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This chapter focuses on chemical kinetic principles and the basic physical chemistry of chemical reactivity in aqueous solutions. It provides the underpinnings for subsequent chapters on the kinetic investigation of enzyme catalysis and control. Chemical kinetics provides the systematic framework for defining time-dependent changes in single- and multistep rate processes. The latter are especially important in enzyme kinetics, because each catalytic cycle can be treated as a series of chemical reactions, wherein the product of one step is an enzyme species that then becomes a reactant in the next step.

There are two fundamentally different ways to treat the kinetic behavior of chemical systems: classically, as a continuous quantity that varies deterministically over time and that can therefore be represented by a set of coupled, first-order, ordinary differential equations, and stochastically, as discrete processes, whose variables are numbers of molecules, with a time-dependent behavior that is probablistic, as controlled by mesoscopic rate constants. Some enzymatic reactions occur on the surface of or deep within the phospholipid bilayer of biomembranes. Such processes are apt to exploit special opportunities for dehydration of active sites as well as facilitation of nucleophilic chemistry. This chapter also reinforces the important interplay of kinetics and thermodynamics as well as the constraints of microscopic reversibility on rate constants and multistep processes. Because catalysts return to their initial-state configuration after each catalytic round, enzyme catalysis is an inherently cyclical process, and the importance of thermodynamic constraints cannot be overstated.

This article has not been cited. Email us even your request is not listed below and don’t give up we have the chance to get it. Classical Dynamics of Particles and  Systems 5th ed! Materials for Civil and Construction Engineers, 3E Michael S.