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In chemical kinetics, the overall rate of a reaction is often approximately determined by the slowest step, known as the rate-determining step (RDS or RD-step [1] or r/d step [2] [3]) or rate-limiting step. For a given reaction mechanism, the prediction of the corresponding rate equation (for comparison with the experimental rate law) is often ...
In biochemistry, a rate-limiting step is a reaction step that controls the rate of a series of biochemical reactions. [1] [2] 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.
The fastest enzymes in the dark box on the right (>10 8 s −1 M −1) are constrained by the diffusion limit. (Data adapted from reference [1]) A diffusion-limited enzyme catalyses a reaction so efficiently that the rate limiting step is that of substrate diffusion into the active site, or product diffusion out. [2]
A reaction is considered to occur if molecules A and B touch, that is, when the distance between the two molecules is apart. If we assume a local steady state, then the rate at which B reaches is the limiting factor and balances the reaction. Therefore, the steady state condition becomes
The reaction starting with [4+2] cycloaddition of CF 3 C≡CCF 3 at one of the furan moieties occurs in a concerted fashion via TS1 and represents the rate limiting step of the whole process with the activation barrier ΔG ‡ ≈ 23.1–26.8 kcal/mol. Gibbs free energy profile for the reaction between bis-dienes 3a-c and hexafluoro-2-butyne.
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Beyond this limit the enzyme is saturated with substrate and the reaction rate ceases to increase. The reaction catalysed by an enzyme uses exactly the same reactants and produces exactly the same products as the uncatalysed reaction. Like other catalysts, enzymes do not alter the position of equilibrium between substrates and products. [1]
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