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Engineering Synthetic Electron Transfer Chains from Metallopeptide Membranes.

Anthony Sementilli, Rolando F Rengifo, Wei Li

  • 1Department of Chemistry, Trinity University, San Antonio, Texas 78212, United States.

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Researchers created a synthetic peptide-copper assembly mimicking electron transfer chains (ETC). This biomimetic system demonstrates efficient electron shuttling, similar to natural cupredoxins, within a peptide membrane.

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Area of Science:

  • Biochemistry
  • Bioinorganic Chemistry
  • Materials Science

Background:

  • Copper cupredoxins are vital electron transfer chain (ETC) proteins.
  • Understanding their energetic and geometric features is key to designing artificial electron transfer systems.
  • Synthetic scaffolds can mimic biological electron transfer functionalities.

Purpose of the Study:

  • To create a synthetic peptide-copper assembly that mimics the function of cupredoxins in electron transfer.
  • To investigate the structural and electronic properties of copper sites within a self-assembled peptide bilayer.
  • To explore the mechanism of electron transfer in this artificial system.

Main Methods:

  • Templating a synthetic nonapeptide (HHQALVFFA-NH2) with copper ions to form cross-β bilayer assemblies.
  • Utilizing electron spin echo envelope modulation and X-ray absorption spectroscopies to characterize copper sites.
  • Employing restrained molecular dynamics to model the peptide bilayer architecture.
  • Conducting cyclic voltammetry to study electron transfer mechanisms.

Main Results:

  • The synthetic assemblies exhibit copper sites with blue-shifted electronic transitions and high reduction potentials, akin to plastocyanin.
  • Square planar Cu(II) sites coordinated by a single histidine ligand were identified.
  • Molecular dynamics simulations confirmed metal ion coordination stabilizing the peptide interface.
  • Cyclic voltammetry revealed a charge-hopping mechanism for electron transfer between copper centers spaced 10-12 Å apart.

Conclusions:

  • The metal-templated peptide scaffold successfully mimics cupredoxin functionality and electron shuttle capabilities.
  • This system represents a novel peptide membrane-localized electron transport chain.
  • The high reduction potential is attributed to factors beyond simple geometric distortion (entasis).