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The objective of this project is to use primarily an electrochemical approach to study the fundamental molecular processes that underlie the light-mediated sensory and energy transduction in model retinal protein membranes. Most light-mediated energy transducing membranes utilize chlorophyll protein complexes as the 'reaction centers' whereas most light-mediated sensory transducing membranes utilize retinal proteins as the light-sensing elements. At a superficial level the only thing in common to both types of membranes is the asymmetrical orientation of the membrane-bound pigment-proteins. The retinal protein, bacteriorhodopsin, from the purple membrane of Halobacterium halobium is a light-driven proton pump. It is unique in the sense that it is similar to the visual pigment rhodopsin chemically but similar to the chlorophyll protein complexes functionally. The bacteriorhodopsin system thus presents an unusual opportunity to gain insights into possible common designs in the photosynthetic and the visual membranes.
This book presents a peer-reviewed selection of the papers of a symposium on interfacial phenomena in biotechnology and materials processing, held in conjunction with the 18th Annual Meeting of the Fine Particle Society. It is of particular interest to researchers, graduate students, and all involved in biotechnology, ceramics, superconducting materials, biomedical applications, minerals and energy conservation.