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The Proton Transfers in the Cytoplasmic Domain of Bacteriorhodopsin are Facilitated by a Cluster of Interacting Residues by Leonid S. Brown; Yoichi Yamazaki; Akio Maeda; Li Sun; Richard Needleman; Janos K. Lanyi is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.
What is The Proton Transfers in the Cytoplasmic Domain of Bacteriorhodopsin are Facilitated by a Cluster of Interacting Residues about?
The stepwise internal proton transfer reactions across the membrane, and the release and uptake at the surface, are the elementary steps that together constitute the transport mechanism in a proton pump. Although the proton donor and acceptor residues can be usually identified, the directionality and the energetics of the proton transfer must be determined to a large extent also by interactions of these with neighboring groups. We have examined the roles of residues D96, T46 and R227 in proton transfers during the photocycle of bacteriorhodopsin near its cytoplasmic surface, and in general the relationship between the reprotonation of the Schiff base and the subsequent proton uptake from the cytoplasmic side. The phenotypes of single and double mutants suggest close functional interaction among D96, T46, R227, and probably internal bound water. Measurements of the free energies of activation indicate that mechanistic interpretation of the rates changed by residue replacements is hindered by a general tendency toward lowered activation enthalpies in the mutated proteins. There is less ambiguity in the free energy levels of the photointermediates. It appears from these that the inhib
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It is typically read by researchers, students, and practitioners in Biochemistry, Genetics and Molecular Biology.
- Author
- Leonid S. Brown; Yoichi Yamazaki; Akio Maeda; Li Sun; Richard Needleman; Janos K. Lanyi
- Publisher
- Elsevier BV
- Published
- 1994
- Language
- EN
- Field
- Biochemistry, Genetics and Molecular Biology (Life Sciences)