MOSSBAUER STUDIES OF THE ULTRAFINE ANTIFERROMAGNETIC CORES OF FERRITIN

被引：7

作者：

HAWKINS, C ^{[1
]}

WILLIAMS, JM ^{[1
]}

HUDSON, AJ ^{[1
]}

ANDREWS, SC ^{[1
]}

TREFFRY, A ^{[1
]}

机构：

[1] UNIV SHEFFIELD,DEPT MOLEC BIOL & BIOTECHNOL,SHEFFIELD,S YORKSHIRE,ENGLAND

来源：

HYPERFINE INTERACTIONS | 1994年 / 91卷 / 1-4期

关键词：

D O I：

10.1007/BF02064614

中图分类号：

O64 [物理化学（理论化学）、化学物理学]; O56 [分子物理学、原子物理学];

学科分类号：

070203 ; 070304 ; 081704 ; 1406 ;

摘要：

The ultrafine iron cores found within the iron-storage protein ferritin are of interest to both the molecular biologist and physicist. The manner in which the protein shell (apoferritin) takes up, releases and sequesters iron is of great biological importance. Also, due to their nano-size(less than or equal to 8 nm), the magnetically ordered cores are singly domained. Such particles possess interesting magnetic relaxation and dynamic properties for which Mossbauer spectroscopy is an ideal analytic tool. Horse ferritin molecules iron-loaded artificially contain ferrihydrite-like cores which behave as superparamagnets due to their nano-size. An anomalous decrease in the f-factor occurs above the blocking temperature of the superparamagnetic particles. This has been attributed to a magnetostriction effect resulting from superparamagnetic switching.

引用

页码：827 / 833

页数：7

共 13 条

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