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Surface-enhanced infrared difference absorption spectroscopy(SEIDAS), is developed which provides acute sensitivity to observe the minute enzymatic change of a protein on the level of a monolayer. It is demonstrated that the relative band intensities in the potential-induced difference spectra of adsorbed cytochrome c are significantly dependent on the type of chemically modified electrodes (CME) used.

Spectroscopic data is presented on vibrational changes of sensory rhodopsin II from Natronomonas pharaonis (NpSR II). The results have shown a molecular model for the physiological regulation of the photocycle of NpSR II by the potential drop across the membrane, which came about by the interplay between the change in local pH at the membrane surface and the external electric field.

The functionality of a lipid-reconstituted recombinant cytochrome c oxidase (CcO) monolayer that is specifically bound through histidine tags (His-tags) to a nickel chelating nitrilotriacetic acid (Ni-NTA)-modified gold electrode is described. The method has shown that the orientation of the membrane protein can be controlled depending on the position of the affinity tag.

The functionality of a lipid-reconstituted recombinant cytochrome c oxidase (CcO) monolayer that is specifically bound through histidine tags (His-tags) to a nickel chelating nitrilotriacetic acid (Ni-NTA)-modified gold electrode is described. The method has shown that the orientation of the membrane protein can be controlled depending on the position of the affinity tag.

A novel strategy for the reconstruction of a membrane protein monolayer in a lipid layer on a solid support is pursued. Quantum mechanical calculations are used to assign the experimentally observed vibrational frequencies of the various steps to normal modes.

The minute enzymatic changes of a protein can be studied on the level of a monolayer. The infrared difference spectra of a protein monolayer by exploiting the surface enhancement exerted by a modified gold surface are recorded.