Abstract
Investigation of electron transfer in synthetic polypeptides provides an important probe of how charge entrainment is mediated in redox-active proteins, including photosynthetic reaction centers. Interest in this field has focused increasingly on experimental probes of photoinduced electron transfer kinetics and thermodynamics, and the influence of various features of polypeptide templates (e.g. the hydrogen bonding network, the permanent dipole moment for α-helices) that assemble redox groups for long range charge transfer. A review of the various approaches is presented here with attention to heliogenic peptides and the mediation of photoinduced charge entrainment.
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