MECHANISM OF FERRITIN FERROXIDATION AND MINERALIZATION
铁蛋白铁氧化和矿化机制
基本信息
- 批准号:6138700
- 负责人:
- 金额:$ 17.96万
- 依托单位:
- 依托单位国家:美国
- 项目类别:
- 财政年份:1999
- 资助国家:美国
- 起止时间:1999-01-01 至 2002-12-31
- 项目状态:已结题
- 来源:
- 关键词:
项目摘要
Iron is an important nutrient, required in almost every aspect of
cellular function. However, at physiological pH and under oxidizing
condition, it is not very soluble. How living organisms sequester iron
for cellular utilization is therefore a fundamental question of vital
importance. Also, in the presence Of 02, free Fe2+ ions are extremely
toxic, capable of generating hydrogen peroxide, superoxide, and other
reactive oxygen species that can attack and destroy important cellular
molecules. Ferritin is unique in the sense that it performs dual
functions of iron detoxification, by oxidizing the Fe2+ ions in
solution, and iron sequestration, by storing the oxidized Fe3+ ions in
its inner protein cavity in the form of ferrihydrite mineral. However,
despite the importance of ferritin functions and decades of research
efforts, the mechanism by which ferritin catalyzes the Fe2+ oxidation
(ferroxidation) and directs the oxidized products to form the mineral
core (mineralization) is still poorly understood. This is partly due
to the complexity of the ferritin molecule and partly due to the fact
that the methods used in previous studies were either indirect or lacked
the required spectroscopic resolution to monitor the complex reaction
catalyzed by ferritin. In this application, we propose to employ
Mssbauer spectroscopy in conjunction with the rapid freeze-rapid
quench kinetic technique to investigate the mechanism of ferritin
ferroxidation and mineralization. Three different recombinant
ferritins, the frog H and M ferritins, and the E. coli bacterioferritin,
are to be examined. Results obtained from our preliminary studies
demonstrate that this combined kinetic/spectroscopic approach provides
the necessary time resolution for obtaining kinetic information and the
required spectroscopic resolution for distinguishing, quantifying and
characterizing the multiple Fe species generated during the
ferroxidation and mineralization processes. Other complementary
spectroscopies, such as EPR, ENDOR, EXAFS, and resonance Raman will also
be employed to obtain further structural information on these reaction
intermediates. Site-specific mutants will be engineered, produced and
subjected to kinetic/spectroscopic investigations for the purpose of
defining the ferroxidase site, the Fe transport pathways, and the
functional roles of certain key residues. A series of double-mixing
rapid freeze-quench Mossbauer investigations using 57Fe and 56Fe
isotopes are particularly designed to address questions concerning the
dynamics of the ferritin function. Detailed mechanistic insights into
the processes involved in ferritin ferroxidase reaction and mineral core
formation are expected to emerge from these proposed studies.
铁是一种重要的营养物质,几乎人体的各个方面都需要铁
项目成果
期刊论文数量(0)
专著数量(0)
科研奖励数量(0)
会议论文数量(0)
专利数量(0)
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Boi-Hanh V. Huynh其他文献
Boi-Hanh V. Huynh的其他文献
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{{ truncateString('Boi-Hanh V. Huynh', 18)}}的其他基金
MECHANISM OF FERRITIN FERROXIDATION AND MINERALIZATION
铁蛋白铁氧化和矿化机制
- 批准号:
2739253 - 财政年份:1999
- 资助金额:
$ 17.96万 - 项目类别:
MECHANISM OF FERRITIN FERROXIDATION AND MINERALIZATION
铁蛋白铁氧化和矿化机制
- 批准号:
6343059 - 财政年份:1999
- 资助金额:
$ 17.96万 - 项目类别:
MECHANISM OF FERRITIN FERROXIDATION AND MINERALIZATION
铁蛋白铁氧化和矿化机制
- 批准号:
6490265 - 财政年份:1999
- 资助金额:
$ 17.96万 - 项目类别:
Biosynthesis and Novel Functions of Fe-S Clusters
Fe-S团簇的生物合成和新功能
- 批准号:
6325357 - 财政年份:1992
- 资助金额:
$ 17.96万 - 项目类别:
NOVEL REDOX PROTEINS FROM SULFATE REDUCING BACT
来自硫酸盐还原菌的新型氧化还原蛋白
- 批准号:
3306756 - 财政年份:1992
- 资助金额:
$ 17.96万 - 项目类别:
NOVEL REDOX PROTEINS FROM SULFATE REDUCING BACT
来自硫酸盐还原菌的新型氧化还原蛋白
- 批准号:
3306758 - 财政年份:1992
- 资助金额:
$ 17.96万 - 项目类别:
Biosynthesis and Novel Function of Fe-S clusters
Fe-S团簇的生物合成和新功能
- 批准号:
6918157 - 财政年份:1992
- 资助金额:
$ 17.96万 - 项目类别:
Biosynthesis and Novel Function of Fe-S clusters
Fe-S团簇的生物合成和新功能
- 批准号:
7217335 - 财政年份:1992
- 资助金额:
$ 17.96万 - 项目类别:
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