ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2015
Fe(2+) substrate transport through ferritin protein cage ion channels influences enzyme activity and biomineralization.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 42 citations in OpenAlex.
- Impact of the three-fold channel substitution D131N on kinetics of translocation of FeDalton transactions (Cambridge, England : 2003) · 2026Article
- Perls' Prussian blue staining and chemistry of Prussian blue and Turnbull blue.Forensic science international. Synergy · 2025Review
- The Mechanism of Mineral Nucleation and Growth in a Mini-Ferritin.Journal of the American Chemical Society · 2025Article
- Genome-wide identification and expression analysis of the ferritin family in sweetpotato and its two diploid relatives.BMC plant biology · 2025Article
- Observation of the Assembly of the Nascent Mineral Core at the Nucleation Site of Human Mitochondrial Ferritin.Journal of the American Chemical Society · 2025Article
- Structural and Functional Insights into the Roles of Potential Metal-Binding Sites inPolymers · 2022Article
- How can sodium-glucose cotransporter 2 inhibitors stimulate erythrocytosis in patients who are iron-deficient? Implications for understanding iron homeostasis in heart failure.European journal of heart failure · 2022Review
- Ferritin: A Promising Nanoreactor and Nanocarrier for Bionanotechnology.ACS bio & med chem Au · 2022Review
- Design of a gold clustering site in an engineered apo-ferritin cage.Communications chemistry · 2022Article
- Crystallographic characterization of a marine invertebrate ferritin from the sea cucumber Apostichopus japonicus.FEBS open bio · 2022Article
- Structural Insights Into the Effects of Interactions With Iron and Copper Ions on Ferritin From the Blood ClamFrontiers in molecular biosciences · 2022Article
- Flavin-mediated reductive iron mobilization from frog M and Mycobacterial ferritins: impact of their size, charge and reactivities with NADH/OJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2021Article
- Cryo-EM structures and functional characterization of homo- and heteropolymers of human ferritin variants.Scientific reports · 2020Article
- Dissecting the structural and functional roles of a putative metal entry site in encapsulated ferritins.The Journal of biological chemistry · 2020Article
- Electrostatic and Structural Bases of Fe2+ Translocation through Ferritin Channels.The Journal of biological chemistry · 2016Article
- Self-assembly is prerequisite for catalysis of Fe(II) oxidation by catalytically active subunits of ferritin.The Journal of biological chemistry · 2015Article
- Genome-wide comparison of ferritin family from Archaea, Bacteria, Eukarya, and Viruses: its distribution, characteristic motif, and phylogenetic relationship.Die Naturwissenschaften · 2015Article
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6 authors at 3 institutions in 2 countries.
Funding
Abstract
Ferritins, complex protein nanocages, form internal iron-oxy minerals (Fe2O3·H2O), by moving cytoplasmic Fe(2+) through intracage ion channels to cage-embedded enzyme (2Fe(2+)/O2 oxidoreductase) sites where ferritin biomineralization is initiated. The products of ferritin enzyme activity are diferric oxy complexes that are mineral precursors. Conserved, carboxylate amino acid side chains of D127 from each of three cage subunits project into ferritin ion channels near the interior ion channel exits and, thus, could direct Fe(2+) movement to the internal enzyme sites. Ferritin D127E was designed and analyzed to probe properties of ion channel size and carboxylate crowding near the internal ion channel opening. Glu side chains are chemically equivalent to, but longer by one -CH2 than Asp, side chains. Ferritin D127E assembled into normal protein cages, but diferric peroxo formation (enzyme activity) was not observed, when measured at 650 nm (DFP λ max). The caged biomineral formation, measured at 350 nm in the middle of the broad, nonspecific Fe(3+)-O absorption band, was slower. Structural differences (protein X-ray crystallography), between ion channels in wild type and ferritin D127E, which correlate with the inhibition of ferritin D127E enzyme activity include: (1) narrower interior ion channel openings/pores; (2) increased numbers of ion channel protein-metal binding sites, and (3) a change in ion channel electrostatics due to carboxylate crowding. The contributions of ion channel size and structure to ferritin activity reflect metal ion transport in ion channels are precisely regulated both in ferritin protein nanocages and membranes of living cells.
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