A Role for Internal Water Molecules in Proton Affinity Changes in the Schiff Base and Asp85 for One-way Proton Transfer in Bacteriorhodopsin
نویسندگان
چکیده
منابع مشابه
Conformational Effects on the Proton Affinity of the Schiff Base in Bacteriorhodopsin: A Density Functional Study
Density functional theory (DFT) calculations have been performed on a number of Schiff base structures related to the retinal Schiff base in bacteriorhodopsin (BR). The proton affinity (PA) of the Schiff base group was calculated in species with different lengths of the conjugated double-bond system and at different cis/trans isomerization states. The results show that the length of the conjuga...
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15 صفحه اولTwo groups control light-induced Schiff base deprotonation and the proton affinity of Asp85 in the Arg82 his mutant of bacteriorhodopsin.
Arg(82) is one of the four buried charged residues in the retinal binding pocket of bacteriorhodopsin (bR). Previous studies show that Arg(82) controls the pK(a)s of Asp(85) and the proton release group and is essential for fast light-induced proton release. To further investigate the role of Arg(82) in light-induced proton pumping, we replaced Arg(82) with histidine and studied the resulting p...
متن کاملProton affinity changes driving unidirectional proton transport in the bacteriorhodopsin photocycle.
Bacteriorhodopsin is the smallest autonomous light-driven proton pump. Proposals as to how it achieves the directionality of its trans-membrane proton transport fall into two categories: accessibility-switch models in which proton transfer pathways in different parts of the molecule are opened and closed during the photocycle, and affinity-switch models, which focus on changes in proton affinit...
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ژورنال
عنوان ژورنال: Photochemistry and Photobiology
سال: 2008
ISSN: 0031-8655,1751-1097
DOI: 10.1111/j.1751-1097.2008.00377.x