Minimal Heterochiral de Novo Designed 4Fe-4S Binding Peptide Capable of Robust Electron Transfer

J. Dongun Kim, Douglas H. Pike, Alexei M. Tyryshkin, G. V.T. Swapna, Hagai Raanan, Gaetano T. Montelione, Vikas Nanda, Paul G. Falkowski

Research output: Contribution to journalArticlepeer-review

31 Scopus citations

Abstract

Ambidoxin is a designed, minimal dodecapeptide consisting of alternating L and D amino acids that binds a 4Fe-4S cluster through ligand-metal interactions and an extensive network of second-shell hydrogen bonds. The peptide can withstand hundreds of oxidation-reduction cycles at room temperature. Ambidoxin suggests how simple, prebiotic peptides may have achieved robust redox catalysis on the early Earth.

Original languageEnglish (US)
Pages (from-to)11210-11213
Number of pages4
JournalJournal of the American Chemical Society
Volume140
Issue number36
DOIs
StatePublished - Sep 12 2018

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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