Abstract
Hierarchical assemblies of the noteworthy photoactive cytochrome b562 reconstituted with zinc protoporphyrin IX covalently linked with the protein surface were constructed on a gold electrode modified with an apoprotein of cytochrome b562. The integrated photoactive hemoproteins were characterized by electrochemical impedance and quartz crystal microbalance analyses. The protein-immobilized electrode exhibits enhanced photocurrent generation relative to the one having a Zn-substituted hemoprotein monolayer.
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