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Issue 92, 2016
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Duplications of an iron–sulphur tripeptide leads to the formation of a protoferredoxin

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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.

Graphical abstract: Duplications of an iron–sulphur tripeptide leads to the formation of a protoferredoxin

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Publication details

The article was received on 29 Sep 2016, accepted on 25 Oct 2016 and first published on 25 Oct 2016


Article type: Communication
DOI: 10.1039/C6CC07912A
Citation: Chem. Commun., 2016,52, 13456-13459
  • Open access: Creative Commons BY license
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    Duplications of an iron–sulphur tripeptide leads to the formation of a protoferredoxin

    S. Scintilla, C. Bonfio, L. Belmonte, M. Forlin, D. Rossetto, J. Li, J. A. Cowan, A. Galliani, F. Arnesano, M. Assfalg and S. S. Mansy, Chem. Commun., 2016, 52, 13456
    DOI: 10.1039/C6CC07912A

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