Electron Transfer through H-bonded Peptide Assemblies
Citations Over TimeTop 20% of 2004 papers
Abstract
A series of ferrocene (Fc)- and cystamine (CSA)-labeled peptides of the sequence [Fc-(Pro-Pro-Gly)n-CSA]2, where n = 1−3, was synthesized and characterized. Peptide 3 forms a trimeric supramolecular structure held together with extensive hydrogen bonding and adopts a collagen-like motif in solution. Cyclic voltammetry (CV) and chronoamperometry (CA) were used to calculate electron-transfer (ET) kinetics. ET rates were 10.9 (2.3) × 103, 6.6 (1.9) × 103, and 4.2 (1.2) × 103 s-1 for peptides where n = 1, 2, and 3, respectively. The peptides, under deuterated conditions (D2O, full exchange of H for D), showed rate constants of 7.3 (1.3) × 103, 5.8 (1.0) × 103, and 3.4 (0.5) × 103 s-1 for n = 1, 2, and 3, respectively. A linear dependence of the ET rate constant and distance is found.
Related Papers
- → The Redox Behaviour of Randomly Dispersed Single Walled Carbon Nanotubes both in the Absence and in the Presence of Adsorbed Glucose Oxidase(2006)48 cited
- → Theoretical aspects of electrochemistry at low temperature(2021)6 cited
- → Ferrocene-Containing DNA Monolayers: Influence of Electrostatics on the Electron Transfer Dynamics(2021)8 cited
- → Electron transfer coupling of diffusional pathways Potential step chronoamperometry and cyclic voltammetry of cobalt(II) tetraphenylprophyrin and 4-nitrotoluene in dimethylformamide solutions(1985)20 cited
- Synthesis and Structure of a Hydrogen-bonding Assembled Three-dimensional Supramolecular Indium(III) Compound Involving One-dimensional Helices(2009)