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Title: The Ferritin Protein Nanocage and Biomineral, from Single Fe Atoms to FeO Nanoparticles: Starting with EXAFS

Abstract

Ferritins are protein nanocages that use iron and oxygen chemistry to concentrate iron and trap dioxygen or hydrogen peroxide in biominerals of hydrated ferric oxides, 5-8 nm in diameter, inside the cages. The proteins are found in nature from archea to humans. Protein catalytic sites are embedded in the protein cage and initiate mineralization by oxido-reduction of ferrous ions and dioxygen or hydrogen peroxide to couple two iron ions through a peroxo bridge, followed by decay to diferric oxo/hydroxyl mineral precursors; ferritin protein subdomains that fold/unfold independently of the protein cage control recovery of ferrous ions from the mineral. Early EXAFS (1978) was extremely useful in defining the ferritin mineral. More recent use of rapid freeze quench (RFQ) EXAFS spectroscopies, coupled with RFQ Moessbauer, Resonance Raman and rapid mixing UV-vis spectroscopy, have identified and characterized unusual ferritin protein catalytic intermediates and mineral precursors. EXAFS spectroscopy can play an important role in the future understanding of protein catalysis in metalloproteins such as ferritin, ribonucleotide reductase and methane monooxygenases. Needed are instrumentation improvements that will provide rapid-scan fluorescence spectra with high signal/noise ratios.

Authors:
 [1];  [2]
  1. Children's Hospital Oakland Research Institute (CHORI), 5700 Martin Luther King Jr. Way, Oakland, CA 94609 (United States)
  2. (United States)
Publication Date:
OSTI Identifier:
21054581
Resource Type:
Journal Article
Resource Relation:
Journal Name: AIP Conference Proceedings; Journal Volume: 882; Journal Issue: 1; Conference: XAFS13: 13. international conference on X-ray absorption fine structure, Stanford, CA (United States), 9-14 Jul 2006; Other Information: DOI: 10.1063/1.2644422; (c) 2007 American Institute of Physics; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
36 MATERIALS SCIENCE; ABSORPTION SPECTROSCOPY; ATOMS; CATALYSIS; FERRITIN; FINE STRUCTURE; FLUORESCENCE SPECTROSCOPY; HYDROGEN PEROXIDE; HYDROXIDES; IRON; IRON IONS; IRON OXIDES; MINERALIZATION; MINERALS; NANOSTRUCTURES; OXIDATION; OXYGEN; REDUCTION; SIGNAL-TO-NOISE RATIO; TRAPS; X-RAY SPECTROSCOPY

Citation Formats

Theil, Elizabeth C., and Department of Nutritional Science and Toxicology, University of California, Berkeley, CA 94720. The Ferritin Protein Nanocage and Biomineral, from Single Fe Atoms to FeO Nanoparticles: Starting with EXAFS. United States: N. p., 2007. Web. doi:10.1063/1.2644422.
Theil, Elizabeth C., & Department of Nutritional Science and Toxicology, University of California, Berkeley, CA 94720. The Ferritin Protein Nanocage and Biomineral, from Single Fe Atoms to FeO Nanoparticles: Starting with EXAFS. United States. doi:10.1063/1.2644422.
Theil, Elizabeth C., and Department of Nutritional Science and Toxicology, University of California, Berkeley, CA 94720. Fri . "The Ferritin Protein Nanocage and Biomineral, from Single Fe Atoms to FeO Nanoparticles: Starting with EXAFS". United States. doi:10.1063/1.2644422.
@article{osti_21054581,
title = {The Ferritin Protein Nanocage and Biomineral, from Single Fe Atoms to FeO Nanoparticles: Starting with EXAFS},
author = {Theil, Elizabeth C. and Department of Nutritional Science and Toxicology, University of California, Berkeley, CA 94720},
abstractNote = {Ferritins are protein nanocages that use iron and oxygen chemistry to concentrate iron and trap dioxygen or hydrogen peroxide in biominerals of hydrated ferric oxides, 5-8 nm in diameter, inside the cages. The proteins are found in nature from archea to humans. Protein catalytic sites are embedded in the protein cage and initiate mineralization by oxido-reduction of ferrous ions and dioxygen or hydrogen peroxide to couple two iron ions through a peroxo bridge, followed by decay to diferric oxo/hydroxyl mineral precursors; ferritin protein subdomains that fold/unfold independently of the protein cage control recovery of ferrous ions from the mineral. Early EXAFS (1978) was extremely useful in defining the ferritin mineral. More recent use of rapid freeze quench (RFQ) EXAFS spectroscopies, coupled with RFQ Moessbauer, Resonance Raman and rapid mixing UV-vis spectroscopy, have identified and characterized unusual ferritin protein catalytic intermediates and mineral precursors. EXAFS spectroscopy can play an important role in the future understanding of protein catalysis in metalloproteins such as ferritin, ribonucleotide reductase and methane monooxygenases. Needed are instrumentation improvements that will provide rapid-scan fluorescence spectra with high signal/noise ratios.},
doi = {10.1063/1.2644422},
journal = {AIP Conference Proceedings},
number = 1,
volume = 882,
place = {United States},
year = {Fri Feb 02 00:00:00 EST 2007},
month = {Fri Feb 02 00:00:00 EST 2007}
}