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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]

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