The main goal of this book is to describe in physical terms the peculiar features of "machines" having molecular dimensions that play the principal role in the most important biological processes. The book is aimed at scientists and graduate students of biochemistry and biophysics as well as biologists and physicians working in this field.

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1 Introduction.- 2 Thermodynamics and Chemical Kinetics of Living Systems.- 2.1. How Scientists Learned to Distinguish Energy from Force (Brief Historic Review).- 2.2. Kinetics and Thermodynamics of Chemical Reactions.- 2.3. Applicability of Equilibrium and Nonequilibrium Thermodynamics to Biological Systems and Processes.- 2.4. The Mechanisms of Energy Coupling in Chemical Reactions.- 2.4.1. Indirect Mechanism of Energy Coupling in Equilibrium (Quasi-Equilibrium) Homogeneous Mixtures of Chemical Reagents.- 2.4.1.1. Enthalpic Mechanism of Indirect Coupling.- 2.4.1.2. Entropic Mechanism of Indirect Coupling.- 2.4.2. Entropic Mechanism of Coupling Chemical Reactions in Open Systems.- 3 Molecular Machines: Mechanics and/or Statistics?.- 3.1. The Second Law of Thermodynamics and Its Application to Biochemical Systems.- 3.2. Energy-Transducing Molecular Machines.- 3.2.1. Macroscopic Machines.- 3.2.2. What Are Molecular Machines? Reversibility of Energy-Transducing Devices and the Problem of the Optimal Functioning of Molecular Machines.- 3.2.3. Models for Calculating the Conversion Factor.- 3.3. Statistical Thermodynamics of Small Systems, Fluctuations, and the Violation of the Mass Action Law.- 3.3.1. Structural Peculiarities of Energy-Transducing Organelles of Chloroplasts.- 3.3.2. Chemical Equilibrium Inside Small Vesicles.- 3.3.3. Compartmentalization and the Problem of the Macroscopic Description of "Channeled" Chemical Reactions.- 3.3.4. The Fluctuations, Random Noise, Energy Transduction, and Apparent Violation of the Second Law of Thermodynamics.- 4 Principles of Enzyme Catalysis.- 4.1. Introduction.- 4.2. Earlier Theories of Enzyme Catalysis.- 4.3. The Relaxation Concept of Enzyme Catalysis.- 4.4. Protein Dynamics and Enzyme Functioning.- 4.4.1. Theoretical Aspects of Protein Structural Dynamics.- 4.4.2. Experimental Evidence for Protein Nonequilibrium States and Their Evolution in the Course of Enzyme Turnover.- 5 Energy Transduction in Biological Membranes.- 5.1. Introduction: Two Views on the Problem of Energy Coupling in Biomembranes.- 5.2. Transmembrane Electrochemical Proton Gradients in Chloroplasts.- 5.2.1. Brief Review of the Methods for the ?pH Measurements with pH-Indicating Probes.- 5.2.2. Measurements of ?pH in the Thylakoids with the Kinetic Method.- 5.2.3. Measurements of ?pH in the Thylakoids with a Spin Labeling Technique.- 5.2.4. Lateral Heterogeneity of ?pH in Chloroplasts.- 5.2.5. Membrane-Sequestered Proton Pools and Alternative Pathways of Proton Transport Coupled with ATP Synthesis.- 5.3. Mechanism of ATP Formation Catalyzed by H+ATPsynthases.- 5.3.1. An Elementary Act of ATP Synthesis.- 5.3.1.1. Initial Events of ATP Formation.- 5.3.1.2. Energy-Requiring Step of ATP Formation.- 5.3.1.3. ATP Synthesis from ADP and Pi Catalyzed by Water-Soluble Coupling Factor F1.- 5.3.1.4. ATP Synthesis Induced by the Acid-Base Transitions.- 5.3.1.5. ATP Synthesis from ADP and Pi as Considered from the Viewpoint of the Relaxation Concept of Enzyme Catalysis.- 5.3.2. ATP Synthesis under Steady State Conditions.- 5.3.2.1. The Possible Model for ATPsynthase Cyclic Functioning.- 5.3.2.2. Photophosphorylation in Chloroplasts and Oxidative Phosphorylation in Mitochondria.- Afterword.