The study of terbium regenerated bacterirhodopsin

Bacteriorhodopsin (bR) is the only retinal-contain- ing protein in the purple membrane of Halobacterium halobium1]. Upon illumination, the protein undergoes a photocycle and pumps protons across the cell mem-brane2,3]. It has been found that well-washed…

The study of terbium regenerated bacterirhodopsin

The localization of Terbium (Tb3+) cations binding to deionized bacteriorhodopsin (bR) has been studied by using spectroscopic methods. It was found that adding Tb3+ cations to deionized bR affects the fluorescence lifetimes of tryptophan (Trp) in bR, the wavelength of fluorescence peak shifts "blue" and the peak value of fluorescence decreases. It was also found that adding one Tb3+ cation to deionized bR can restore the purple state from its blue state obviously. The measurements of absorbance, fluorescence and lifetime of fluorescence also show that when more than three Tb3+ cations are added, no further changes can be found. It is suggested that one Tb3+ specific binding site for the color-controlling is located on the exterior of the bR trimer structure to negatively charged lipids near Trp-10 and Trp-12. Three Tb3+ cations binding per bR is needed for the regenerated bR.