Department of Biophysics, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, New York 10461, USA.
J Phys Chem B. 2010 Dec 9;114(48):15985-90. doi: 10.1021/jp1071296. Epub 2010 Nov 15.
It has been accepted for many years that functionally important motions are crucial to binding properties of ligands in such molecules as hemoglobin and myoglobin. In enzymatic reactions, theory and now experiment are beginning to confirm the importance of motions on a fast (ps) time scale in the chemical step of the catalytic process. What is missing is a clear physical picture of how slow conformational fluctuations are related to the fast motions that have been identified as crucial. This paper presents a theoretical analysis of this issue for human heart lactate dehydrogenase. We will examine how slow conformational motions bring the system to conformations that are distinguished as catalytically competent because they favor specific fast motions.
多年来，人们一直认为功能重要的运动对于血红蛋白和肌红蛋白等分子中配体的结合性质至关重要。在酶反应中，理论和现在的实验都开始证实，在催化过程的化学步骤中，快速（ps）时间尺度上的运动的重要性。目前缺少的是一个明确的物理图像，说明缓慢的构象波动如何与已确定为关键的快速运动相关。本文针对人心脏乳酸脱氢酶对此问题进行了理论分析。我们将研究缓慢的构象运动如何使系统达到催化能力的构象，因为它们有利于特定的快速运动。
