Electron transfer between myoglobin and electrodes in thin films of phosphatidylcholines and dihexadecylphosphate.

Myoglobin (Mb) in thin films of phosphatidyl cholines (PC) or dihexadecyl phosphate (DHP) gave direct, reversible electron transfer between pyrolytic graphite electrodes and the heme Fe(III)/Fe(II) redox couple of the protein. PC films incorporated much more Mb than DHP films. A model assuming several classes of electroactive sites in the films on the electrode with a dispersion of standard potentials successfully fit square-wave voltammetric data at pulse heights > 50 mV. Electron transfer rate constants in PC and DHP films were significantly larger than for Mb in thin films of an insoluble cationic surfactant. The pH dependence of the formal potential of Mb in the PC films suggested that protonation, possibly inducing conformational change, accompanies electron transfer to MbFe(III) between pH 5 and 11. Mb in PC films was used for catalysis of the reduction of trichloroacetic acid.