Phosphorylation energy hypothesis: Open chemical systems and their biological functions

被引：220

作者：

Qian, Hong ^{[1
]}

机构：

[1] Univ Washington, Dept Appl Math, Seattle, WA 98195 USA

来源：

ANNUAL REVIEW OF PHYSICAL CHEMISTRY | 2007年 / 58卷 / 113-142期

关键词：

chemical kinetics; kinetic proofreading; nonequilibrium steady state; signal transduction; thermodynamics;

D O I：

10.1146/annurev.physchem.58.032806.104550

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Biochemical systems and processes in living cells generally operate far from equilibrium. This review presents an overview of a statistical thermodynamic treatment for such systems, with examples from several key components in cellular signal transduction. Open-system. nonequilibrium steady-state (NESS) models are introduced. The models account quantitatively for the energetics and thermodynamics in phosphorylation-dephosphorylation switches, GTPase timers, and specificity amplification through kinetic proofreading. The chemical energy derived from ATP and GTP hydrolysis establishes the NESS of a cell and makes the cell-a mesoscopic-biochemical reaction system that consists of a collection of thermally driven fluctuating macromolecules-a genetically programmed chemical machine.

引用

页码：113 / 142

页数：30

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