Department of Cell and Molecular Biology (ICM), Uppsala Biomedical Centre, Uppsala University, Box 596, S-751 24 Uppsala, Sweden.
Q Rev Biophys. 2013 Feb;46(1):1-132. doi: 10.1017/S0033583512000157. Epub 2013 Jan 15.
Phosphoryl transfer plays key roles in signaling, energy transduction, protein synthesis, and maintaining the integrity of the genetic material. On the surface, it would appear to be a simple nucleophile displacement reaction. However, this simplicity is deceptive, as, even in aqueous solution, the low-lying d-orbitals on the phosphorus atom allow for eight distinct mechanistic possibilities, before even introducing the complexities of the enzyme catalyzed reactions. To further complicate matters, while powerful, traditional experimental techniques such as the use of linear free-energy relationships (LFER) or measuring isotope effects cannot make unique distinctions between different potential mechanisms. A quarter of a century has passed since Westheimer wrote his seminal review, 'Why Nature Chose Phosphate' (Science 235 (1987), 1173), and a lot has changed in the field since then. The present review revisits this biologically crucial issue, exploring both relevant enzymatic systems as well as the corresponding chemistry in aqueous solution, and demonstrating that the only way key questions in this field are likely to be resolved is through careful theoretical studies (which of course should be able to reproduce all relevant experimental data). Finally, we demonstrate that the reason that nature really chose phosphate is due to interplay between two counteracting effects: on the one hand, phosphates are negatively charged and the resulting charge-charge repulsion with the attacking nucleophile contributes to the very high barrier for hydrolysis, making phosphate esters among the most inert compounds known. However, biology is not only about reducing the barrier to unfavorable chemical reactions. That is, the same charge-charge repulsion that makes phosphate ester hydrolysis so unfavorable also makes it possible to regulate, by exploiting the electrostatics. This means that phosphate ester hydrolysis can not only be turned on, but also be turned off, by fine tuning the electrostatic environment and the present review demonstrates numerous examples where this is the case. Without this capacity for regulation, it would be impossible to have for instance a signaling or metabolic cascade, where the action of each participant is determined by the fine-tuned activity of the previous piece in the production line. This makes phosphate esters the ideal compounds to facilitate life as we know it.
磷酸化转移在信号转导、能量传递、蛋白质合成和遗传物质完整性维持中起着关键作用。从表面上看,它似乎是一种简单的亲核取代反应。然而,这种简单性具有欺骗性,即使在水溶液中,磷原子的低能 d 轨道也允许在引入酶催化反应的复杂性之前,有八种不同的机械可能性。更复杂的是,尽管强大的传统实验技术,如使用线性自由能关系(LFER)或测量同位素效应,不能在不同的潜在机制之间做出独特的区分。自 Westheimer 撰写他的开创性综述《为什么自然界选择磷酸酯》(Science 235 (1987), 1173)以来,已经过去了四分之一个世纪,自那时以来,该领域发生了很多变化。本综述重新探讨了这一具有生物学重要意义的问题,既探讨了相关的酶系统,也探讨了水溶液中的相应化学,证明了该领域的关键问题只有通过仔细的理论研究才能得到解决(当然,这些理论研究应该能够重现所有相关的实验数据)。最后,我们证明了自然界之所以选择磷酸酯,是因为两种相互作用的效应:一方面,磷酸酯带负电荷,与进攻亲核试剂的电荷-电荷排斥作用有助于水解的高壁垒,使磷酸酯成为已知最惰性的化合物之一。然而,生物学不仅仅是降低不利于化学反应的壁垒。也就是说,使磷酸酯水解如此不利的相同电荷-电荷排斥作用也使其能够通过利用静电来进行调节。这意味着磷酸酯水解不仅可以打开,而且可以关闭,通过微调静电环境,本综述展示了许多这样的例子。如果没有这种调节能力,就不可能有信号转导或代谢级联,在这种级联中,每个参与者的作用由生产线前一个部分的精细调节活性决定。这使得磷酸酯成为促进我们所知的生命的理想化合物。