Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 400, Issue 1, Pages 94-99Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2010.08.017
Keywords
Ferritin; Ferroxidase site; Metal sequestration; Transit site
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Funding
- Ministry of Education, Culture, Sports, Science and Technology of Japan [22780303]
- Shorai Foundation for Science and Technology
- Grants-in-Aid for Scientific Research [22780303] Funding Source: KAKEN
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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. (C) 2010 Elsevier Inc. All rights reserved.
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