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

ASSFALG, Michael;
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.
2016
iron-sulfur cluster,origin of life, protoferredoxin
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11562/951948
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