ArticleProceedings of the National Academy of Sciences of the United States of America2005
Proton binding within a membrane protein by a protonated water cluster.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed.
- Revealing the glutamate switch: Insights into proton translocation in plant HBiophysical journal · 2025Article
- A second photoactivatable state of the anion-conducting channelrhodopsin GtACR1 empowers persistent activity.Communications biology · 2025Article
- NaMolecules (Basel, Switzerland) · 2023Review
- A Proteorhodopsin-Related Photosensor Expands the Repertoire of Structural Motifs Employed by Sensory Rhodopsins.The journal of physical chemistry. B · 2023Article
- Voltage Imaging with Engineered Proton-Pumping Rhodopsins: Insights from the Proton Transfer Pathway.ACS physical chemistry Au · 2023Review
- Structures of channelrhodopsin paralogs in peptidiscs explain their contrasting KNature communications · 2023Article
- Article
- True-atomic-resolution insights into the structure and functional role of linear chains and low-barrier hydrogen bonds in proteins.Nature structural & molecular biology · 2022Article
- Anharmonic Vibrational Calculations Based on Group-Localized Coordinates: Applications to Internal Water Molecules in Bacteriorhodopsin.Journal of chemical theory and computation · 2021Article
- Time-resolved spectroscopic and electrophysiological data reveal insights in the gating mechanism of anion channelrhodopsin.Communications biology · 2021Article
- The crystal structures of a chloride-pumping microbial rhodopsin and its proton-pumping mutant illuminate proton transfer determinants.The Journal of biological chemistry · 2020Article
- Collective exchange processes reveal an active site proton cage in bacteriorhodopsin.Communications biology · 2020Article
- X-ray structure analysis of bacteriorhodopsin at 1.3 Å resolution.Scientific reports · 2018Article
- Orientation of non-spherical protonated water clusters revealed by infrared absorption dichroism.Nature communications · 2018Article
- pH-sensitive vibrational probe reveals a cytoplasmic protonated cluster in bacteriorhodopsin.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Time-resolved infrared spectroscopy in the study of photosynthetic systems.Photosynthesis research · 2017Review
- Molecular Basis for Differential Anion Binding and Proton Coupling in the Cl(-)/H(+) Exchanger ClC-ec1.Journal of the American Chemical Society · 2016Article
- Proton transfer-mediated GPCR activation.Protein & cell · 2015Review
- Light-driven Na(+) pump from Gillisia limnaea: a high-affinity Na(+) binding site is formed transiently in the photocycle.Biochemistry · 2014Article
- Density functional tight binding: values of semi-empirical methods in an ab initio era.Physical chemistry chemical physics : PCCP · 2014Article
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4 authors.
Funding
Abstract
Proton transfer is crucial for many enzyme reactions. Here, we show that in addition to protonatable amino acid side chains, water networks could constitute proton-binding sites in proteins. A broad IR continuum absorbance change during the proton pumping photocycle of bacteriorhodopsin (bR) indicates most likely deprotonation of a protonated water cluster at the proton release site close to the surface. We investigate the influence of several mutations on the proton release network and the continuum change, to gain information about the location and extent of the protonated water network and to reveal the participating residues necessary for its stabilization. We identify a protonated water cluster consisting in total of one proton and about five water molecules surrounded by six side chains and three backbone groups (Tyr-57, Arg-82, Tyr-83, Glu-204, Glu-194, Ser-193, Pro-77, Tyr-79, and Thr-205). The observed perturbation of proton release by many single-residue mutations is now explained by the influence of numerous side chains on the protonated H bonded network. In situ hydrogen/deuterium exchange Fourier transform IR measurements of the bR ground state, show that the proton of the release group becomes localized on Glu-204 and Asp-204 in the ground state of the mutants E194D and E204D, respectively, even though it is delocalized in the ground state of wild-type bR. Thus, the release mechanism switches between the wild-type and mutated proteins from a delocalized to a localized proton-binding site.
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