Evidence against the hopping mechanism as an important electron transfer pathway for conformationally constrained oligopeptides.
The rate constant of intramolecular electron transfer through oligopeptides based on the alpha-aminoisobutyric acid residue was determined as a function of the peptide length and found to depend weakly on the donor-acceptor separation. By measuring the electron-transfer activation energy and estimating the energy gap between donor and bridge, we were able to discard the electron hopping mechanism.
Polo
Federico
F
Dipartimento di Scienze Chimiche, Università di Padova, via Marzolo 1, 35131 Padova, Italy.
Antonello
Sabrina
S
Formaggio
Fernando
F
Toniolo
Claudio
C
Maran
Flavio
F
D000577:Amides / Q000737:chemistry; D000621:Aminoisobutyric Acids / Q000737:chemistry*; D001565:Benzoates / Q000737:chemistry; D004563:Electrochemistry; D004583:Electrons; D006860:Hydrogen Bonding; D009842:Oligopeptides / Q000737:chemistry*; D011487:Protein Conformation
D000577:Amides; D000621:Aminoisobutyric Acids; D001565:Benzoates; D009842:Oligopeptides; C100049:2-aminoisobutyric acid; C097383:4-cyanobenzoic acid