| Autor: |
Li P; Department of Chemistry, Yale University, 225 Prospect Street, New Haven, Connecticut 06520, United States., Soudackov AV; Department of Chemistry, Yale University, 225 Prospect Street, New Haven, Connecticut 06520, United States., Koronkiewicz B; Department of Chemistry, Yale University, 225 Prospect Street, New Haven, Connecticut 06520, United States., Mayer JM; Department of Chemistry, Yale University, 225 Prospect Street, New Haven, Connecticut 06520, United States., Hammes-Schiffer S; Department of Chemistry, Yale University, 225 Prospect Street, New Haven, Connecticut 06520, United States. |
| Abstrakt: |
Long-range electron transfer is coupled to proton transfer in a wide range of chemically and biologically important processes. Recently the proton-coupled electron transfer (PCET) rate constants for a series of biomimetic oligoproline peptides linking Ru(bpy) 3 2+ to tyrosine were shown to exhibit a substantially shallower dependence on the number of proline spacers compared to the analogous electron transfer (ET) systems. The experiments implicated a concerted PCET mechanism involving intramolecular electron transfer from tyrosine to Ru(bpy) 3 3+ and proton transfer from tyrosine to a hydrogen phosphate dianion. Herein these PCET systems, as well as the analogous ET systems, are studied with microsecond molecular dynamics, and the ET and PCET rate constants are calculated with the corresponding nonadiabatic theories. The molecular dynamics simulations illustrate that smaller ET donor-acceptor distances are sampled by the PCET systems than by the analogous ET systems. The shallower dependence of the PCET rate constant on the ET donor-acceptor distance is explained in terms of an additional positive, distance-dependent electrostatic term in the PCET driving force, which attenuates the rate constant at smaller distances. This electrostatic term depends on the change in the electrostatic interaction between the charges on each end of the bridge and can be modified by altering these charges. On the basis of these insights, this theory predicted a less shallow distance dependence of the PCET rate constant when imidazole rather than hydrogen phosphate serves as the proton acceptor, even though their p K a values are similar. This theoretical prediction was subsequently validated experimentally, illustrating that long-range electron transfer processes can be tuned by modifying the nature of the proton acceptor in concerted PCET processes. This level of control has broad implications for the design of more effective charge-transfer systems. |
