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  • Title: Crystal structures of bR(D85S) favor a model of bacteriorhodopsin as a hydroxyl-ion pump.
    Author: Facciotti MT, Rouhani S, Glaeser RM.
    Journal: FEBS Lett; 2004 Apr 30; 564(3):301-6. PubMed ID: 15111113.
    Abstract:
    Structural features on the extracellular side of the D85S mutant of bacteriorhodopsin (bR) suggest that wild-type bR could be a hydroxyl-ion pump. A position between the protonated Schiff base and residue 85 serves as an anion-binding site in the mutant protein, and hydroxyl ions should have access to this site during the O-intermediate of the wild-type bR photocycle. The guanidinium group of R82 is proposed (1) to serve as a shuttle that eliminates the Born energy penalty for entry of an anion into this binding pocket, and conversely, (2) to block the exit of a proton or a related proton carrier.
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