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Volume 270, Number 23, Issue of June 9, pp. 13860-13868, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.

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Itay Rousso , Igor Brodsky , Aaron Lewis , Mordechai Sheves

A system is described that allows for the delineation of the factors that effect the complexation of retinal to the apoprotein of bacteriorhodopsin. This complexation is investigated in various states of hydration, in HO and DO, at a variety of pH levels, with mutant membranes and labeled retinals. The complexation reaction was also investigated using absorption spectroscopy and vibrational spectra using difference Fourier transform infrared spectroscopy. The results demonstrate the crucial role of water in controlling the protein conformations that lead to protein/ligand binding reactions and begin to shed new light on the protein control of a reaction that normally cannot take place in an aqueous medium.

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