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j.bbrc.2010.08.017.pdf | 3.89 MB | Adobe PDF | 見る/開く |
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DCフィールド | 値 | 言語 |
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dc.contributor.author | Masuda, Taro | en |
dc.contributor.author | Goto, Fumiyuki | en |
dc.contributor.author | Yoshihara, Toshihiro | en |
dc.contributor.author | Mikami, Bunzo | en |
dc.contributor.alternative | 増田, 太郎 | ja |
dc.date.accessioned | 2010-10-21T05:41:23Z | - |
dc.date.available | 2010-10-21T05:41:23Z | - |
dc.date.issued | 2010-09-10 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.uri | http://hdl.handle.net/2433/128933 | - |
dc.description.abstract | Ferritins are ubiquitous iron storage proteins. Recently, we identified a novel metal-binding site, transit site, in the crystal structure of phytoferritin. To elucidate the function of the transit site in ferritin from other species, we prepared transit-site-deficient mutants of human H ferritin, E140A and E140Q, and their iron oxidation kinetics was analyzed. The initial velocities of iron oxidization were reduced in the variants, especially in E140Q. The crystal structure of E140Q showed that the side chain of the mutated Gln140 was fixed by a hydrogen bond, whereas that of native Glu140 was flexible. These results suggest that the conserved transit site also has a function to assist with the metal ion sequestration to the ferroxidase site in ferritins from vertebrates. | en |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | Elsevier Inc. | en |
dc.rights | © 2010 Elsevier Inc. | 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 | Ferritin | en |
dc.subject | Ferroxidase site | en |
dc.subject | Metal sequestration | en |
dc.subject | Transit site | en |
dc.subject.mesh | Ceruloplasmin/chemistry | en |
dc.subject.mesh | Ceruloplasmin/genetics | en |
dc.subject.mesh | Ceruloplasmin/metabolism | en |
dc.subject.mesh | Ferritins/chemistry | en |
dc.subject.mesh | Ferritins/genetics | en |
dc.subject.mesh | Ferritins/metabolism | en |
dc.subject.mesh | Humans | en |
dc.subject.mesh | Iron/metabolism | en |
dc.subject.mesh | Oxidation-Reduction | en |
dc.subject.mesh | Protein Conformation | en |
dc.title | The universal mechanism for iron translocation to the ferroxidase site in ferritin, which is mediated by the well conserved transit site. | en |
dc.type | journal article | - |
dc.type.niitype | Journal Article | - |
dc.identifier.ncid | AA00564395 | - |
dc.identifier.jtitle | Biochemical and biophysical research communications | en |
dc.identifier.volume | 400 | - |
dc.identifier.issue | 1 | - |
dc.identifier.spage | 94 | - |
dc.identifier.epage | 99 | - |
dc.relation.doi | 10.1016/j.bbrc.2010.08.017 | - |
dc.textversion | author | - |
dc.identifier.pmid | 20705053 | - |
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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