Evidence for fast and discriminatory electron transfer of proteins at modified gold electrodes

Abstract

The electrochemistry of the redox proteins, cytochrome c, cytochrome b₅, plastocyanin and ferredoxin at modified gold electrodes has been examined on the basis that electron transfer takes place at electroactive sites which are microscopic in size. Using this model, it is now proposed that electrochemistry of these proteins occurs at suitably modified sites with fast rates at potentials near the standard redox potential. The microscopic model implies that redox proteins and enzymes take part in fast electron transfer at specific sites on the electrode, other sites being completely ineffective. This form of molecular recognition, i.e. the ability to discriminate between the different sites on an electrode surface, mimics homogeneous redox reactions wherein redox active proteins ‘recognize’ their biological partners in a very specific sense. Previously, protein electrochemistry has been interpreted via use of a macroscopic model in which the proteins are transported to the electrode surface by linear diffusion followed by quasi-reversible or irreversible electron transfer to the electrode surface. The microscopic model, which assumes that the movement of the protein occurs predominantly by radial diffusion to very small sites, would appear to explain the data more satisfactorily and be consistent with biologically important, homogeneous redox reactions which are known to be fast.