Issue 92, 2016

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

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

Supplementary files

Article information

Article type
Communication
Submitted
29 sen 2016
Accepted
25 okt 2016
First published
25 okt 2016
This article is Open Access
Creative Commons BY license

Chem. Commun., 2016,52, 13456-13459

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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