A diatom ferritin optimized for iron oxidation but not iron storage

Pfaffen, Stephanie, Bradley, Justin, Abdulqadir, Raz, Firme, Marlo R., Moore, Geoff, Le Brun, Nick ORCID: https://orcid.org/0000-0001-9780-4061 and Murphy, Michael (2015) A diatom ferritin optimized for iron oxidation but not iron storage. The Journal of Biological Chemistry, 290. pp. 28416-28427. ISSN 1083-351X

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Abstract

Ferritin from the marine pennate diatom Pseudo-nitzschia multiseries (PmFTN) plays a key role in sustaining growth in iron-limited ocean environments. The di-iron catalytic ferroxidase center of PmFTN (sites A and B) has a nearby third iron site (site C) in an arrangement typically observed in prokaryotic ferritins. Here we demonstrate that Glu44, a site C ligand, and Glu130, a residue that bridges iron bound at sites B and C, limit the rate of post-oxidation reorganization of iron coordination and the rate at which Fe3+ exits the ferroxidase center for storage within the mineral core. The latter, in particular, severely limits the overall rate of iron mineralization. Thus, the diatom ferritin is optimized for initial Fe2+ oxidation but not for mineralization, pointing to a role for this protein in buffering iron availability and facilitating iron-sparing rather than only long-term iron storage.

Item Type:	Article
Uncontrolled Keywords:	sdg 14 - life below water ,/dk/atira/pure/sustainabledevelopmentgoals/life_below_water
Faculty \ School:	Faculty of Science > School of Chemistry (former - to 2024)
UEA Research Groups:	Faculty of Science > Research Groups > Biophysical Chemistry (former - to 2017) Faculty of Science > Research Groups > Centre for Ocean and Atmospheric Sciences Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry Faculty of Science > Research Groups > Chemistry of Life Processes
Depositing User:	Pure Connector
Date Deposited:	01 Dec 2015 07:27
Last Modified:	24 Sep 2024 11:24
URI:	https://ueaeprints.uea.ac.uk/id/eprint/55534
DOI:	10.1074/jbc.M115.669713

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