|Björn Heidel1 and Norbert Hampp1,2
1Faculty of Chemistry, University of Marburg, Hans-Meerwein-Straße, 35032 Marburg, Germany
2Material Science Center Marburg, D-35032 Marburg, Germany
The deep purple retinal-protein complex bacteriorhodopsin (BR) is the major photosynthetic protein of the archeon Halobacterium salinarum. As a light-driven proton pump it exemplifies a vectorial catalysis which energizes a nuber of cellular processes, such as ATP generation by ATPase, secondary active transport of amino acids and rotation of the flagellar motor.
In the purple membrane form (PM) bacteriorhodopsin receives a functionally significant chemical and thermodynamic stability. BR comprises three basic molecular functions which may be used in technical applications: photoelectric, photochromic, and proton transport properties. The main problem in term of this applications is to get a high degree of orientation of the PM patches. Therefore specific genetic modifications of BR are necessary to arrange two- and threedimensional structures which also include a high potential for specific fusion proteins.