Spectroscopic evidence for the role of a site of the di-iron catalytic center of ferritins in tuning the kinetics of Fe(ii) oxidation
Author:
Affiliation:
1. Department of Biotechnology
2. Delft University of Technology
3. 2629 HZ Delft
4. The Netherlands
5. Max Planck Institute for Chemical Energy Conversion (MPI-CEC)
6. D-45470 Mülheim
7. Germany
Abstract
Spectroscopic studies of human H-type ferritin in comparison with an archaeal ferritin from Pyrococcus furiosus reveal how kinetics of a common mechanism of Fe(ii) oxidation is tuned differently in these two ferritins.
Funder
European Molecular Biology Organization
Publisher
Royal Society of Chemistry (RSC)
Subject
Molecular Biology,Biotechnology
Link
http://pubs.rsc.org/en/content/articlepdf/2016/MB/C6MB00235H
Reference57 articles.
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3. The ferritin superfamily: Supramolecular templates for materials synthesis
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5. Moving Fe2+ from ferritin ion channels to catalytic OH centers depends on conserved protein cage carboxylates
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