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  • Title: Changes in the protonation state of bacterio-opsin during reconstitution of bacteriorhodopsin.
    Author: Fischer UC, Oesterhelt D.
    Journal: Biophys J; 1980 Jul; 31(1):139-45. PubMed ID: 6268211.
    Abstract:
    Protonation changes of the protein occur during the reconstitution of bacteriorhodopsin from bacterio-opsin and all-trans retinal in the purple membrane of Halobacterium halobium. The protonation changes are conveniently determined from measures of the pH changes after photoisomerisation of 9-cis retinal in apomembrane preparations, which induces the reconstitution. In addition, to the omega-amino group of the lysine which is involved in the condensation of retinal and bacterio-opsin, the dissociation equilibria of at least two other amino acid residues are changed during the reconstitution. The results are consistent with a proposed model of chromophore structure in which an interaction of the Schiff's base occurs with two protonable amino acid residues.
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