Low-damage fabrication of high aspect nanocolumns by using neutral beams and ferritin-iron-core mask

2007 ◽  
Vol 25 (3) ◽  
pp. 760 ◽  
Author(s):  
Tomohiro Kubota ◽  
Tomohiro Baba ◽  
Suguru Saito ◽  
Satoshi Yamasaki ◽  
Shinya Kumagai ◽  
...  
Keyword(s):  
Iron Core ◽  
Neutral Beams ◽  
Ferritin Iron

A 7-nm nanocolumn structure fabricated by using a ferritin iron-core mask and low-energy Cl neutral beams

2004 ◽  
Vol 84 (9) ◽  
pp. 1555-1557 ◽  
Author(s):  
Tomohiro Kubota ◽  
Tomohiro Baba ◽  
Seiji Samukawa ◽  
Hiroyuki Kawashima ◽  
Yukiharu Uraoka ◽  
...  
Keyword(s):  
Low Energy ◽  
Iron Core ◽  
Neutral Beams ◽  
Ferritin Iron

THE FORMATION, STRUCTURE AND DISSOLUTION OF THE FERRITIN IRON CORE STUDIED BY X-RAY ABSORPTION SPECTROSCOPY

1986 ◽  
Vol 47 (C8) ◽  
pp. C8-1155-C8-1157
Author(s):  
E. C. THEIL ◽  
D. E. SAYERS ◽  
C. Y. YANG ◽  
A. FONTAINE ◽  
E. DARTYGE
Keyword(s):  
Absorption Spectroscopy ◽  
Iron Core ◽  
X Ray ◽  
Ferritin Iron ◽  
X Ray Absorption

scholarly journals μ-1,2-Peroxobridged di-iron(III) dimer formation in human H-chain ferritin

2002 ◽  
Vol 364 (1) ◽  
pp. 57-63 ◽  
Author(s):  
Fadi BOU-ABDALLAH ◽  
Georgia C. PAPAEFTHYMIOU ◽  
Danielle M. SCHESWOHL ◽  
Sean D. STANGA ◽  
Paolo AROSIO ◽  
...  
Keyword(s):  
Iron Oxidation ◽  
Iron Core ◽  
Intermediate Species ◽  
Direct Oxidation ◽  
Dimer Formation ◽  
Complex Species ◽  
Ferritin Iron ◽  
Human Ferritin ◽  
Mössbauer Parameters ◽  
Almost All

Biomineralization of the ferritin iron core involves a complex series of events in which H2O2 is produced during iron oxidation by O2 at a dinuclear centre, the ‘ferroxidase site’, located on the H-subunit of mammalian proteins. Rapid-freeze quench Mössbauer spectroscopy was used to probe the early events of iron oxidation and mineralization in recombinant human ferritin containing 24 H-subunits. The spectra reveal that a μ-1,2-peroxodiFe(III) intermediate (species P) with Mössbauer parameters δ (isomer shift) = 0.58mm/s and ΔEQ (quadrupole splitting) = 1.07mm/s at 4.2K is formed within 50ms of mixing Fe(II) with the apoprotein. This intermediate accounts for almost all of the iron in the sample at 160ms. It subsequently decays within 10s to form a μ-oxodiFe(III)—protein complex (species D), which partially vacates the ferroxidase sites of the protein to generate Fe(III) clusters (species C) at a reaction time of 10min. The intermediate peroxodiFe(III) complex does not decay under O2-limiting conditions, an observation suggesting inhibition of decay by unreacted Fe(II), or a possible role for O2 in ferritin biomineralization in addition to that of direct oxidation of iron(II).

A New Silicon Quantum-Well Structure with Controlled Diameter and Thickness Fabricated with Ferritin Iron Core Mask and Chlorine Neutral Beam Etching

2008 ◽  
Vol 1 ◽  
pp. 074002 ◽  
Author(s):  
Seiji Samukawa ◽  
Tomohiro Kubota ◽  
Chi-Hsien Huang ◽  
Takeshi Hashimoto ◽  
Makoto Igarashi ◽  
...  
Keyword(s):  
Quantum Well ◽  
Neutral Beam ◽  
Iron Core ◽  
Quantum Well Structure ◽  
Ferritin Iron ◽  
Neutral Beam Etching

Study of neutral-beam etching conditions for the fabrication of 7-nm-diameter nanocolumn structures using ferritin iron-core masks

2005 ◽  
Vol 23 (2) ◽  
pp. 534 ◽  
Author(s):  
Tomohiro Kubota ◽  
Tomohiro Baba ◽  
Hiroyuki Kawashima ◽  
Yukiharu Uraoka ◽  
Takashi Fuyuki ◽  
...  
Keyword(s):  
Neutral Beam ◽  
Iron Core ◽  
Ferritin Iron ◽  
Neutral Beam Etching

A comparison of an undecairon(III) complex with the ferritin iron core

1989 ◽  
Vol 36 (1) ◽  
pp. 51-62 ◽  
Author(s):  
Q.T. Islam ◽  
D.E. Sayers ◽  
E.C. Theil ◽  
S.M. Gorun
Keyword(s):  
Iron Core ◽  
Ferritin Iron

A new approach to the ferritin iron core growth: influence of the H/L ratio on the core shape

2012 ◽  
Vol 41 (4) ◽  
pp. 1320-1324 ◽  
Author(s):  
J. D. López-Castro ◽  
J. J. Delgado ◽  
J. A. Perez-Omil ◽  
Natividad Gálvez ◽  
Rafael Cuesta ◽  
...  
Keyword(s):  
Iron Core ◽  
New Approach ◽  
The Core ◽  
Ferritin Iron

scholarly journals Incorporation and release of inorganic phosphate in horse spleen ferritin

1978 ◽  
Vol 171 (2) ◽  
pp. 313-320 ◽  
Author(s):  
A Trefry ◽  
P M Harrison
Keyword(s):  
Inorganic Phosphate ◽  
Iron Core ◽  
Ferritin Iron ◽  
Horse Spleen Ferritin

When ferritin is reconstituted from Fe and apoferritin in vitro in the presence of Pi, the product obtained differs both from native ferritin and from ferritin reconstituted in the absence of Pi. When the latter is incubated with Pi the product resembles native ferritin with respect both to the pattern of Pi incorporated per molecule or per Fe atom and to the ease of release of this Pi relative to Fe release. It is concluded that much of the Pi of native ferritin is adsorbed on surfaces of ferritin iron-core crystallites. The results also suggest that Pi is not present at the intracellular site of Fe incorporation into ferritin, but is added after Fe.

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