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.
Duplications of an iron-sulphur tripeptide leads to the formation of a protoferredoxin / Scintilla, S., Bonfio, C., Belmonte, L., Forlin, M., Rossetto, D., Li, J., Cowan, J.A., Galliani, A., Arnesano, F., Assfalg, M., Mansy, S.S.. - In: CHEMICAL COMMUNICATIONS. - ISSN 1359-7345. - 2016, 52:92(2016), pp. 13456-13459. [10.1039/c6cc07912a]
Duplications of an iron-sulphur tripeptide leads to the formation of a protoferredoxin
Scintilla, Simone;Bonfio, Claudia;Belmonte, Luca;Forlin, Michele;Rossetto, Daniele;Mansy, Sheref Samir
2016-01-01
Abstract
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.| File | Dimensione | Formato | |
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