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A common form for the rate equation is a power law: [6] = [] [] The constant is called the rate constant.The exponents, which can be fractional, [6] are called partial orders of reaction and their sum is the overall order of reaction.
where A and B are reactants C is a product a, b, and c are stoichiometric coefficients,. the reaction rate is often found to have the form: = [] [] Here is the reaction rate constant that depends on temperature, and [A] and [B] are the molar concentrations of substances A and B in moles per unit volume of solution, assuming the reaction is taking place throughout the volume of the ...
In physical chemistry, the Arrhenius equation is a formula for the temperature dependence of reaction rates.The equation was proposed by Svante Arrhenius in 1889, based on the work of Dutch chemist Jacobus Henricus van 't Hoff who had noted in 1884 that the van 't Hoff equation for the temperature dependence of equilibrium constants suggests such a formula for the rates of both forward and ...
Zero order reaction. Zero-order process (statistics), a sequence of random variables, each independent of the previous ones; Zero order process (chemistry), a chemical reaction in which the rate of change of concentration is independent of the concentrations; Zeroth-order approximation, an approximation of a function by a constant
The Michaelis constant is defined as the concentration of substrate at which the reaction rate is half of . [6] Biochemical reactions involving a single substrate are often assumed to follow Michaelis–Menten kinetics, without regard to the model's underlying assumptions.
In a chemical reaction, the half-life of a species is the time it takes for the concentration of that substance to fall to half of its initial value. In a first-order reaction the half-life of the reactant is ln(2)/λ, where λ (also denoted as k) is the reaction rate constant.
The apparent unimolecular rate constant k cat is also called turnover number, and denotes the maximum number of enzymatic reactions catalysed per second. The Michaelis–Menten equation [10] describes how the (initial) reaction rate v 0 depends on the position of the substrate-binding equilibrium and the rate constant k 2.
The steady state approximation, [1] occasionally called the stationary-state approximation or Bodenstein's quasi-steady state approximation, involves setting the rate of change of a reaction intermediate in a reaction mechanism equal to zero so that the kinetic equations can be simplified by setting the rate of formation of the intermediate equal to the rate of its destruction.