Examining the Effects of Homochirality for Electron Transfer in Protein Assemblies.

Protein voltammetry studies of cytochrome c , immobilized on chiral tripeptide monolayer films, reveal the importance of the electron spin and the film's homochirality on electron transfer kinetics. Magnetic film electrodes are used to examine how an asymmetry in the standard heterogeneous electron transfer rate constant arises from changes in the electron spin direction and the enantiomer composition of the tripeptide monolayer; rate constant asymmetries as large as 60% are observed. These findings are rationalized in terms of the chiral induced spin selectivity effect and spin-dependent changes in electronic coupling. Lastly, marked differences in the average rate constant are shown between homochiral ensembles, in which the peptide and protein possess the same enantiomeric form, compared to heterochiral ensembles, where the handedness of the peptide layer is opposite to that of the protein or itself comprises heterochiral building blocks. These data demonstrate a compelling rationale for why nature is homochiral; namely, spin alignment in homochiral systems enables more efficient energy transduction.