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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 1
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pubmed:dateCreated |
2002-5-3
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pubmed:abstractText |
Biomineralization of the ferritin iron core involves a complex series of events in which H(2)O(2) is produced during iron oxidation by O(2) 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 mu-1,2-peroxodiFe(III) intermediate (species P) with Mössbauer parameters delta (isomer shift)=0.58 mm/s and DeltaE(Q) (quadrupole splitting)=1.07 mm/s at 4.2 K is formed within 50 ms of mixing Fe(II) with the apoprotein. This intermediate accounts for almost all of the iron in the sample at 160 ms. It subsequently decays within 10 s to form a mu-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 10 min. The intermediate peroxodiFe(III) complex does not decay under O(2)-limiting conditions, an observation suggesting inhibition of decay by unreacted Fe(II), or a possible role for O(2) in ferritin biomineralization in addition to that of direct oxidation of iron(II).
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11988076-10220314,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11988076-10387019,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11988076-10441528,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11988076-10493786,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11988076-10615044,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11988076-10625425,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11988076-10769150,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11988076-10903139,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11988076-11535059,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11988076-1463463,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11988076-1764477,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11988076-1939058,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11988076-1992356,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11988076-2190093,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11988076-2669970,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11988076-2775718,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11988076-7578135,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11988076-7999768,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11988076-8224163,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11988076-8241182,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11988076-8255292,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11988076-8280069,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11988076-8430332,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11988076-8695634,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11988076-9003196,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/11988076-9657687,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11988076-9665690
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
364
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
57-63
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:11988076-Biochemical Phenomena,
pubmed-meshheading:11988076-Biochemistry,
pubmed-meshheading:11988076-Dimerization,
pubmed-meshheading:11988076-Ferritins,
pubmed-meshheading:11988076-Humans,
pubmed-meshheading:11988076-Hydrogen Peroxide,
pubmed-meshheading:11988076-Iron,
pubmed-meshheading:11988076-Models, Chemical,
pubmed-meshheading:11988076-Recombinant Proteins,
pubmed-meshheading:11988076-Spectrum Analysis,
pubmed-meshheading:11988076-Temperature,
pubmed-meshheading:11988076-Thermodynamics
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pubmed:year |
2002
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pubmed:articleTitle |
mu-1,2-Peroxobridged di-iron(III) dimer formation in human H-chain ferritin.
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pubmed:affiliation |
Department of Chemistry, University of New Hampshire, Durham, NH 03824, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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