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

Journal of the American Chemical Society
J Dongun KimPaul G Falkowski

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.

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Citations

Jul 3, 2019·Proceedings of the National Academy of Sciences of the United States of America·Andrew C MutterPaul G Falkowski
Sep 6, 2019·Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry·Amanda GalambasEric M Shepard
Oct 24, 2019·Interface Focus·Stuart J Bartlett, Patrick Beckett
Mar 20, 2020·Proceedings of the National Academy of Sciences of the United States of America·Hagai RaananPaul G Falkowski
Aug 10, 2020·Biotechnology and Applied Biochemistry·Joshua A ManciniVikas Nanda
Oct 31, 2020·The FEBS Journal·Inês B TrindadeMario Piccioli
Dec 23, 2020·Dalton Transactions : an International Journal of Inorganic Chemistry·Claudia Bonfio
Nov 11, 2019·Emerging Topics in Life Sciences·Kristian Le Vay, Hannes Mutschler
Feb 27, 2020·Chemical Reviews·Moran Frenkel-PinterLuke J Leman
Nov 14, 2020·ACS Synthetic Biology·Bhanu P JagilinkiVikas Nanda

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