnas.1608533113. Epub 2016 Sep 19.
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J Bioenerg Biomembr. 1993 Jun;25(3):285-95. doi: 10.1007/BF00762589.

本文引用的文献

1
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Hypothesis. The mechanism of ATP synthase. Conformational change by rotation of the beta-subunit.
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Assessment of the rate of bound substrate interconversion and of ATP acceleration of product release during catalysis by mitochondrial adenosine triphosphatase.线粒体三磷酸腺苷酶催化过程中结合底物相互转化速率及ATP对产物释放的加速作用评估。
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Recent developments on structural and functional aspects of the F1 sector of H+-linked ATPases.H⁺ 连接的ATP酶F1 部分结构和功能方面的最新进展。
Mol Cell Biochem. 1984;60(1):33-71. doi: 10.1007/BF00226299.
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The proton conducting F0-part of bacterial ATP synthases.细菌ATP合酶的质子传导F0部分。
Biochim Biophys Acta. 1984 Apr 9;768(1):1-27. doi: 10.1016/0304-4173(84)90005-3.
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Structure and function of proton-translocating adenosine triphosphatase (F0F1): biochemical and molecular biological approaches.质子转运三磷酸腺苷酶(F0F1)的结构与功能:生化及分子生物学方法
Microbiol Rev. 1983 Sep;47(3):285-312. doi: 10.1128/mr.47.3.285-312.1983.
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Proton atpases: structure and mechanism.质子ATP酶:结构与机制
Annu Rev Biochem. 1983;52:801-24. doi: 10.1146/annurev.bi.52.070183.004101.
8
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J Biol Chem. 1982 Oct 25;257(20):12030-8.
9
Biochemical and genetic studies on the assembly and function of the F1-F0 adenosine triphosphatase of Escherichia coli.关于大肠杆菌F1-F0三磷酸腺苷酶组装及功能的生化与遗传学研究。
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