Abstract

Recently, a new mechanism for reaction selectivity, arising from conformational gating of the reactions, has been reported in the acetylcholinesterase system. Fluctuations in the enzyme are thought to greatly slow the access of molecules larger than the normal substrate to the active-site region. By assuming the gate fluctuations occur as a Brownian process in a harmonic well, it is possible to approximate the reaction rates for various limiting cases of substrate size. However, it is not possible to simplify the rates into a ratio which is equivalent to the Boltzmann distribution of states for the gate fluctuations.

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