Catalysis of electron transfer across phospholipid bilayers by iron-porphyrin complexes

Phospholipid vesicles containing K₃Fe(CN)₆ were prepared from egg yolk phosphatidylcholine. Hemin dimethyl ester was incorporated into these vesicles during preparation in ratios of phospholipid to hemin dimethyl ester that varied from 200 : 1 to 45000 : 1. Electron transfer across the bilayer was measured anaerobically after injecting the vesicles into a solution containing reduced indigotetrasulfonic acid. Vesicles containing hemin dimethyl ester exhibited high rates of electron transfer (240 electrons/molecule hemin dimethyl ester per min). Conditions could be selected where the rate-limiting step for catalysis was either the bimolecular reaction between ferric hemin dimethyl ester and reduced indigotetrasulfonic acid or the movement of hemin dimethyl ester from interface to interface. The hemin dimethyl ester-catalyzed electron transfer went to completion within a few seconds, completely oxidizing the reduced indigotetrasulfonic acid. Valinomycin (in the presence of potassium) and carbonyl cyanide p-trifluoromethoxyphenylhydrazone were without effect on catalyzed electron transport. Thus, the electron transport is not electrogenic but is a coupled, neutral system. By specific assay, neither phosphate nor cyanide was significantly transported during electron transfer but evidence is provided to suggest that a coordinated hydroxide accompanies movement of Fe(III) hemin dimethyl ester from the inside surface to the outside surface of the bilayer. It was also demonstrated in a bulk phase transport system that hemin dimethyl ester readily catalyzes transfer of S¹⁴CN^- through a chloroform layer separating two aqueous phases. Another more hydrophobic iron-porphyrin complex, Fe(III) tetraphenylporphyrin, was found to be twice as effective as hemin dimethyl ester. Other porphyrin complexes were also tested as control systems. No significant catalysis was found for metal-free protoporphyrin IX dimethyl ester or Ni(II) tetraphenylporphyrin. The results are discussed in comparison with in vivo electron transport and the future usefulness of this model system.