NDLI: Opening protein pores with chaotropes enhances Fe reduction and chelation of Fe from the ferritin biomineral

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Opening protein pores with chaotropes enhances Fe reduction and chelation of Fe from the ferritin biomineral

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Opening protein pores with chaotropes enhances Fe reduction and chelation of Fe from the ferritin biomineral

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Jin, Weili Theil, Elizabeth C. Liu, Xiaofeng
Description	Author Affiliation: Liu X ( Children's Hospital of Oakland Research Institute, 5700 Martin Luther King, Jr. Way, Oakland, CA 94609, USA.);
Abstract	Iron is concentrated in ferritin, a spherical protein with a capacious cavity for ferric nanominerals of <4,500 Fe atoms. Global ferritin structure is very stable, resisting 6 M urea and heat (85 degrees C) at neutral pH. Eight pores, each formed by six helices from 3 of the 24 polypeptide subunits, restrict mineral access to reductant, protons, or chelators. Protein-directed transport of Fe and aqueous Fe(3+) chemistry (solubility approximately 10(-18) M) drive mineralization. Ferritin pores are 'gated' based on protein crystals and Fe chelation rates of wild-type (WT) and engineered proteins. Pore structure and gate residues, which are highly conserved, thus should be sensitive to environmental changes such as low concentrations of chaotropes. We now demonstrate that urea or guanidine (1-10 mM), far below concentrations for global unfolding, induced multiphasic rate increases in Fe(2+)-bipyridyl formation similar to conservative substitutions of pore residues. Urea (1 M) or the nonconservative LeuPro substitution that fully unfolded pores without urea both induced monophasic rate increases in Fe(2+) chelation rates, indicating unrestricted access between mineral and reductantchelator. The observation of low-melting ferritin subdomains by CD spectroscopy (melting midpoint 53 degrees C), accounting for 10% of ferritin alpha-helices, is unprecedented. The low-melting ferritin subdomains are pores, based on percentage helix and destabilization by either very dilute urea solutions (1 mM) or LeuPro substitution, which both increased Fe(2+) chelation. Biological molecules may have evolved to control gating of ferritin pores in response to cell iron need and, if mimicked by designer drugs, could impact chelation therapies in iron-overload diseases.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	7
Volume Number	100
Language	English
Publisher	National Academy of Sciences
Publisher Date	2003-04-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Ferritins Chemistry Metabolism Animals Chelating Agents Models, Molecular Oxidation-Reduction Protein Conformation Protein Subunits Ranidae Recombinant Proteins Thermodynamics Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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