| How does a membrane protein achieve a vectorial proton transfer via water molecules? | |
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MedLine Citation:
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PMID: 19072873 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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We present a detailed mechanism for the proton transfer from a protein-bound protonated water cluster to the bulk water directed by protein side chains in the membrane protein bacteriorhodopsin. We use a combined approach of time-resolved Fourier transform infrared spectroscopy, molecular dynamics simulations, and X-ray structure analysis to elucidate the functional role of a hydrogen bond between Ser193 and Glu204. These two residues seal the internal protonated water cluster from the bulk water and the protein surface. During the photocycle of bacteriorhodopsin, a transient protonation of Glu204 leads to a breaking of this hydrogen bond. This breaking opens the gate to the extracellular bulk water, leading to a subsequent proton release from the protonated water cluster. We show in detail how the protein achieves vectorial proton transfer via protonated water clusters in contrast to random proton transfer in liquid water. |
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Authors:
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Steffen Wolf; Erik Freier; Klaus Gerwert |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Chemphyschem : a European journal of chemical physics and physical chemistry Volume: 9 ISSN: 1439-7641 ISO Abbreviation: Chemphyschem Publication Date: 2008 Dec |
Date Detail:
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Created Date: 2008-12-22 Completed Date: 2009-01-22 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 100954211 Medline TA: Chemphyschem Country: Germany |
Other Details:
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Languages: eng Pagination: 2772-8 Citation Subset: IM |
Affiliation:
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Department of Biophysics, ND 04 North, Ruhr-University BochumD-44780 Bochum, Germany. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Bacteriorhodopsins
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chemistry Computer Simulation Hydrogen Bonding* Membrane Proteins / chemistry* Protons* Spectroscopy, Fourier Transform Infrared Water / chemistry* X-Ray Diffraction |
| Chemical | |
Reg. No./Substance:
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0/Membrane Proteins; 0/Protons; 53026-44-1/Bacteriorhodopsins; 7732-18-5/Water |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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