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dc.contributor.author | Saito, Keisuke | en |
dc.contributor.author | Kandori, Hideki | en |
dc.contributor.author | Ishikita, Hiroshi | en |
dc.contributor.alternative | 石北, 央 | ja |
dc.date.accessioned | 2013-02-06T05:46:58Z | - |
dc.date.available | 2013-02-06T05:46:58Z | - |
dc.date.issued | 2012-10-05 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | http://hdl.handle.net/2433/169708 | - |
dc.description.abstract | Bacteriorhodopsin (BR) functions as a light-driven proton pump, whereas Anabaena sensory rhodopsin (ASR) is believed to function as a photosensor despite the high similarity in their protein sequences. In Fourier transform infrared (FTIR) spectroscopic studies, the lowest O-D stretch for D(2)O was observed at ∼2200 cm(-1) in BR but was significantly higher in ASR (>2500 cm(-1)), which was previously attributed to a water molecule near the Schiff base (W402) that is H-bonded to Asp-85 in BR and Asp-75 in ASR. We investigated the factors that differentiate the lowest O-D stretches of W402 in BR and ASR. Quantum mechanical/molecular mechanical calculations reproduced the H-bond geometries of the crystal structures, and the calculated O-D stretching frequencies were corroborated by the FTIR band assignments. The potential energy profiles indicate that the smaller O-D stretching frequency in BR originates from the significantly higher pK(a)(Asp-85) in BR relative to the pK(a)(Asp-75) in ASR, which were calculated to be 1.5 and -5.1, respectively. The difference is mostly due to the influences of Ala-53, Arg-82, Glu-194-Glu-204, and Asp-212 on pK(a)(Asp-85) in BR and the corresponding residues Ser-47, Arg-72, Ser-188-Asp-198, and Pro-206 on pK(a)(Asp-75) in ASR. Because these residues participate in proton transfer pathways in BR but not in ASR, the presence of a strongly H-bonded water molecule near the Schiff base ultimately results from the proton-pumping activity in BR. | en |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | American Society for Biochemistry and Molecular Biology | en |
dc.rights | This research was originally published in "Journal of Biological Chemistry". Saito K., Kandori H., Ishikita H.. Factors that differentiate the H-bond strengths of water near the schiff bases in bacteriorhodopsin and Anabaena sensory rhodopsin. 2012;287:34009-34018. © the American Society for Biochemistry and Molecular Biology. | en |
dc.rights | This is not the published version. Please cite only the published version. | en |
dc.rights | この論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。 | ja |
dc.subject.mesh | Anabaena/chemistry | en |
dc.subject.mesh | Bacteriorhodopsins/chemistry | en |
dc.subject.mesh | Crystallography, X-Ray | en |
dc.subject.mesh | Deuterium Oxide/chemistry | en |
dc.subject.mesh | Hydrogen Bonding | en |
dc.subject.mesh | Protein Structure, Tertiary | en |
dc.subject.mesh | Schiff Bases | en |
dc.title | Factors that differentiate the H-bond strengths of water near the Schiff bases in bacteriorhodopsin and Anabaena sensory rhodopsin. | en |
dc.type | journal article | - |
dc.type.niitype | Journal Article | - |
dc.identifier.ncid | AA00251083 | - |
dc.identifier.jtitle | The Journal of biological chemistry | en |
dc.identifier.volume | 287 | - |
dc.identifier.issue | 41 | - |
dc.identifier.spage | 34009 | - |
dc.identifier.epage | 34018 | - |
dc.relation.doi | 10.1074/jbc.M112.388348 | - |
dc.textversion | author | - |
dc.identifier.pmid | 22865888 | - |
dcterms.accessRights | open access | - |
出現コレクション: | 学術雑誌掲載論文等 |
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