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最小异手性从头设计的 4Fe-4S 结合肽,能够进行稳健的电子转移。

Minimal Heterochiral de Novo Designed 4Fe-4S Binding Peptide Capable of Robust Electron Transfer.

机构信息

Environmental Biophysics and Molecular Ecology Program, Department of Marine and Coastal Sciences, Rutgers , the State University of New Jersey , New Brunswick , New Jersey 08901 , United States.

Center for Advanced Biotechnology and Medicine , Rutgers, the State University of New Jersey , Piscataway , New Jersey 08854 , United States.

出版信息

J Am Chem Soc. 2018 Sep 12;140(36):11210-11213. doi: 10.1021/jacs.8b07553. Epub 2018 Aug 29.

Abstract

Ambidoxin is a designed, minimal dodecapeptide consisting of alternating L and D amino acids that binds a 4Fe-4S cluster through ligand-metal interactions and an extensive network of second-shell hydrogen bonds. The peptide can withstand hundreds of oxidation-reduction cycles at room temperature. Ambidoxin suggests how simple, prebiotic peptides may have achieved robust redox catalysis on the early Earth.

摘要

两性霉素是一种设计的、最小的十二肽,由交替的 L 和 D 氨基酸组成,通过配体-金属相互作用和广泛的第二壳层氢键网络结合 4Fe-4S 簇。该肽在室温下可以承受数百个氧化还原循环。两性霉素表明,简单的、前生物肽可能在早期地球上实现了强大的氧化还原催化作用。

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