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

Simone Scintilla; Claudia Bonfio; Luca Belmonte; Michele Forlin; Daniele Rossetto; Jingwei Li; James A. Cowan; Angela Galliani; Fabio Arnesano; Michael Assfalg; Sheref S. Mansy

doi:10.1039/C6CC07912A

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

Simone Scintilla,^a Claudia Bonfio,^a Luca Belmonte,^a Michele Forlin,^a Daniele Rossetto,^a Jingwei Li,^b James A. Cowan,^b Angela Galliani,^c Fabio Arnesano,^c Michael Assfalg^d and Sheref S. Mansy

*^a

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* Corresponding authors

^a CIBIO, University of Trento, Via Sommarive 9, 38123 Povo, Italy
E-mail: mansy@science.unitn.it

^b Department of Chemistry and Biochemistry, The Ohio State University, 100 West 18th Ave, Columbus, OH 43210, USA

^c Department of Chemistry, University of “Bari A. Moro”, Via E. Orabona 4, 70125 Bari, Italy

^d Department of Biotechnology, University of Verona, Strada Le Grazie 15, 37134 Verona, Italy

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.

This article is part of the themed collection: Celebrating our 2019 Prize and Award winners

Chemical Communications

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

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

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