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 language | English (US) |
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Pages (from-to) | 207-212 |
Number of pages | 6 |
Journal | Inorganica Chimica Acta |
Volume | 243 |
Issue number | 1-2 |
DOIs | |
State | Published - Feb 29 1996 |
Keywords
- Electron transfer
- Ruthenium complexes
- α-Helical peptides complexes
ASJC Scopus subject areas
- Physical and Theoretical Chemistry
- Inorganic Chemistry
- Materials Chemistry