Warshel A
Proc Natl Acad Sci U S A. 1984 Jan;81(2):444-8. doi: 10.1073/pnas.81.2.444.
The detailed molecular dynamics of an actual bond-breaking event in a fluctuating enzyme substrate complex is simulated. The method developed allows one to explore what type of fluctuations are involved in enzymatic reactions and to evaluate entropic contributions to enzyme catalysis. The fluctuations of the enzyme electrostatic potential are found to be a key dynamical factor in reactions that involve a large change in the polarity of the reacting bonds.
模拟了波动的酶-底物复合物中实际键断裂事件的详细分子动力学。所开发的方法使人们能够探索酶促反应中涉及何种类型的波动，并评估熵对酶催化的贡献。发现酶静电势的波动是涉及反应键极性发生重大变化的反应中的关键动力学因素。
