Site-specific modification of α-helical peptides with electron donors and acceptors

Bassil I. Dahiyat, Thomas J. Meade*, Stephen L. Mayo

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

14 Scopus citations

Abstract

We have prepared a histidine containing monomeric α-helical peptide, ETH6 (A2KA4KA2HA6HA4KA 4K) in order to study long-range electron transfer (ET). This peptide was site-specifically labeled with a ruthenium (donor) at one histidine and a second ruthenium (acceptor) at a second histidine located on the same peptide. Both the unlabeled peptide and the singly labeled peptide-metal complex, Ru(bpy)2(im)(His)-ETH6, were shown to form stable monomeric α-helical structures as determined by circular dichroism. Ru(NH3)4(py) was coupled to Ru(bpy)2(im)(His)-ETH6, forming a Ru(bpy)2(im)(His)-ETH6-(His)Ru(NH3)4(py) donor-acceptor complex. The synthesis and characterization of these peptides provide an entry into a series of molecules that are ideally suited to evaluate pathway differences such as H-bond mediated versus backbone-coupled long-range ET in protein α-helices.

Original languageEnglish (US)
Pages (from-to)207-212
Number of pages6
JournalInorganica Chimica Acta
Volume243
Issue number1-2
DOIs
StatePublished - Feb 29 1996

Keywords

  • Electron transfer
  • Ruthenium complexes
  • α-Helical peptides complexes

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Inorganic Chemistry
  • Materials Chemistry

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