Supramolecular protein polymers: When a heme moiety was introduced to the surface of an apo-cytochrome b(562)(H63C) mutant, supramolecular polymers formed through noncovalent heme-heme pocket interactions. The incorporation of a heme triad as a pivot molecule in the protein polymer further led to a two-dimensional protein network structure, which was visualized by tapping-mode atomic force microscopy (see picture).

All connected: a protein-immobilized electrode comprising hierarchical assemblies of photoactive cytochrome b(562) reconstituted with zinc protoporphyrin IX exhibits remarkably enhanced photocurrent generation relative to an electrode bearing a single zinc-substituted hemoprotein layer. The protein oligomers, which bear a covalently linked protoporphyrin group, assemble by a supramolecular heme/heme pocket interaction.

No 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.

Supramolekulare Proteinpolymere: Wenn eine Hämeinheit an der Oberfläche einer Apo‐Cytochrom‐b562(H63C)‐Mutante eingeführt wird, entstehen durch nichtkovalente Wechselwirkungen zwischen Hämtaschen supramolekulare Polymere. Der Einbau einer Hämtriade als Angelmolekül in das Proteinpolymer führt zu einer zweidimensionalen Proteinnetzwerkstruktur, die mithilfe der Rasterkraftmikroskopie im intermittierenden Modus sichtbar gemacht wurde (siehe Bild).