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• W2110343112 endingPage "1045" @default.
• W2110343112 startingPage "1038" @default.
• W2110343112 abstract "Abstract Light‐induced proton pumping in bacteriorhodospin is carried out through five proton transfer steps. We propose that the proton transfer to Asp85 from the Schiff base in the L‐to‐M transition is accompanied by the relocation of a water cluster on the cytoplasmic side of the Schiff base from a site close to the Schiff base in L to the Phe219‐Thr46 region in M. The water cluster present in L, formed at 170 K, is more rigid than that at room temperature. This may be responsible for blocking the conversion of L to M at 170 K. In the photocycle at room temperature, this water cluster returns to the site close to the Schiff base in N, with a rigid structure similar to that of L at 170 K. The increase in the proton affinity of Asp85, which is a prerequisite for the one‐way proton transfer in the M‐to‐N transition, is suggested to be facilitated by a structural change which disrupts interactions between Asp212 and the Schiff base, and between Asp212 and Arg82. We propose that this liberation of Asp212 is accompanied by a rearrangement of the structure of water molecules between Asp85 and Asp212, stabilizing the protonated Asp85 in M." @default.
• W2110343112 created "2016-06-24" @default.
• W2110343112 creator A5004508137 @default.
• W2110343112 creator A5008855880 @default.
• W2110343112 creator A5042710232 @default.
• W2110343112 date "2008-07-01" @default.
• W2110343112 modified "2023-10-15" @default.
• W2110343112 title "A Role for Internal Water Molecules in Proton Affinity Changes in the Schiff Base and Asp85 for One‐way Proton Transfer in Bacteriorhodopsin^†" @default.
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• W2110343112 doi "https://doi.org/10.1111/j.1751-1097.2008.00377.x" @default.
• W2110343112 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4038396" @default.
• W2110343112 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18557823" @default.
• W2110343112 hasPublicationYear "2008" @default.
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