Membrane Proteins in Tethered Bilayer Lipid Membranes

Renate Naumann and Wolfgang Knoll

The tethered Bilayer Lipid Membrane, tBLM, has been introduced as a model system of the biological membrane. Membrane proteins are shown to incorporate in a functionally active form into tBLMs in two different formats:

Thiolipid-based tBLMs have been used to incorporate porines, ion carriers and channels such as hemolysin, valinomycin, melittin, gramicidin [1], MaxiK, the M2 channel of the AChR. The kinetics of ion transport has been analysed using impedance measurements. The spectra are simulated using the computer program Spice designed to analyze bioelectrochemical processes.

Larger complex proteins such as the cytochrome c oxidase from Rh. sphaeroidis, CcO, are incorporated in the so-called protein-tethered Bilayer Lipid Membrane (ptBLM) developed in our laboratories. Recombinant CcO is immobilized gold surface to a nickel chelating nitrilo-triacetic acid (NTA) surface. The CcO monolayer is reconstituted into the lipid by in-situ dialysis.

Direct electron exchange between the gold electrode and the CuA redox center of the CcO is then investigated by electrochemical methods combined in a spectroelectrochemical cell with surface enhanced resonance raman spectroscopy (SERRS) .

The combined information is discussed in terms of current models of the mechanism of the CcO.

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