Schlitter J
J Theor Biol. 1984 Feb 7;106(3):303-13. doi: 10.1016/0022-5193(84)90032-8.
One important problem for the function of proteins, especially enzymes, concerns the exchange of energy with the surrounding medium. In this paper, we study the interaction of vibrational degrees of freedom with the fluctuating water dipole moments. The rates of activation or deactivation attain a maximum at slow frequency vibrations near the water dispersion frequencies, i.e. in the gigahertz region. For medium proteins with molecular weights of approximately 10(4) a.m.u., the rates are estimated to be of the order of magnitude of kBT/h, the frequency factor of the transition state theory. We discuss the connection between energy exchange and reaction rates and show that a rapid energy exchange is at least a necessary condition for enzymatic catalysis.
蛋白质（尤其是酶）功能的一个重要问题涉及与周围介质的能量交换。在本文中，我们研究了振动自由度与波动的水分子偶极矩之间的相互作用。激活或失活速率在接近水分散频率（即在千兆赫兹区域）的低频振动时达到最大值。对于分子量约为10⁴原子质量单位的中等大小蛋白质，该速率估计为过渡态理论频率因子kBT/h的量级。我们讨论了能量交换与反应速率之间的联系，并表明快速的能量交换至少是酶催化的必要条件。
