Source:http://linkedlifedata.com/resource/pubmed/id/20702403
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
42
|
pubmed:dateCreated |
2010-10-11
|
pubmed:abstractText |
Naturally occurring phytoferritin is a heteropolymer consisting of two different H-type subunits, H-1 and H-2. Prior to this study, however, the function of the two subunits in oxidative deposition of iron in ferritin was unknown. The data show that, upon aerobic addition of 48-200 Fe(2+)/shell to apoferritin, iron oxidation occurs only at the diiron ferroxidase center of recombinant H1 (rH-1). In addition to the diiron ferroxidase mechanism, such oxidation is catalyzed by the extension peptide (a specific domain found in phytoferritin) of rH-2, because the H-1 subunit is able to remove Fe(3+) from the center to the inner cavity better than the H-2 subunit. These findings support the idea that the H-1 and H-2 subunits play different roles in iron mineralization in protein. Interestingly, at medium iron loading (200 irons/shell), wild-type (WT) soybean seed ferritin (SSF) exhibits a stronger activity in catalyzing iron oxidation (1.10 ± 0.13 ?m iron/subunit/s) than rH-1 (0.59 ± 0.07 ?m iron/subunit/s) and rH-2 (0.48 ± 0.04 ?m iron/subunit/s), demonstrating that a synergistic interaction exists between the H-1 and H-2 subunits in SSF during iron mineralization. Such synergistic interaction becomes considerably stronger at high iron loading (400 irons/shell) as indicated by the observation that the iron oxidation activity of WT SSF is ?10 times larger than those of rH-1 and rH-2. This helps elucidate the widespread occurrence of heteropolymeric ferritins in plants.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Oct
|
pubmed:issn |
1083-351X
|
pubmed:author | |
pubmed:issnType |
Electronic
|
pubmed:day |
15
|
pubmed:volume |
285
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
32075-86
|
pubmed:dateRevised |
2011-10-17
|
pubmed:meshHeading |
pubmed-meshheading:20702403-Amino Acid Sequence,
pubmed-meshheading:20702403-Animals,
pubmed-meshheading:20702403-Ferritins,
pubmed-meshheading:20702403-Iron,
pubmed-meshheading:20702403-Molecular Sequence Data,
pubmed-meshheading:20702403-Oxidation-Reduction,
pubmed-meshheading:20702403-Protein Subunits,
pubmed-meshheading:20702403-Soybeans,
pubmed-meshheading:20702403-Spectrometry, Mass, Matrix-Assisted Laser...
|
pubmed:year |
2010
|
pubmed:articleTitle |
Role of H-1 and H-2 subunits of soybean seed ferritin in oxidative deposition of iron in protein.
|
pubmed:affiliation |
CAU and ACC Joint Laboratory of Space Food, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|