Design of redox-active peptides: Towards functional materials

Dayn Joseph Sommer, Rafael Alcala-Torano, Zahra Bahrami Dizicheh, Giovanna Ghirlanda

Research output: Contribution to journalArticle

Abstract

In nature, the majority of processes that occur in the cell involve the cycling of electrons and protons, changing the reduction and oxidation state of substrates to alter their chemical reactivity and usefulness in vivo. One of the most relevant examples of these processes is the electron transport chain, a series of oxidoreductase proteins that shuttle electrons through well-defined pathways, concurrently moving protons across the cell membrane. Inspired by these processes, researchers have sought to develop materials to mimic natural systems for a number of applications, including fuel production. The most common cofactors found in proteins to carry out electron transfer are iron sulfur clusters and porphyrin-like molecules. Both types have been studied within natural proteins, such as in photosynthetic machinery or soluble electron carriers; in parallel, an extensive literature has developed over recent years attempting to model and study these cofactors within peptide-based materials. This chapter will focus on major designs that have significantly advanced the field.

Original languageEnglish (US)
Pages (from-to)215-243
Number of pages29
JournalAdvances in Experimental Medicine and Biology
Volume940
DOIs
StatePublished - Sep 1 2016

Keywords

  • Electron transfer
  • Functional materials
  • Hydrogenases
  • Iron sulfur clusters
  • Oxidoreductases
  • Peptide scaffolds
  • Porphyrins
  • Redox enzymes

ASJC Scopus subject areas

  • Medicine(all)
  • Biochemistry, Genetics and Molecular Biology(all)

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