| Abstract
| - A novel concept is introduced for the oriented incorporation of membrane proteins into solidsupported lipid bilayers. Recombinant cytochrome c oxidase solubilized in detergent was immobilized ona chemically modified gold surface via the affinity of its histidine-tag to a nickel-chelating nitrilo-triaceticacid (NTA) surface. The oriented protein monolayer was reconstituted into the lipid environment by detergentsubstitution. The individual steps of the surface modification, including (1) chemical modification of thegold support, (2) adsorption of the protein, and (3) reconstitution of the lipid bilayer, were followed in situby means of surface-enhanced infrared absorption spectroscopy (SEIRAS) and accompanied by normal-mode analysis. The high surface sensitivity of SEIRAS allows for the identification of each chemical reactionprocess within the monolayer at the molecular level. Finally, full functionality of the surface-tetheredcytochrome c oxidase was demonstrated by cyclic voltammetry after binding of the natural electron donorcytochrome c.
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