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.
