School of Chemical Science, Indian Association for the Cultivation of Science, 2A Raja SC Mullick Road, Kolkata 700032, India.
Chem Rev. 2022 Jul 27;122(14):12370-12426. doi: 10.1021/acs.chemrev.1c01021. Epub 2022 Apr 11.
Activation and reduction of O and HO by synthetic and biosynthetic iron porphyrin models have proved to be a versatile platform for evaluating second-sphere effects deemed important in naturally occurring heme active sites. Advances in synthetic techniques have made it possible to install different functional groups around the porphyrin ligand, recreating artificial analogues of the proximal and distal sites encountered in the heme proteins. Using judicious choices of these substituents, several of the elegant second-sphere effects that are proposed to be important in the reactivity of key heme proteins have been evaluated under controlled environments, adding fundamental insight into the roles played by these weak interactions in nature. This review presents a detailed description of these efforts and how these have not only demystified these second-sphere effects but also how the knowledge obtained resulted in functional mimics of these heme enzymes.
合成和生物合成铁卟啉模型对 O 和 HO 的活化和还原已被证明是评估第二壳层效应的多功能平台，这些效应被认为在天然存在的血红素活性部位中很重要。合成技术的进步使得在卟啉配体周围安装不同的官能团成为可能，从而重新创建在血红素蛋白中遇到的近端和远端部位的人工类似物。通过明智地选择这些取代基，可以在受控环境下评估被认为对关键血红素蛋白反应性很重要的几种优雅的第二壳层效应，从而深入了解这些弱相互作用在自然界中所扮演的角色。这篇综述详细介绍了这些努力，以及这些努力不仅如何揭开这些第二壳层效应的神秘面纱，而且如何获得的知识导致了这些血红素酶的功能模拟物。
