In a chemical reaction, chemical equilibrium is the state in which both the reactants and products are present in concentrations which have no further tendency to change with time, so that there is no observable change in the properties of the system. This state results when the forward reaction proceeds at the same rate as the reverse reaction. The reaction rates of the forward and backward reactions are generally not zero, but they are equal. Thus, there are no net changes in the concentrations of the reactants and products. Such a state is known as dynamic equilibrium.
Fick's laws of diffusion describe diffusion and were first posited by Adolf Fick in 1855 on the basis of largely experimental results. They can be used to solve for the diffusion coefficient, D. Fick's first law can be used to derive his second law which in turn is identical to the diffusion equation.
The reaction rate or rate of reaction is the speed at which a chemical reaction takes place, defined as proportional to the increase in the concentration of a product per unit time and to the decrease in the concentration of a reactant per unit time. Reaction rates can vary dramatically. For example, the oxidative rusting of iron under Earth's atmosphere is a slow reaction that can take many years, but the combustion of cellulose in a fire is a reaction that takes place in fractions of a second. For most reactions, the rate decreases as the reaction proceeds. A reaction's rate can be determined by measuring the changes in concentration over time.
The equilibrium constant of a chemical reaction is the value of its reaction quotient at chemical equilibrium, a state approached by a dynamic chemical system after sufficient time has elapsed at which its composition has no measurable tendency towards further change. For a given set of reaction conditions, the equilibrium constant is independent of the initial analytical concentrations of the reactant and product species in the mixture. Thus, given the initial composition of a system, known equilibrium constant values can be used to determine the composition of the system at equilibrium. However, reaction parameters like temperature, solvent, and ionic strength may all influence the value of the equilibrium constant.
The Green–Kubo relations give the exact mathematical expression for a transport coefficient in terms of the integral of the equilibrium time correlation function of the time derivative of a corresponding microscopic variable :
In chemistry, the rate equation is an empirical differential mathematical expression for the reaction rate of a given reaction in terms of concentrations of chemical species and constant parameters only. For many reactions, the initial rate is given by a power law such as
Enzyme kinetics is the study of the rates of enzyme-catalysed chemical reactions. In enzyme kinetics, the reaction rate is measured and the effects of varying the conditions of the reaction are investigated. Studying an enzyme's kinetics in this way can reveal the catalytic mechanism of this enzyme, its role in metabolism, how its activity is controlled, and how a drug or a modifier might affect the rate.
In biochemistry, metabolic control analysis (MCA) is a mathematical framework for describing metabolic, signaling, and genetic pathways. MCA quantifies how variables, such as fluxes and species concentrations, depend on network parameters. In particular, it is able to describe how network-dependent properties, called control coefficients, depend on local properties called elasticities or elasticity coefficients.
In chemistry, transition state theory (TST) explains the reaction rates of elementary chemical reactions. The theory assumes a special type of chemical equilibrium (quasi-equilibrium) between reactants and activated transition state complexes.
In chemistry, the rate of a chemical reaction is influenced by many different factors, such as temperature, pH, reactant, the concentration of products, and other effectors. The degree to which these factors change the reaction rate is described by the elasticity coefficient. This coefficient is defined as follows:
Diffusion is the net movement of anything generally from a region of higher concentration to a region of lower concentration. Diffusion is driven by a gradient in Gibbs free energy or chemical potential. It is possible to diffuse "uphill" from a region of lower concentration to a region of higher concentration, as in spinodal decomposition. Diffusion is a stochastic process due to the inherent randomness of the diffusing entity and can be used to model many real-life stochastic scenarios. Therefore, diffusion and the corresponding mathematical models are used in several fields beyond physics, such as statistics, probability theory, information theory, neural networks, finance, and marketing.
Equilibrium chemistry is concerned with systems in chemical equilibrium. The unifying principle is that the free energy of a system at equilibrium is the minimum possible, so that the slope of the free energy with respect to the reaction coordinate is zero. This principle, applied to mixtures at equilibrium provides a definition of an equilibrium constant. Applications include acid–base, host–guest, metal–complex, solubility, partition, chromatography and redox equilibria.
In electrochemistry, the Randles–Ševčík equation describes the effect of scan rate on the peak current for a cyclic voltammetry experiment. For simple redox events where the reaction is electrochemically reversible, and the products and reactants are both soluble, such as the ferrocene/ferrocenium couple, ip depends not only on the concentration and diffusional properties of the electroactive species but also on scan rate.
The system size expansion, also known as van Kampen's expansion or the Ω-expansion, is a technique pioneered by Nico van Kampen used in the analysis of stochastic processes. Specifically, it allows one to find an approximation to the solution of a master equation with nonlinear transition rates. The leading order term of the expansion is given by the linear noise approximation, in which the master equation is approximated by a Fokker–Planck equation with linear coefficients determined by the transition rates and stoichiometry of the system.
In biochemistry, a rate-limiting step is a reaction step that controls the rate of a series of biochemical reactions. The statement is, however, a misunderstanding of how a sequence of enzyme-catalyzed reaction steps operate. Rather than a single step controlling the rate, it has been discovered that multiple steps control the rate. Moreover, each controlling step controls the rate to varying degrees.
Branched pathways, also known as branch points, are a common pattern found in metabolism. This is where an intermediate species is chemically made or transformed by multiple enzymatic processes. linear pathways only have one enzymatic reaction producing a species and one enzymatic reaction consuming the species.
Control coefficients measure the response of a biochemical pathway to changes in enzyme activity. The response coefficient, as originally defined by Kacser and Burns, is a measure of how external factors such as inhibitors, pharmaceutical drugs, or boundary species affect the steady-state fluxes and species concentrations. The flux response coefficient is defined by:
In metabolic control analysis, a variety of theorems have been discovered and discussed in the literature. The most well known of these are flux and concentration control coefficient summation relationships. These theorems are the result of the stoichiometric structure and mass conservation properties of biochemical networks. Equivalent theorems have not been found, for example, in electrical or economic systems.
The stoichiometric structure and mass-conservation properties of biochemical pathways gives rise to a series of theorems or relationships between the control coefficients and the control coefficients and elasticities. There are a large number of such relationships depending on the pathway configuration which have been documented and discovered by various authors. The term theorem has been used to describe these relationships because they can be proved in terms of more elementary concepts. The operational proofs in particular are of this nature.
A linear biochemical pathway is a chain of enzyme-catalyzed reaction steps where the product of one reaction becomes the substrate for the next reaction. The molecules progress through the pathway sequentially from the starting substrate to the final product. Each step in the pathway is usually facilitated by a different specific enzyme that catalyzes the chemical transformation. An example includes DNA replication, which connects the starting substrate and the end product in a straightforward sequence.
