Abstract

Structural stability and electrochemistry of Chlorella ferredoxin immobilized in a cast film of molecular bilayer membranes of a biological lipid, dimyristoylphosphatidylcholine (DMPC) on a quartz substrate or a pyrolytic graphite electrode were examined. A specular reflectance spectrum of the film showed that the [2Fe-2S] cluster in ferredoxin retains its original structure even in an air atmosphere. This indicates that the lipid bilayers provide suitable microenvironments for a stable immobilization of the protein. Cast films of ferredoxin + DMPC on a graphite electrode gave well-defined, nearly reversible redox waves with a formal potential of − 0.59 V vs. Ag¦AgCl, which is close to the reported value at promoter-modified electrodes, indicating that the electrochemical communication is from native ferredoxin.

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