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作 者:Yijun Dong Siqi Zhang Liang Zhao
机构地区:[1]School of Life Sciences,Tsinghua University,Beijing 100084,China [2]Key Laboratory of Bioorganic Phosphorus Chemistry&Chemical Biology,Department of Chemistry,Tsinghua University,Beijing 100084,China
出 处:《Chinese Journal of Chemistry》2022年第12期1478-1491,共14页中国化学(英文版)
摘 要:Iron-sulfur(Fe-S)proteins are among the most common type of natural metalloproteins that participate in a large range of key metabolic processes.To date,enormous research works on the exploration of protein structures and catalytic mechanisms have revealed that the active sites are generally composed of a Fe-S cluster and a highly conserved coordination environment.Accordingly,people are enlightened by the prebiotic evolution of an-cient clusters and are dedicated to the development of biosynthetic methods for modern clusters.This review aims to systemically summarize the structural development of peptide-coordinated iron-sulfur clusters from two perspectives:"bottom-up"approaches involving evolution of prebiotic chemical synthesis for natural proteins and"top-down"analyses of biosynthesis in modern biological systems for artificial metalloproteins.Moreover,current challenges and the direction of future development are also presented to provide new perspectives of developing enzyme mimics and further mechanistic studies.
关 键 词:PEPTIDES Iron-sulfur clusters Prebiotic evolution BIOSYNTHESIS Biomimetic synthesis
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