Biosynthesis and Novel Functions of Fe-S Clusters
Fe-S团簇的生物合成和新功能
基本信息
- 批准号:6325357
- 负责人:
- 金额:$ 19.02万
- 依托单位:
- 依托单位国家:美国
- 项目类别:
- 财政年份:1992
- 资助国家:美国
- 起止时间:1992-09-30 至 2005-03-31
- 项目状态:已结题
- 来源:
- 关键词:Escherichia coli Mossbauer spectrometry bacterial proteins cofactor electron nuclear double resonance spectroscopy electron spin resonance spectroscopy enzyme activity ferritin ferroxidase iron sulfur protein metal complex methane monooxygenase oxidation reduction reaction oxygen protein biosynthesis protein structure function ribonucleotide reductase stop flow technique
项目摘要
DESCRIPTION: (provided by applicant) Fe-S proteins are a group of functionally
diverse proteins that contain prosthetic groups composed of Fe and inorganic
sulfur of various structures, termed Fe-S clusters. In addition to the
well-established role of electron transport, Fe-S proteins are involved in a
diverse range of non-redox processes including sensing and regulatory
functions. In this application, we propose to employ a combined
spectroscopic/rapid-kinetic approach to investigate the biosynthesis of Fe-S
clusters and to study the newly discovered functional role of Fe-S cluster in
stabilizing radical intermediates. It has been established that a pair of the
nitrogen fixation gene products, NifU and NifS, are essential for the assembly
of the Fe-S clusters for the nitrogenase enzyme system. Homologs of NifS and
NifU, termed IscS and IscU, respectively, are found in a wide spectrum of
living organisms ranging from bacteria to human, and thus, have been proposed
to be involved in the general assembly/repair of Fe-S clusters in biology.
Here, experiments are proposed to investigate the mechanism of Fe-S
biosynthesis and to establish the roles play by NifU/NifS and IscU/IscS in this
important biological process. For the purpose of enhancing our understanding of
Fe-S cluster functions, three functionally diverse proteins were chosen for the
proposed studies: pyruvate formate-lyase activating enzyme (PFL-AE),
ferredoxin: thioredoxin reductase (FTR) and biotin synthase. PFL-AE activates
pyruvate formate lyase (PFL) by catalyzing the generation of a glycyl radical
in PFL. FTR catalyzes the reductive cleavage of disulfide groups in
thioredoxins for enzyme activations, and biotin synthase converts dethiobiotin
to biotin. Evidence accumulated so far suggests that all three enzymes employ a
4Fe-4S cluster-mediated site-specific u(3)-S(2-) based chemistry for their
respective functions. The proposed study is designed to evaluate the validity
of this suggestion and to determine the detailed mechanistic steps involved in
the catalytic cycles. The methods of choice for the proposed studies are
Mossbauer and EPR spectroscopies, which are particularly suited for the study
of Fe-containing proteins. Rapid freeze-quench kinetic techniques will be used
to trap reaction intermediates for spectroscopic characterization and for
kinetic investigations. Whenever possible, other complementary techniques, such
as resonance Raman, ENDOR, and EXAFS will be used to obtain further structural
information on the reaction intermediates. Site-specific variants will be
engineered, produced and subjected to similar kinetic/spectroscopic
investigations for the purpose of defining the functional roles of specific
residues. Detailed mechanistic insights at a molecular level are expected to
emerge from the proposed investigations.
描述:(由申请人提供)Fe-S蛋白是一组功能
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:
$ 19.02万 - 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:
$ 19.02万 - 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:
$ 19.02万 - 项目类别:
MECHANISM OF FERRITIN FERROXIDATION AND MINERALIZATION
铁蛋白铁氧化和矿化机制
- 批准号:
6138700 - 财政年份:1999
- 资助金额:
$ 19.02万 - 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:
$ 19.02万 - 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:
$ 19.02万 - 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:
$ 19.02万 - 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:
$ 19.02万 - 项目类别:
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Grant-in-Aid for Scientific Research (C)














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