Abstract
Abstract Bacterial photosynthetic antenna polypeptide (LH1-α) was synthesized as a water-soluble fusion protein with maltose-binding protein (MBP) and a His-tag portion (MBP–rubα-YH) using an E. coli expression system. Reconstitution experiments indicated that LH1-type complexes with pigments were successfully formed, regardless of the presence of a large hydrophilic MBP portion. The reconstituted complex was immobilized onto a Au electrode via a His-tag–Ni–NTA interaction. When the complex was incorporated into a planar lipid bilayer, protruding MBP portions were clearly observed by AFM.
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