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.
Minimal Heterochiral de Novo Designed 4Fe-4S Binding Peptide Capable of Robust Electron Transfer.
J. Dongun Kim,Douglas Pike,A. Tyryshkin,G. Swapna,Hagai Raanan,G. Montelione,Vikas Nanda,P. Falkowski
Published 2018 in Journal of the American Chemical Society
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- Publication year
2018
- Venue
Journal of the American Chemical Society
- Publication date
2018-08-24
- Fields of study
Medicine, Chemistry
- Identifiers
- External record
- Source metadata
Semantic Scholar, PubMed
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