论文标题
灵活性如何增强催化
How flexibility can enhance catalysis
论文作者
论文摘要
在许多酶中观察到构象变化，但是它们在催化中的作用是有争议的。在这里，我们提出了一个理论模型，该模型说明了如何从根本上受到限制的刚性催化剂以及底物结合引起的构象变化如何克服这种限制，最终实现了无屏障的催化。该模型故意最小，但其说明的原理是一般的，并且与蛋白质的独特特征以及以前的非正式建议一致，以解释酶优于其他类别的催化剂。该模型建议的判别开关可以帮助克服人工催化剂设计中当前遇到的局限性。
Conformational changes are observed in many enzymes, but their role in catalysis is highly controversial. Here we present a theoretical model that illustrates how rigid catalysts can be fundamentally limited and how a conformational change induced by substrate binding can overcome this limitation, ultimately enabling barrier-free catalysis. The model is deliberately minimal, but the principle it illustrates is general and consistent with unique features of proteins as well as with previous informal proposals to explain the superiority of enzymes over other classes of catalysts. Implementing the discriminative switch suggested by the model could help overcome limitations currently encountered in the design of artificial catalysts.
