Orientated Monolayers of Membrane Proteins Tethered to the Gold Surface and Probed by Surface-Enhanced IR Absorption Spectroscopy (SEIRAS)


Joachim Heberle

Bielefeld University, Department of Chemistry, Biophysical Chemistry, Universitätsstraße 25, 33615 Bielefeld, Germany

e-mail: joachim.heberle@uni-bielefeld.de

URL: http://www.uni-bielefeld.de/chemie/pc3/

 

Electrophysiological techniques, like patch-clamp, unravelled many functional aspects of ion channels but usually suffer from poor structural sensitivity. We have recently developed Surface Enhanced Infrared Difference Absorption Spectroscopy (SEIDAS)[1] to probe potential-induced structural changes of a protein on the level of a monolayer. A novel concept is introduced to incorporate membrane proteins into solid supported lipid bilayers in an orientated way via the affinity of the His-tag to the Ni-NTA terminated gold surface.[2,3] Full functionality of the surface tethered cytochrome c oxidase is demonstrated by cyclic voltammetry after binding of the natural electron donor cytochrome c. General applicability of the methodological approach is shown by tethering photosystem II to the gold surface.[4] In conjunction with hydrogenase, the basis is set towards a biomimetic system for H2-production.