铁硫三肽的重复导致原ferredoxin的形成。
Duplications of an iron-sulphur tripeptide leads to the formation of a protoferredoxin.
作者信息
Scintilla Simone, Bonfio Claudia, Belmonte Luca, Forlin Michele, Rossetto Daniele, Li Jingwei, Cowan James A, Galliani Angela, Arnesano Fabio, Assfalg Michael, Mansy Sheref S
机构信息
CIBIO, University of Trento, Via Sommarive 9, 38123 Povo, Italy.
Department of Chemistry and Biochemistry, The Ohio State University, 100 West 18th Ave, Columbus, OH 43210, USA.
出版信息
Chem Commun (Camb). 2016 Nov 10;52(92):13456-13459. doi: 10.1039/c6cc07912a.
Based on UV-Vis, NMR, and EPR spectroscopies and DFT and molecular dynamics calculations, a model prebiotic [2Fe-2S] tripeptide was shown to accept and donate electrons. Duplications of the tripeptide sequence led to a protoferredoxin with increased stability. Duplications of primitive peptides may have contributed to the formation of contemporary ferredoxins.
基于紫外可见光谱、核磁共振光谱和电子顺磁共振光谱以及密度泛函理论和分子动力学计算，一种模型益生元[2Fe-2S]三肽被证明能够接受和传递电子。三肽序列的重复导致了一种稳定性增强的原铁氧化还原蛋白。原始肽的重复可能有助于当代铁氧化还原蛋白的形成。
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