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Curve of the Michaelis–Menten equation labelled in accordance with IUBMB recommendations. In biochemistry, Michaelis–Menten kinetics, named after Leonor Michaelis and Maud Menten, is the simplest case of enzyme kinetics, applied to enzyme-catalysed reactions involving the transformation of one substrate into one product.
Similarly, reactions with heterogeneous catalysis can be zero order if the catalytic surface is saturated. For example, the decomposition of phosphine (PH 3) on a hot tungsten surface at high pressure is zero order in phosphine, which decomposes at a constant rate. [15] In homogeneous catalysis zero order behavior can come about from reversible ...
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 zero-order hold (ZOH) is a mathematical model of the practical signal reconstruction done by a conventional digital-to-analog converter (DAC). [1] That is, it describes the effect of converting a discrete-time signal to a continuous-time signal by holding each sample value for one sample interval. It has several applications in electrical ...
Reactant concentrations, which usually make the reaction happen at a faster rate if raised through increased collisions per unit of time. Some reactions, however, have rates that are independent of reactant concentrations, due to a limited number of catalytic sites. These are called zero order reactions.
n th-order reaction (r = kC A n), where k is the reaction rate constant, C A is the concentration of species A, and n is the order of the reaction; isothermal conditions, or constant temperature (k is constant) single, irreversible reaction (ν A = −1) All reactant A is converted to products via chemical reaction; N A = C A V
Random-order ternary-complex mechanism for an enzyme reaction. The reaction path is shown as a line and enzyme intermediates containing substrates A and B or products P and Q are written below the line. In these enzymes, both substrates bind to the enzyme at the same time to produce an EAB ternary complex.
[1] [2] Thus, the rate equation is often shown as having first-order dependence on the substrate and zero-order dependence on the nucleophile. This relationship holds for situations where the amount of nucleophile is much greater than that of the intermediate. Instead, the rate equation may be more accurately described using steady-state kinetics.