Mossbauer studies of iron containing enzyme active sites and model complexes

含铁酶活性位点和模型复合物的穆斯鲍尔研究

基本信息

  • 批准号:
    0956779
  • 负责人:
  • 金额:
    $ 16.5万
  • 依托单位:
  • 依托单位国家:
    美国
  • 项目类别:
    Continuing Grant
  • 财政年份:
    2010
  • 资助国家:
    美国
  • 起止时间:
    2010-06-01 至 2014-05-31
  • 项目状态:
    已结题

项目摘要

This award in the Chemistry of Life Processes (CLP) program, co-funded with the Division of Molecular and Cellular Biosciences (MCB), supports work by Professor Codrina V. Popescu at Ursinus College, an undergraduate liberal arts institution. The proposed Mössbauer investigations include studies of iron complexes and the exploration of novel iron sites in proteins. Mössbauer spectroscopy provides insight into the electronic structure and bonding situation of iron compounds by probing the iron nucleus. Iron is the most abundant transition metal found in biological systems, being involved in a variety of physiological processes carried out by enzymes and transport proteins. Thus, to understand biological processes at a molecular level, one must elucidate the electronic structure of iron coordination complexes. The study of metalloproteins has seen a great development due to the enticing prospect of using design elements inspired by Nature in manmade catalysts for cleaning out pollutants through catalytic oxidation, or cheaply obtaining hydrogen to be used as a fuel. This fundamental research seeks to accomplish two types of results. First, large families of iron compounds could be systematically characterized, a broad study useful in establishing correlations between structural and spectroscopic changes in these molecules. A second, more challenging endeavor, is the resolution of spectroscopic problems by analyzing a set of spectra for a single compound under carefully chosen conditions. A picture of the electronic structure of a given compound can then be generated from the spectral parameters. The long-term goals of this research are the elucidation of structure and mechanism of hydrogenases and certain oxygenases, which have direct applications in fuel and pollution control technologies. For example, the enzymes hydrogenases catalyze the production and breakdown of molecular hydrogen. If understood well, these enzymes may offer a cheaper, non-polluting way, to obtain hydrogen fuel. This type of research has a significant impact in the chemical and biological sciences, given that it provides answers to fundamental structural questions, such as structure and bonding, and uncovers their profound implications on the function of the active sites in question.In terms of broader impacts, the proposed research supports a close mentor-student relationship, in which students are part of the scientific pursuit from hypothesis generation to interpretation of results. The expected impacts on undergraduate training and education include: (1) to develop and maintain an undergraduate research program that fosters student growth and independence through cultivation of logic and problem-solving skills; (2) to provide students with interdisciplinary projects that promote learning spectroscopy hands-on while solving current scientific problems; (3) to provide the resources for external presentations and publications.
该奖项为生命过程化学(CLP)项目,与分子和细胞生物科学系(MCB)共同资助,支持乌尔辛斯学院Codrina V.Popescu教授的工作,乌尔辛斯学院是一所本科文科院校。拟议的穆斯堡尔研究包括对铁络合物的研究和对蛋白质中新的铁位置的探索。穆斯堡尔谱学通过探测铁核,提供了对铁化合物的电子结构和成键情况的洞察。铁是生物系统中含量最丰富的过渡金属,参与酶和转运蛋白进行的各种生理过程。因此,要在分子水平上理解生物过程,就必须阐明铁配位络合物的电子结构。金属蛋白的研究取得了很大的发展,这是因为在人造催化剂中利用受自然启发的设计元素通过催化氧化来清除污染物,或者廉价地获得氢作为燃料的前景。这项基础性研究寻求实现两种类型的结果。首先,可以系统地表征大家族的铁化合物,这是一项广泛的研究,有助于建立这些分子的结构变化和光谱变化之间的关联。第二个更具挑战性的努力是通过在精心选择的条件下分析一组单一化合物的光谱来解决光谱问题。然后,可以从光谱参数中生成给定化合物的电子结构的图像。这项研究的长期目标是阐明氢酶和某些加氧酶的结构和机制,它们在燃料和污染控制技术中具有直接应用。例如,氢酶催化分子氢的产生和分解。如果理解得很好,这些酶可能会提供一种更便宜、无污染的方式来获得氢燃料。这类研究在化学和生物科学中具有重大影响,因为它提供了基本结构问题的答案,如结构和成键,并揭示了它们对所讨论的活性部位功能的深刻影响。就更广泛的影响而言,拟议的研究支持一种密切的导师-学生关系,在这种关系中,学生是从假设生成到结果解释的科学追求的一部分。对本科生培训和教育的预期影响包括:(1)开发和维持一个本科生研究计划,通过培养逻辑和解决问题的能力来促进学生的成长和独立;(2)为学生提供跨学科项目,促进学生在解决当前科学问题的同时亲身实践学习光谱学;(3)为外部演示和出版物提供资源。

项目成果

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Codrina Popescu其他文献

Codrina Popescu的其他文献

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{{ truncateString('Codrina Popescu', 18)}}的其他基金

Collaborative Research:The ferric uptake regulator (Fur) regulates intracellular iron homeostasis via reversible binding of a [2Fe-2S] cluster in Escherichia coli
合作研究:铁摄取调节剂 (Fur) 通过与大肠杆菌中的 [2Fe-2S] 簇可逆结合来调节细胞内铁稳态
  • 批准号:
    2050045
  • 财政年份:
    2021
  • 资助金额:
    $ 16.5万
  • 项目类别:
    Standard Grant
RUI: Mossbauer Studies of Iron Containing Enzyme Active Sites and Model Complexes
RUI:含铁酶活性位点和模型复合物的穆斯堡尔研究
  • 批准号:
    1445959
  • 财政年份:
    2014
  • 资助金额:
    $ 16.5万
  • 项目类别:
    Standard Grant
RUI: Mossbauer Studies of Iron Containing Enzyme Active Sites and Model Complexes
RUI:含铁酶活性位点和模型复合物的穆斯堡尔研究
  • 批准号:
    1307650
  • 财政年份:
    2013
  • 资助金额:
    $ 16.5万
  • 项目类别:
    Standard Grant
Acquisition of a Mossbauer Spectrometer
购买穆斯堡尔光谱仪
  • 批准号:
    0421116
  • 财政年份:
    2004
  • 资助金额:
    $ 16.5万
  • 项目类别:
    Standard Grant

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RUI: Mossbauer Studies of Iron Containing Enzyme Active Sites and Model Complexes
RUI:含铁酶活性位点和模型复合物的穆斯堡尔研究
  • 批准号:
    1445959
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    2014
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    $ 16.5万
  • 项目类别:
    Standard Grant
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RUI:含铁酶活性位点和模型复合物的穆斯堡尔研究
  • 批准号:
    1307650
  • 财政年份:
    2013
  • 资助金额:
    $ 16.5万
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通过穆斯鲍尔光谱研究 O2 活化
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    3271260
  • 财政年份:
    1990
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    $ 16.5万
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Study of O2 Activation by Mossbauer Spectroscopy
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  • 批准号:
    7569976
  • 财政年份:
    1990
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  • 财政年份:
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