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DCフィールド | 値 | 言語 |
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dc.contributor.author | Saito, Keisuke | en |
dc.contributor.author | Ishikita, Hiroshi | en |
dc.contributor.alternative | 石北, 央 | ja |
dc.date.accessioned | 2013-02-06T06:58:09Z | - |
dc.date.available | 2013-02-06T06:58:09Z | - |
dc.date.issued | 2012-11-29 | - |
dc.identifier.issn | 0006-3002 | - |
dc.identifier.uri | http://hdl.handle.net/2433/169709 | - |
dc.description.abstract | The photoactive chromophore of photoactive yellow protein (PYP) is p-coumaric acid (pCA). In the ground state, the pCA chromophore exists as a phenolate anion, which is H-bonded by protonated Glu46 (O(Glu46)-O(pCA)=~2.6Å) and protonated Tyr42. On the other hand, the O(Glu46)-O(pCA) H-bond was unusually short (O(Glu46)-O(pCA)=2.47Å) in the intermediate pR(CW) state observed in time-resolved Laue diffraction studies. To understand how the existence of the unusually short H-bond is energetically possible, we analyzed the H-bond energetics adopting a quantum mechanical/molecular mechanical (QM/MM) approach based on the atomic coordinates of the PYP crystal structures. In QM/MM calculations, the O(Glu46)-O(pCA) bond is 2.60Å in the ground state, where Tyr42 donates an H-bond to pCA. In contrast, when the hydroxyl group of Tyr42 is flipped away from pCA, the H-bond was significantly shortened to 2.49Å in the ground state. The same H-bond pattern reproduced the unusually short H-bond in the pR(CW) structure (O(Glu46)-O(pCA)=2.49Å). Intriguingly, the potential-energy profile resembles that of a single-well H-bond, suggesting that the pK(a) values of the donor (Glu46) and acceptor (pCA) moieties are nearly equal. The present results indicate that the "equal pK(a)" requirement for formation of single-well or low-barrier H-bond (LBHB) is satisfied only when Tyr42 does not donate an H-bond to pCA, and argue against the possibility that the O(Glu46)-O(pCA) bond is an LBHB in the ground state, where Tyr42 donates an H-bond to pCA. | en |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.rights | © 2012 Elsevier B.V. | 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.rights | This is not the published version. Please cite only the published version. | en |
dc.subject | Low-barrier hydrogen bond | en |
dc.subject | Proton transfer | en |
dc.subject | Photoactive yellow protein | en |
dc.subject | Laue diffraction crystallography | en |
dc.subject | [1]H NMR | en |
dc.title | Formation of an unusually short hydrogen bond in photoactive yellow protein. | en |
dc.type | journal article | - |
dc.type.niitype | Journal Article | - |
dc.identifier.ncid | AA00564635 | - |
dc.identifier.jtitle | Biochimica et biophysica acta | en |
dc.identifier.volume | 1827 | - |
dc.identifier.issue | 3 | - |
dc.identifier.spage | 387 | - |
dc.identifier.epage | 394 | - |
dc.relation.doi | 10.1016/j.bbabio.2012.11.009 | - |
dc.textversion | author | - |
dc.identifier.pmid | 23201477 | - |
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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