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Second Sphere Effects on Oxygen Reduction and Peroxide Activation by Mononuclear Iron Porphyrins and Related Systems
Chemical Reviews ( IF 62.1 ) Pub Date : 2022-04-11 , DOI: 10.1021/acs.chemrev.1c01021
Sarmistha Bhunia 1 , Arnab Ghatak 1 , Abhishek Dey 1
Affiliation  

Activation and reduction of O2 and H2O2 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.

中文翻译:

单核铁卟啉和相关系统对氧还原和过氧化物活化的第二球效应

O 2和H 2 O 2的活化和还原通过合成和生物合成的铁卟啉模型已被证明是一个多功能平台,用于评估在天然存在的血红素活性位点中被认为很重要的第二层效应。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,从而重建血红素蛋白中近端和远端位点的人工类似物。使用这些取代基的明智选择,已在受控环境下评估了一些被提议对关键血红素蛋白的反应性很重要的优雅的第二球效应,从而增加了对这些弱相互作用在自然界中所起的作用的基本认识。
更新日期:2022-04-11
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