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

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.

SUBMITTER: Kim JD

PROVIDER: S-EPMC7050467 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature

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

Kim J Dongun JD Pike Douglas H DH Tyryshkin Alexei M AM Swapna G V T GVT Raanan Hagai H Montelione Gaetano T GT Nanda Vikas V Falkowski Paul G PG

Journal of the American Chemical Society 20180829 36

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. ...[more]

PMID: 30141918

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