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Design of Redox-Active Peptides: Towards Functional Materials

  • Dayn Joseph Sommer
  • Rafael Alcala-Torano
  • Zahra Bahrami Dizicheh
  • Giovanna GhirlandaEmail author
Chapter
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 940)

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.

Keywords

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

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Copyright information

© Springer International Publishing Switzerland 2016

Authors and Affiliations

  • Dayn Joseph Sommer
    • 1
  • Rafael Alcala-Torano
    • 1
  • Zahra Bahrami Dizicheh
    • 1
  • Giovanna Ghirlanda
    • 1
    Email author
  1. 1.School of Molecular SciencesArizona State UniversityTempeUSA

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