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In chemical kinetics, the Lindemann mechanism (also called the Lindemann–Christiansen mechanism[1] or the Lindemann–Hinshelwood mechanism[2][3]) is a schematic reaction mechanism for unimolecular reactions. Frederick Lindemann and J. A. Christiansen proposed the concept almost simultaneously in 1921, [4][1] and Cyril Hinshelwood developed ...
There are two main descriptions of motion: dynamics and kinematics.Dynamics is general, since the momenta, forces and energy of the particles are taken into account. In this instance, sometimes the term dynamics refers to the differential equations that the system satisfies (e.g., Newton's second law or Euler–Lagrange equations), and sometimes to the solutions to those equations.
The second step with OH − is much faster, so the overall rate is independent of the concentration of OH −. In contrast, the alkaline hydrolysis of methyl bromide (CH 3 Br) is a bimolecular nucleophilic substitution (S N 2) reaction in a single bimolecular step. Its rate law is second-order: r = k[R−Br][OH −].
The Van 't Hoff equation relates the change in the equilibrium constant, Keq, of a chemical reaction to the change in temperature, T, given the standard enthalpy change, ΔrH⊖, for the process. The subscript means "reaction" and the superscript means "standard". It was proposed by Dutch chemist Jacobus Henricus van 't Hoff in 1884 in his book ...
Fick's first law relates the diffusive flux to the gradient of the concentration. It postulates that the flux goes from regions of high concentration to regions of low concentration, with a magnitude that is proportional to the concentration gradient (spatial derivative), or in simplistic terms the concept that a solute will move from a region of high concentration to a region of low ...
Hanes–Woolf plot. In biochemistry, a Hanes–Woolf plot, Hanes plot, or plot of against is a graphical representation of enzyme kinetics in which the ratio of the initial substrate concentration to the reaction velocity is plotted against . It is based on the rearrangement of the Michaelis–Menten equation shown below:
The result is equivalent to the Michaelis–Menten kinetics of reactions catalyzed at a site on an enzyme. The rate equation is complex, and the reaction order is not clear. In experimental work, usually two extreme cases are looked for in order to prove the mechanism. In them, the rate-determining step can be: Limiting step: adsorption/desorption
Reaction progress kinetic analysis. In chemistry, reaction progress kinetic analysis (RPKA) is a subset of a broad range of kinetic techniques utilized to determine the rate laws of chemical reactions and to aid in elucidation of reaction mechanisms. While the concepts guiding reaction progress kinetic analysis are not new, the process was ...