Authors: Sosale Chandrasekhar
The key assumption of activated complex theory (ACT), that the AC is in thermodynamic equilibrium with the reactants, needs to be reconsidered. This is because the formation of the AC is slower than its collapse to product. However, this can be remedied by assuming that the AC is formed in a rapid pre-equilibrium as a thermally activated species, which collapses to products in a slow step involving the diffusion of another AC molecule (or solvent in the case of a unimolecular reaction). This implies a violation of the principle of microscopic reversibility (PMR), as also the relation between standard free energy change and equilibrium constant (ΔGo = -RTlnK). However, it may be argued that not only do these not apply to processes performed irreversibly, but also that irreversibility requires the breakdown of the PMR. Accordingly, catalysts may alter equilibrium constants, and enzymes may regulate biochemical processes in hitherto unsuspected ways.
Comments: 15 Pages.
[v1] 2012-04-18 06:01:16
Unique-IP document downloads: 379 times
Add your own feedback and questions here:
You are equally welcome to be positive or negative about any paper but please be polite. If you are being critical you must mention at least one specific error, otherwise your comment will be deleted as unhelpful.