| The universal mechanism for iron translocation to the ferroxidase site in ferritin, which is mediated by the well conserved transit site. | |
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MedLine Citation:
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PMID: 20705053 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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Taro Masuda; Fumiyuki Goto; Toshihiro Yoshihara; Bunzo Mikami |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2010-08-10 |
Journal Detail:
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Title: Biochemical and biophysical research communications Volume: 400 ISSN: 1090-2104 ISO Abbreviation: Biochem. Biophys. Res. Commun. Publication Date: 2010 Sep |
Date Detail:
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Created Date: 2010-09-13 Completed Date: 2010-10-11 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0372516 Medline TA: Biochem Biophys Res Commun Country: United States |
Other Details:
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Languages: eng Pagination: 94-9 Citation Subset: IM |
Copyright Information:
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Copyright © 2010 Elsevier Inc. All rights reserved. |
Affiliation:
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Laboratory of Food Quality Design and Development, Division of Agronomy and Horticultural Science, Graduate School of Agriculture, Kyoto University, Gokasho, Uji, Kyoto 611-0011, Japan. masutaro@kais.kyoto-u.ac.jp |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Ceruloplasmin
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chemistry,
genetics,
metabolism* Ferritins / chemistry, genetics, metabolism* Humans Iron / metabolism* Oxidation-Reduction Protein Conformation |
| Chemical | |
Reg. No./Substance:
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0/FTH1 protein, human; 7439-89-6/Iron; 9007-73-2/Ferritins; EC 1.16.3.1/Ceruloplasmin |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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