Photoinduced electron transfer in α-helical polypeptides: dependence on conformation and electron donor-acceptor distance

Long distance electron transfer in proteins is a multiple-pathway process whose kinetics is modulated by the dynamics of flexible peptide chains. Such complexity can be observed even in relatively simple systems, e.g. donor-bridge-acceptor, where the bridge is a polypeptide α-helix. We have investigated a series of 24-residue helical polypeptides that exist as monomers in water-alcohol media. The principal chromophore and electron acceptor, a pyrene moiety, is connected to the N-terminus via a flexible linker. The electron donor, a tryptophan residue, was placed various distances away from the pyrene-labeled terminus. Time-resolved emission spectroscopy, associated with the fluorescent pendant, pyrene, was employed to study the photoinduced electron-transfer kinetics for the polypeptide analogs. Mechanisms involving only through-bond pathways could not account for the pattern of measured fast charge-separation rates. When the electron donor was placed far enough from the acceptor (i.e. at least six residues apart), a decrease in the electron-transfer rates with the donor-acceptor distance was observed. The emission decays for polypeptides with the electron donor exhibited complex behavior and could not be fit using a single-exponential function. For the treatment of the time-resolved data, a multi-exponential model was developed that is based on the assumption of a Gaussian distribution of the classical electronic coupling β values among the conformers responsible for the observed electron-transfer processes. This approach proved to be informative because, in addition to the mean values of the electron-transfer rate constants, the widths of the distributions of these rates illustrate the size of the conformational space explored by the flexible chains that provide pathways for electron transfer.